메뉴 건너뛰기




Volumn 7, Issue MAR, 2016, Pages

Action and traction: Cytoskeletal control of receptor triggering at the immunological synapse

Author keywords

Actin; Adhesion; Costimulation; Cytoskeleton; Immunological synapse; Integrin; Mechanotransduction; T cell receptor

Indexed keywords

CD28 ANTIGEN; CYTOSKELETON PROTEIN; F ACTIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; MYOSIN ADENOSINE TRIPHOSPHATASE; PATTERN RECOGNITION RECEPTOR; T LYMPHOCYTE RECEPTOR;

EID: 84964669635     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2016.00068     Document Type: Review
Times cited : (91)

References (267)
  • 1
    • 33746011209 scopus 로고    scopus 로고
    • T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster
    • Varma R, Campi G, Yokosuka T, Saito T, Dustin ML. T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. Immunity (2006) 25(1):117-27. doi:10.1016/j.immuni.2006.04.010
    • (2006) Immunity , vol.25 , Issue.1 , pp. 117-127
    • Varma, R.1    Campi, G.2    Yokosuka, T.3    Saito, T.4    Dustin, M.L.5
  • 2
    • 84863992208 scopus 로고    scopus 로고
    • F-actin polymerization and retrograde flow drive sustained PLCgamma1 signaling during T cell activation
    • Babich A, Li S, O'Connor RS, Milone MC, Freedman BD, Burkhardt JK. F-actin polymerization and retrograde flow drive sustained PLCgamma1 signaling during T cell activation. J Cell Biol (2012) 197(6):775-87. doi:10.1083/jcb.201201018
    • (2012) J Cell Biol , vol.197 , Issue.6 , pp. 775-787
    • Babich, A.1    Li, S.2    O'Connor, R.S.3    Milone, M.C.4    Freedman, B.D.5    Burkhardt, J.K.6
  • 3
    • 84885347038 scopus 로고    scopus 로고
    • Mechanical regulation of T-cell functions
    • Chen W, Zhu C. Mechanical regulation of T-cell functions. Immunol Rev (2013) 256(1):160-76. doi:10.1111/imr.12122
    • (2013) Immunol Rev , vol.256 , Issue.1 , pp. 160-176
    • Chen, W.1    Zhu, C.2
  • 4
    • 84863229197 scopus 로고    scopus 로고
    • Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells
    • Yi J, Wu XS, Crites T, Hammer JA III. Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells. Mol Biol Cell (2012) 23(5):834-52. doi:10.1091/mbc.E11-08-0731
    • (2012) Mol Biol Cell , vol.23 , Issue.5 , pp. 834-852
    • Yi, J.1    Wu, X.S.2    Crites, T.3    Hammer, J.A.4
  • 5
    • 67349114397 scopus 로고    scopus 로고
    • T cell antigen receptor signaling and immunological synapse stability require myosin IIA
    • Ilani T, Vasiliver-Shamis G, Vardhana S, Bretscher A, Dustin ML. T cell antigen receptor signaling and immunological synapse stability require myosin IIA. Nat Immunol (2009) 10(5):531-9. doi:10.1038/ni.1723
    • (2009) Nat Immunol , vol.10 , Issue.5 , pp. 531-539
    • Ilani, T.1    Vasiliver-Shamis, G.2    Vardhana, S.3    Bretscher, A.4    Dustin, M.L.5
  • 6
    • 84881450224 scopus 로고    scopus 로고
    • Ratiometric imaging of the T-cell actin cytoskeleton reveals the nature of receptor-induced cytoskeletal enrichment
    • Smoligovets AA, Smith AW, Groves JT. Ratiometric imaging of the T-cell actin cytoskeleton reveals the nature of receptor-induced cytoskeletal enrichment. Biophys J (2013) 105(3):L11-3. doi:10.1016/j.bpj.2013.06.031
    • (2013) Biophys J , vol.105 , Issue.3 , pp. L11-L13
    • Smoligovets, A.A.1    Smith, A.W.2    Groves, J.T.3
  • 7
    • 84964694672 scopus 로고    scopus 로고
    • Actin foci facilitate activation of the phospholipase C-gamma in primary T lymphocytes via the WASP pathway
    • Kumari S, Depoil D, Martinelli R, Judokusumo E, Carmona G, Gertler FB, et al. Actin foci facilitate activation of the phospholipase C-gamma in primary T lymphocytes via the WASP pathway. Elife (2015) 4. doi:10.7554/eLife.04953
    • (2015) Elife , vol.4
    • Kumari, S.1    Depoil, D.2    Martinelli, R.3    Judokusumo, E.4    Carmona, G.5    Gertler, F.B.6
  • 8
    • 84860333171 scopus 로고    scopus 로고
    • Antigen recognition is facilitated by invadosome-like protrusions formed by memory/effector T cells
    • Sage PT, Varghese LM, Martinelli R, Sciuto TE, Kamei M, Dvorak AM, et al. Antigen recognition is facilitated by invadosome-like protrusions formed by memory/effector T cells. J Immunol (2012) 188(8):3686-99. doi:10.4049/jimmunol.1102594
    • (2012) J Immunol , vol.188 , Issue.8 , pp. 3686-3699
    • Sage, P.T.1    Varghese, L.M.2    Martinelli, R.3    Sciuto, T.E.4    Kamei, M.5    Dvorak, A.M.6
  • 10
    • 33846626054 scopus 로고    scopus 로고
    • Regulation of T-cell activation by the cytoskeleton
    • Billadeau DD, Nolz JC, Gomez TS. Regulation of T-cell activation by the cytoskeleton. Nat Rev Immunol (2007) 7(2):131-43. doi:10.1038/nri2021
    • (2007) Nat Rev Immunol , vol.7 , Issue.2 , pp. 131-143
    • Billadeau, D.D.1    Nolz, J.C.2    Gomez, T.S.3
  • 11
    • 42649127027 scopus 로고    scopus 로고
    • The actin cytoskeleton in T cell activation
    • Burkhardt JK, Carrizosa E, Shaffer MH. The actin cytoskeleton in T cell activation. Annu Rev Immunol (2008) 26:233-59. doi:10.1146/annurev.immunol.26.021607.090347
    • (2008) Annu Rev Immunol , vol.26 , pp. 233-259
    • Burkhardt, J.K.1    Carrizosa, E.2    Shaffer, M.H.3
  • 12
    • 84892165063 scopus 로고    scopus 로고
    • T cell antigen receptor activation and actin cytoskeleton remodeling
    • Kumari S, Curado S, Mayya V, Dustin ML. T cell antigen receptor activation and actin cytoskeleton remodeling. Biochim Biophys Acta (2014) 1838(2):546-56. doi:10.1016/j.bbamem.2013.05.004
    • (2014) Biochim Biophys Acta , vol.1838 , Issue.2 , pp. 546-556
    • Kumari, S.1    Curado, S.2    Mayya, V.3    Dustin, M.L.4
  • 13
    • 70350370714 scopus 로고    scopus 로고
    • SWAP-70-like adapter of T cells: a novel Lck-regulated guanine nucleotide exchange factor coordinating actin cytoskeleton reorganization and Ca2+ signaling in T cells
    • Becart S, Altman A. SWAP-70-like adapter of T cells: a novel Lck-regulated guanine nucleotide exchange factor coordinating actin cytoskeleton reorganization and Ca2+ signaling in T cells. Immunol Rev (2009) 232(1):319-33. doi:10.1111/j.1600-065X.2009.00839.x
    • (2009) Immunol Rev , vol.232 , Issue.1 , pp. 319-333
    • Becart, S.1    Altman, A.2
  • 14
    • 0035254857 scopus 로고    scopus 로고
    • A PAK1-PIX-PKL complex is activated by the T-cell receptor independent of Nck, Slp-76 and LAT
    • Ku GM, Yablonski D, Manser E, Lim L, Weiss A. A PAK1-PIX-PKL complex is activated by the T-cell receptor independent of Nck, Slp-76 and LAT. EMBO J (2001) 20(3):457-65. doi:10.1093/emboj/20.3.457
    • (2001) EMBO J , vol.20 , Issue.3 , pp. 457-465
    • Ku, G.M.1    Yablonski, D.2    Manser, E.3    Lim, L.4    Weiss, A.5
  • 15
    • 44349127316 scopus 로고    scopus 로고
    • AlphaPIX Rho GTPase guanine nucleotide exchange factor regulates lymphocyte functions and antigen receptor signaling
    • Missy K, Hu B, Schilling K, Harenberg A, Sakk V, Kuchenbecker K, et al. AlphaPIX Rho GTPase guanine nucleotide exchange factor regulates lymphocyte functions and antigen receptor signaling. Mol Cell Biol (2008) 28(11):3776-89. doi:10.1128/MCB.00507-07
    • (2008) Mol Cell Biol , vol.28 , Issue.11 , pp. 3776-3789
    • Missy, K.1    Hu, B.2    Schilling, K.3    Harenberg, A.4    Sakk, V.5    Kuchenbecker, K.6
  • 16
    • 33744981370 scopus 로고    scopus 로고
    • HS1 functions as an essential actin-regulatory adaptor protein at the immune synapse
    • Gomez TS, McCarney SD, Carrizosa E, Labno CM, Comiskey EO, Nolz JC, et al. HS1 functions as an essential actin-regulatory adaptor protein at the immune synapse. Immunity (2006) 24(6):741-52. doi:10.1016/j.immuni.2006.03.022
    • (2006) Immunity , vol.24 , Issue.6 , pp. 741-752
    • Gomez, T.S.1    McCarney, S.D.2    Carrizosa, E.3    Labno, C.M.4    Comiskey, E.O.5    Nolz, J.C.6
  • 17
    • 30044446991 scopus 로고    scopus 로고
    • The WAVE2 complex regulates actin cytoskeletal reorganization and CRAC-mediated calcium entry during T cell activation
    • Nolz JC, Gomez TS, Zhu P, Li S, Medeiros RB, Shimizu Y, et al. The WAVE2 complex regulates actin cytoskeletal reorganization and CRAC-mediated calcium entry during T cell activation. Curr Biol (2006) 16(1):24-34. doi:10.1016/j.cub.2005.11.036
    • (2006) Curr Biol , vol.16 , Issue.1 , pp. 24-34
    • Nolz, J.C.1    Gomez, T.S.2    Zhu, P.3    Li, S.4    Medeiros, R.B.5    Shimizu, Y.6
  • 18
    • 0033230229 scopus 로고    scopus 로고
    • Antigen receptor-induced activation and cytoskeletal rearrangement are impaired in Wiskott-Aldrich syndrome protein-deficient lymphocytes
    • Zhang J, Shehabeldin A, da Cruz LA, Butler J, Somani AK, McGavin M, et al. Antigen receptor-induced activation and cytoskeletal rearrangement are impaired in Wiskott-Aldrich syndrome protein-deficient lymphocytes. J Exp Med (1999) 190(9):1329-42. doi:10.1084/jem.190.9.1329
    • (1999) J Exp Med , vol.190 , Issue.9 , pp. 1329-1342
    • Zhang, J.1    Shehabeldin, A.2    da Cruz, L.A.3    Butler, J.4    Somani, A.K.5    McGavin, M.6
  • 19
    • 84918527460 scopus 로고    scopus 로고
    • WASp family verprolin-homologous protein-2 (WAVE2) and Wiskott-Aldrich syndrome protein (WASp) engage in distinct downstream signaling interactions at the T cell antigen receptor site
    • Pauker MH, Reicher B, Joseph N, Wortzel I, Jakubowicz S, Noy E, et al. WASp family verprolin-homologous protein-2 (WAVE2) and Wiskott-Aldrich syndrome protein (WASp) engage in distinct downstream signaling interactions at the T cell antigen receptor site. J Biol Chem (2014) 289(50):34503-19. doi:10.1074/jbc.M114.591685
    • (2014) J Biol Chem , vol.289 , Issue.50 , pp. 34503-34519
    • Pauker, M.H.1    Reicher, B.2    Joseph, N.3    Wortzel, I.4    Jakubowicz, S.5    Noy, E.6
  • 20
    • 3242762840 scopus 로고    scopus 로고
    • Differential roles for Wiskott-Aldrich syndrome protein in immune synapse formation and IL-2 production
    • Cannon JL, Burkhardt JK. Differential roles for Wiskott-Aldrich syndrome protein in immune synapse formation and IL-2 production. J Immunol (2004) 173(3):1658-62. doi:10.4049/jimmunol.173.3.1658
    • (2004) J Immunol , vol.173 , Issue.3 , pp. 1658-1662
    • Cannon, J.L.1    Burkhardt, J.K.2
  • 21
    • 70450236976 scopus 로고    scopus 로고
    • Regulation of podosome dynamics by WASp phosphorylation: implication in matrix degradation and chemotaxis in macrophages
    • Dovas A, Gevrey JC, Grossi A, Park H, Abou-Kheir W, Cox D. Regulation of podosome dynamics by WASp phosphorylation: implication in matrix degradation and chemotaxis in macrophages. J Cell Sci (2009) 122(Pt 21):3873-82. doi:10.1242/jcs.051755
    • (2009) J Cell Sci , vol.122 , pp. 3873-3882
    • Dovas, A.1    Gevrey, J.C.2    Grossi, A.3    Park, H.4    Abou-Kheir, W.5    Cox, D.6
  • 22
    • 79955007763 scopus 로고    scopus 로고
    • Hematopoietic lineage cell-specific protein 1 functions in concert with the Wiskott-Aldrich syndrome protein to promote podosome array organization and chemotaxis in dendritic cells
    • Dehring DA, Clarke F, Ricart BG, Huang Y, Gomez TS, Williamson EK, et al. Hematopoietic lineage cell-specific protein 1 functions in concert with the Wiskott-Aldrich syndrome protein to promote podosome array organization and chemotaxis in dendritic cells. J Immunol (2011) 186(8):4805-18. doi:10.4049/jimmunol.1003102
    • (2011) J Immunol , vol.186 , Issue.8 , pp. 4805-4818
    • Dehring, D.A.1    Clarke, F.2    Ricart, B.G.3    Huang, Y.4    Gomez, T.S.5    Williamson, E.K.6
  • 23
    • 0036696174 scopus 로고    scopus 로고
    • The immunological synapse: integrins take the stage
    • Sims TN, Dustin ML. The immunological synapse: integrins take the stage. Immunol Rev (2002) 186:100-17. doi:10.1034/j.1600-065X.2002.18610.x
    • (2002) Immunol Rev , vol.186 , pp. 100-117
    • Sims, T.N.1    Dustin, M.L.2
  • 24
    • 0242708766 scopus 로고    scopus 로고
    • Leukocyte functional antigen 1 lowers T cell activation thresholds and signaling through cytohesin-1 and Jun-activating binding protein 1
    • Perez OD, Mitchell D, Jager GC, South S, Murriel C, McBride J, et al. Leukocyte functional antigen 1 lowers T cell activation thresholds and signaling through cytohesin-1 and Jun-activating binding protein 1. Nat Immunol (2003) 4(11):1083-92. doi:10.1038/ni984
    • (2003) Nat Immunol , vol.4 , Issue.11 , pp. 1083-1092
    • Perez, O.D.1    Mitchell, D.2    Jager, G.C.3    South, S.4    Murriel, C.5    McBride, J.6
  • 25
    • 68949085309 scopus 로고    scopus 로고
    • LFA-1 regulates CD8+ T cell activation via T cell receptor-mediated and LFA-1-mediated Erk1/2 signal pathways
    • Li D, Molldrem JJ, Ma Q. LFA-1 regulates CD8+ T cell activation via T cell receptor-mediated and LFA-1-mediated Erk1/2 signal pathways. J Biol Chem (2009) 284(31):21001-10. doi:10.1074/jbc.M109.002865
    • (2009) J Biol Chem , vol.284 , Issue.31 , pp. 21001-21010
    • Li, D.1    Molldrem, J.J.2    Ma, Q.3
  • 26
    • 0032587163 scopus 로고    scopus 로고
    • Beta2-integrin, LFA-1, and TCR/CD3 synergistically induce tyrosine phosphorylation of focal adhesion kinase (pp125(FAK)) in PHA-activated T cells
    • Tabassam FH, Umehara H, Huang JY, Gouda S, Kono T, Okazaki T, et al. Beta2-integrin, LFA-1, and TCR/CD3 synergistically induce tyrosine phosphorylation of focal adhesion kinase (pp125(FAK)) in PHA-activated T cells. Cell Immunol (1999) 193(2):179-84. doi:10.1006/cimm.1999.1472
    • (1999) Cell Immunol , vol.193 , Issue.2 , pp. 179-184
    • Tabassam, F.H.1    Umehara, H.2    Huang, J.Y.3    Gouda, S.4    Kono, T.5    Okazaki, T.6
  • 27
    • 70350437964 scopus 로고    scopus 로고
    • The adapter protein SLP-76 mediates "outside-in" integrin signaling and function in T cells
    • Baker RG, Hsu CJ, Lee D, Jordan MS, Maltzman JS, Hammer DA, et al. The adapter protein SLP-76 mediates "outside-in" integrin signaling and function in T cells. Mol Cell Biol (2009) 29(20):5578-89. doi:10.1128/MCB.00283-09
    • (2009) Mol Cell Biol , vol.29 , Issue.20 , pp. 5578-5589
    • Baker, R.G.1    Hsu, C.J.2    Lee, D.3    Jordan, M.S.4    Maltzman, J.S.5    Hammer, D.A.6
  • 28
    • 33846031421 scopus 로고    scopus 로고
    • The actin cloud induced by LFA-1-mediated outside-in signals lowers the threshold for T-cell activation
    • Suzuki J, Yamasaki S, Wu J, Koretzky GA, Saito T. The actin cloud induced by LFA-1-mediated outside-in signals lowers the threshold for T-cell activation. Blood (2007) 109(1):168-75. doi:10.1182/blood-2005-12-020164
    • (2007) Blood , vol.109 , Issue.1 , pp. 168-175
    • Suzuki, J.1    Yamasaki, S.2    Wu, J.3    Koretzky, G.A.4    Saito, T.5
  • 29
    • 68149153184 scopus 로고    scopus 로고
    • SLP-76-ADAP adaptor module regulates LFA-1 mediated costimulation and T cell motility
    • Wang H, Wei B, Bismuth G, Rudd CE. SLP-76-ADAP adaptor module regulates LFA-1 mediated costimulation and T cell motility. Proc Natl Acad Sci U S A (2009) 106(30):12436-41. doi:10.1073/pnas.0900510106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.30 , pp. 12436-12441
    • Wang, H.1    Wei, B.2    Bismuth, G.3    Rudd, C.E.4
  • 30
    • 11144355979 scopus 로고    scopus 로고
    • Signaling through the leukocyte integrin LFA-1 in T cells induces a transient activation of Rac-1 that is regulated by Vav and PI3K/Akt-1
    • Sanchez-Martin L, Sanchez-Sanchez N, Gutierrez-Lopez MD, Rojo AI, Vicente-Manzanares M, Perez-Alvarez MJ, et al. Signaling through the leukocyte integrin LFA-1 in T cells induces a transient activation of Rac-1 that is regulated by Vav and PI3K/Akt-1. J Biol Chem (2004) 279(16):16194-205. doi:10.1074/jbc.M400905200
    • (2004) J Biol Chem , vol.279 , Issue.16 , pp. 16194-16205
    • Sanchez-Martin, L.1    Sanchez-Sanchez, N.2    Gutierrez-Lopez, M.D.3    Rojo, A.I.4    Vicente-Manzanares, M.5    Perez-Alvarez, M.J.6
  • 31
    • 33847765059 scopus 로고    scopus 로고
    • Phosphorylation of the LFA-1 integrin beta2-chain on Thr-758 leads to adhesion, Rac-1/Cdc42 activation, and stimulation of CD69 expression in human T cells
    • Nurmi SM, Autero M, Raunio AK, Gahmberg CG, Fagerholm SC. Phosphorylation of the LFA-1 integrin beta2-chain on Thr-758 leads to adhesion, Rac-1/Cdc42 activation, and stimulation of CD69 expression in human T cells. J Biol Chem (2007) 282(2):968-75. doi:10.1074/jbc.M608524200
    • (2007) J Biol Chem , vol.282 , Issue.2 , pp. 968-975
    • Nurmi, S.M.1    Autero, M.2    Raunio, A.K.3    Gahmberg, C.G.4    Fagerholm, S.C.5
  • 32
    • 77956535011 scopus 로고    scopus 로고
    • Elucidation of the integrin LFA-1-mediated signaling pathway of actin polarization in natural killer cells
    • Mace EM, Zhang J, Siminovitch KA, Takei F. Elucidation of the integrin LFA-1-mediated signaling pathway of actin polarization in natural killer cells. Blood (2010) 116(8):1272-9. doi:10.1182/blood-2009-12-261487
    • (2010) Blood , vol.116 , Issue.8 , pp. 1272-1279
    • Mace, E.M.1    Zhang, J.2    Siminovitch, K.A.3    Takei, F.4
  • 33
    • 0037049555 scopus 로고    scopus 로고
    • Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion
    • DeMali KA, Barlow CA, Burridge K. Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J Cell Biol (2002) 159(5):881-91. doi:10.1083/jcb.200206043
    • (2002) J Cell Biol , vol.159 , Issue.5 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 34
    • 84899885606 scopus 로고    scopus 로고
    • Regulation of focal adhesion formation by a vinculin-Arp2/3 hybrid complex
    • Chorev DS, Moscovitz O, Geiger B, Sharon M. Regulation of focal adhesion formation by a vinculin-Arp2/3 hybrid complex. Nat Commun (2014) 5:3758. doi:10.1038/ncomms4758
    • (2014) Nat Commun , vol.5 , pp. 3758
    • Chorev, D.S.1    Moscovitz, O.2    Geiger, B.3    Sharon, M.4
  • 35
    • 44649191160 scopus 로고    scopus 로고
    • T cell costimulation via the integrin VLA-4 inhibits the actin-dependent centralization of signaling microclusters containing the adaptor SLP-76
    • Nguyen K, Sylvain NR, Bunnell SC. T cell costimulation via the integrin VLA-4 inhibits the actin-dependent centralization of signaling microclusters containing the adaptor SLP-76. Immunity (2008) 28(6):810-21. doi:10.1016/j.immuni.2008.04.019
    • (2008) Immunity , vol.28 , Issue.6 , pp. 810-821
    • Nguyen, K.1    Sylvain, N.R.2    Bunnell, S.C.3
  • 36
    • 84880642716 scopus 로고    scopus 로고
    • Vinculin-actin interaction couples actin retrograde flow to focal adhesions, but is dispensable for focal adhesion growth
    • Thievessen I, Thompson PM, Berlemont S, Plevock KM, Plotnikov SV, Zemljic-Harpf A, et al. Vinculin-actin interaction couples actin retrograde flow to focal adhesions, but is dispensable for focal adhesion growth. J Cell Biol (2013) 202(1):163-77. doi:10.1083/jcb.201303129
    • (2013) J Cell Biol , vol.202 , Issue.1 , pp. 163-177
    • Thievessen, I.1    Thompson, P.M.2    Berlemont, S.3    Plevock, K.M.4    Plotnikov, S.V.5    Zemljic-Harpf, A.6
  • 37
    • 0031022715 scopus 로고    scopus 로고
    • Accessory molecule and costimulation requirements for CD4 T cell response
    • Croft M, Dubey C. Accessory molecule and costimulation requirements for CD4 T cell response. Crit Rev Immunol (1997) 17(1):89-118. doi:10.1615/CritRevImmunol.v17.i1.40
    • (1997) Crit Rev Immunol , vol.17 , Issue.1 , pp. 89-118
    • Croft, M.1    Dubey, C.2
  • 39
    • 84870545526 scopus 로고    scopus 로고
    • PKC-theta-mediated signal delivery from the TCR/CD28 surface receptors
    • Isakov N, Altman A. PKC-theta-mediated signal delivery from the TCR/CD28 surface receptors. Front Immunol (2012) 3:273. doi:10.3389/fimmu.2012.00273
    • (2012) Front Immunol , vol.3 , pp. 273
    • Isakov, N.1    Altman, A.2
  • 40
    • 84875463042 scopus 로고    scopus 로고
    • Molecular mechanisms of T cell co-stimulation and co-inhibition
    • Chen L, Flies DB. Molecular mechanisms of T cell co-stimulation and co-inhibition. Nat Rev Immunol (2013) 13(4):227-42. doi:10.1038/nri3405
    • (2013) Nat Rev Immunol , vol.13 , Issue.4 , pp. 227-242
    • Chen, L.1    Flies, D.B.2
  • 41
    • 65349184024 scopus 로고    scopus 로고
    • Dynamic regulation of T-cell costimulation through TCR-CD28 microclusters
    • Yokosuka T, Saito T. Dynamic regulation of T-cell costimulation through TCR-CD28 microclusters. Immunol Rev (2009) 229(1):27-40. doi:10.1111/j.1600-065X.2009.00779.x
    • (2009) Immunol Rev , vol.229 , Issue.1 , pp. 27-40
    • Yokosuka, T.1    Saito, T.2
  • 42
    • 0037902616 scopus 로고    scopus 로고
    • Independent CD28 signaling via VAV and SLP-76: a model for in trans costimulation
    • Rudd CE, Raab M. Independent CD28 signaling via VAV and SLP-76: a model for in trans costimulation. Immunol Rev (2003) 192:32-41. doi:10.1034/j.1600-065X.2003.00005.x
    • (2003) Immunol Rev , vol.192 , pp. 32-41
    • Rudd, C.E.1    Raab, M.2
  • 43
    • 0035690584 scopus 로고    scopus 로고
    • CD28 signaling via VAV/SLP-76 adaptors: regulation of cytokine transcription independent of TCR ligation
    • Raab M, Pfister S, Rudd CE. CD28 signaling via VAV/SLP-76 adaptors: regulation of cytokine transcription independent of TCR ligation. Immunity (2001) 15(6):921-33. doi:10.1016/S1074-7613(01)00248-5
    • (2001) Immunity , vol.15 , Issue.6 , pp. 921-933
    • Raab, M.1    Pfister, S.2    Rudd, C.E.3
  • 44
    • 33846526236 scopus 로고    scopus 로고
    • Mitogenic CD28 signals require the exchange factor Vav1 to enhance TCR signaling at the SLP-76-Vav-Itk signalosome
    • Dennehy KM, Elias F, Na SY, Fischer KD, Hunig T, Luhder F. Mitogenic CD28 signals require the exchange factor Vav1 to enhance TCR signaling at the SLP-76-Vav-Itk signalosome. J Immunol (2007) 178(3):1363-71. doi:10.4049/jimmunol.178.3.1363
    • (2007) J Immunol , vol.178 , Issue.3 , pp. 1363-1371
    • Dennehy, K.M.1    Elias, F.2    Na, S.Y.3    Fischer, K.D.4    Hunig, T.5    Luhder, F.6
  • 45
    • 84892719664 scopus 로고    scopus 로고
    • Inhibition of the kinase Csk in thymocytes reveals a requirement for actin remodeling in the initiation of full TCR signaling
    • Tan YX, Manz BN, Freedman TS, Zhang C, Shokat KM, Weiss A. Inhibition of the kinase Csk in thymocytes reveals a requirement for actin remodeling in the initiation of full TCR signaling. Nat Immunol (2014) 15(2):186-94. doi:10.1038/ni.2772
    • (2014) Nat Immunol , vol.15 , Issue.2 , pp. 186-194
    • Tan, Y.X.1    Manz, B.N.2    Freedman, T.S.3    Zhang, C.4    Shokat, K.M.5    Weiss, A.6
  • 46
    • 0041929574 scopus 로고    scopus 로고
    • CD28 engagement promotes actin polymerization through the activation of the small Rho GTPase Cdc42 in human T cells
    • Salazar-Fontana LI, Barr V, Samelson LE, Bierer BE. CD28 engagement promotes actin polymerization through the activation of the small Rho GTPase Cdc42 in human T cells. J Immunol (2003) 171(5):2225-32. doi:10.4049/jimmunol.171.5.2225
    • (2003) J Immunol , vol.171 , Issue.5 , pp. 2225-2232
    • Salazar-Fontana, L.I.1    Barr, V.2    Samelson, L.E.3    Bierer, B.E.4
  • 47
    • 84899472242 scopus 로고    scopus 로고
    • NKG2D-and CD28-mediated costimulation regulate CD8+ T cell chemotaxis through different mechanisms: the role of Cdc42/N-WASp
    • Serrano-Pertierra E, Cernuda-Morollon E, Lopez-Larrea C. NKG2D-and CD28-mediated costimulation regulate CD8+ T cell chemotaxis through different mechanisms: the role of Cdc42/N-WASp. J Leukoc Biol (2014) 95(3):487-95. doi:10.1189/jlb.0613316
    • (2014) J Leukoc Biol , vol.95 , Issue.3 , pp. 487-495
    • Serrano-Pertierra, E.1    Cernuda-Morollon, E.2    Lopez-Larrea, C.3
  • 48
    • 33646167587 scopus 로고    scopus 로고
    • Stimulation of actin polymerization by filament severing
    • Carlsson AE. Stimulation of actin polymerization by filament severing. Biophys J (2006) 90(2):413-22. doi:10.1529/biophysj.105.069765
    • (2006) Biophys J , vol.90 , Issue.2 , pp. 413-422
    • Carlsson, A.E.1
  • 49
    • 84880830434 scopus 로고    scopus 로고
    • The lymphoid lineage-specific actin-uncapping protein Rltpr is essential for costimulation via CD28 and the development of regulatory T cells
    • Liang Y, Cucchetti M, Roncagalli R, Yokosuka T, Malzac A, Bertosio E, et al. The lymphoid lineage-specific actin-uncapping protein Rltpr is essential for costimulation via CD28 and the development of regulatory T cells. Nat Immunol (2013) 14(8):858-66. doi:10.1038/ni.2634
    • (2013) Nat Immunol , vol.14 , Issue.8 , pp. 858-866
    • Liang, Y.1    Cucchetti, M.2    Roncagalli, R.3    Yokosuka, T.4    Malzac, A.5    Bertosio, E.6
  • 50
    • 0033571386 scopus 로고    scopus 로고
    • CD2 sets quantitative thresholds in T cell activation
    • Bachmann MF, Barner M, Kopf M. CD2 sets quantitative thresholds in T cell activation. J Exp Med (1999) 190(10):1383-92. doi:10.1084/jem.190.10.1383
    • (1999) J Exp Med , vol.190 , Issue.10 , pp. 1383-1392
    • Bachmann, M.F.1    Barner, M.2    Kopf, M.3
  • 51
    • 65649098764 scopus 로고    scopus 로고
    • The coreceptor CD2 uses plasma membrane microdomains to transduce signals in T cells
    • Kaizuka Y, Douglass AD, Vardhana S, Dustin ML, Vale RD. The coreceptor CD2 uses plasma membrane microdomains to transduce signals in T cells. J Cell Biol (2009) 185(3):521-34. doi:10.1083/jcb.200809136
    • (2009) J Cell Biol , vol.185 , Issue.3 , pp. 521-534
    • Kaizuka, Y.1    Douglass, A.D.2    Vardhana, S.3    Dustin, M.L.4    Vale, R.D.5
  • 52
    • 0037590956 scopus 로고    scopus 로고
    • Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85
    • Hutchings NJ, Clarkson N, Chalkley R, Barclay AN, Brown MH. Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85. J Biol Chem (2003) 278(25):22396-403. doi:10.1074/jbc.M302540200
    • (2003) J Biol Chem , vol.278 , Issue.25 , pp. 22396-22403
    • Hutchings, N.J.1    Clarkson, N.2    Chalkley, R.3    Barclay, A.N.4    Brown, M.H.5
  • 53
    • 0037341006 scopus 로고    scopus 로고
    • CD2BP3, CIN85 and the structurally related adaptor protein CMS bind to the same CD2 cytoplasmic segment, but elicit divergent functional activities
    • Tibaldi EV, Reinherz EL. CD2BP3, CIN85 and the structurally related adaptor protein CMS bind to the same CD2 cytoplasmic segment, but elicit divergent functional activities. Int Immunol (2003) 15(3):313-29. doi:10.1093/intimm/dxg032
    • (2003) Int Immunol , vol.15 , Issue.3 , pp. 313-329
    • Tibaldi, E.V.1    Reinherz, E.L.2
  • 54
    • 84871902136 scopus 로고    scopus 로고
    • CD2AP links cortactin and capping protein at the cell periphery to facilitate formation of lamellipodia
    • Zhao J, Bruck S, Cemerski S, Zhang L, Butler B, Dani A, et al. CD2AP links cortactin and capping protein at the cell periphery to facilitate formation of lamellipodia. Mol Cell Biol (2013) 33(1):38-47. doi:10.1128/MCB.00734-12
    • (2013) Mol Cell Biol , vol.33 , Issue.1 , pp. 38-47
    • Zhao, J.1    Bruck, S.2    Cemerski, S.3    Zhang, L.4    Butler, B.5    Dani, A.6
  • 55
    • 0037241232 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse
    • Badour K, Zhang J, Shi F, McGavin MK, Rampersad V, Hardy LA, et al. The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse. Immunity (2003) 18(1):141-54. doi:10.1016/S1074-7613(02)00516-2
    • (2003) Immunity , vol.18 , Issue.1 , pp. 141-154
    • Badour, K.1    Zhang, J.2    Shi, F.3    McGavin, M.K.4    Rampersad, V.5    Hardy, L.A.6
  • 56
    • 0032991649 scopus 로고    scopus 로고
    • CMS: an adapter molecule involved in cytoskeletal rearrangements
    • Kirsch KH, Georgescu MM, Ishimaru S, Hanafusa H. CMS: an adapter molecule involved in cytoskeletal rearrangements. Proc Natl Acad Sci U S A (1999) 96(11):6211-6. doi:10.1073/pnas.96.11.6211
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.11 , pp. 6211-6216
    • Kirsch, K.H.1    Georgescu, M.M.2    Ishimaru, S.3    Hanafusa, H.4
  • 57
    • 76949108167 scopus 로고    scopus 로고
    • The membrane skeleton controls diffusion dynamics and signaling through the B cell receptor
    • Treanor B, Depoil D, Gonzalez-Granja A, Barral P, Weber M, Dushek O, et al. The membrane skeleton controls diffusion dynamics and signaling through the B cell receptor. Immunity (2010) 32(2):187-99. doi:10.1016/j.immuni.2009.12.005
    • (2010) Immunity , vol.32 , Issue.2 , pp. 187-199
    • Treanor, B.1    Depoil, D.2    Gonzalez-Granja, A.3    Barral, P.4    Weber, M.5    Dushek, O.6
  • 58
    • 80053132781 scopus 로고    scopus 로고
    • Increased sensitivity of antigen-experienced T cells through the enrichment of oligomeric T cell receptor complexes
    • Kumar R, Ferez M, Swamy M, Arechaga I, Rejas MT, Valpuesta JM, et al. Increased sensitivity of antigen-experienced T cells through the enrichment of oligomeric T cell receptor complexes. Immunity (2011) 35(3):375-87. doi:10.1016/j.immuni.2011.08.010
    • (2011) Immunity , vol.35 , Issue.3 , pp. 375-387
    • Kumar, R.1    Ferez, M.2    Swamy, M.3    Arechaga, I.4    Rejas, M.T.5    Valpuesta, J.M.6
  • 59
    • 74049157769 scopus 로고    scopus 로고
    • TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation
    • Lillemeier BF, Mortelmaier MA, Forstner MB, Huppa JB, Groves JT, Davis MM. TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation. Nat Immunol (2010) 11(1):90-6. doi:10.1038/ni.1832
    • (2010) Nat Immunol , vol.11 , Issue.1 , pp. 90-96
    • Lillemeier, B.F.1    Mortelmaier, M.A.2    Forstner, M.B.3    Huppa, J.B.4    Groves, J.T.5    Davis, M.M.6
  • 60
    • 81955164142 scopus 로고    scopus 로고
    • Functional nanoscale organization of signaling molecules downstream of the T cell antigen receptor
    • Sherman E, Barr V, Manley S, Patterson G, Balagopalan L, Akpan I, et al. Functional nanoscale organization of signaling molecules downstream of the T cell antigen receptor. Immunity (2011) 35(5):705-20. doi:10.1016/j.immuni.2011.10.004
    • (2011) Immunity , vol.35 , Issue.5 , pp. 705-720
    • Sherman, E.1    Barr, V.2    Manley, S.3    Patterson, G.4    Balagopalan, L.5    Akpan, I.6
  • 61
    • 79956106702 scopus 로고    scopus 로고
    • Dynamic cortical actin remodeling by ERM proteins controls BCR microcluster organization and integrity
    • Treanor B, Depoil D, Bruckbauer A, Batista FD. Dynamic cortical actin remodeling by ERM proteins controls BCR microcluster organization and integrity. J Exp Med (2011) 208(5):1055-68. doi:10.1084/jem.20101125
    • (2011) J Exp Med , vol.208 , Issue.5 , pp. 1055-1068
    • Treanor, B.1    Depoil, D.2    Bruckbauer, A.3    Batista, F.D.4
  • 63
    • 43049085527 scopus 로고    scopus 로고
    • Rapid leukocyte migration by integrin-independent flowing and squeezing
    • Lammermann T, Bader BL, Monkley SJ, Worbs T, Wedlich-Soldner R, Hirsch K, et al. Rapid leukocyte migration by integrin-independent flowing and squeezing. Nature (2008) 453(7191):51-5. doi:10.1038/nature06887
    • (2008) Nature , vol.453 , Issue.7191 , pp. 51-55
    • Lammermann, T.1    Bader, B.L.2    Monkley, S.J.3    Worbs, T.4    Wedlich-Soldner, R.5    Hirsch, K.6
  • 64
    • 38749134480 scopus 로고    scopus 로고
    • Nonmuscle myosin heavy chain IIA mediates integrin LFA-1 de-adhesion during T lymphocyte migration
    • Morin NA, Oakes PW, Hyun YM, Lee D, Chin YE, King MR, et al. Nonmuscle myosin heavy chain IIA mediates integrin LFA-1 de-adhesion during T lymphocyte migration. J Exp Med (2008) 205(1):195-205. doi:10.1084/jem.20071543
    • (2008) J Exp Med , vol.205 , Issue.1 , pp. 195-205
    • Morin, N.A.1    Oakes, P.W.2    Hyun, Y.M.3    Lee, D.4    Chin, Y.E.5    King, M.R.6
  • 65
    • 67349256860 scopus 로고    scopus 로고
    • Bringing up the rear: defining the roles of the uropod
    • Sanchez-Madrid F, Serrador JM. Bringing up the rear: defining the roles of the uropod. Nat Rev Mol Cell Biol (2009) 10(5):353-9. doi:10.1038/nrm2680
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.5 , pp. 353-359
    • Sanchez-Madrid, F.1    Serrador, J.M.2
  • 66
    • 77957272682 scopus 로고    scopus 로고
    • Modular design of immunological synapses and kinapses
    • Dustin ML. Modular design of immunological synapses and kinapses. Cold Spring Harbor Perspect Biol (2009) 1(1):a002873. doi:10.1101/cshperspect.a002873
    • (2009) Cold Spring Harbor Perspect Biol , vol.1 , Issue.1
    • Dustin, M.L.1
  • 67
    • 55849090253 scopus 로고    scopus 로고
    • Hunter to gatherer and back: immunological synapses and kinapses as variations on the theme of amoeboid locomotion
    • Dustin ML. Hunter to gatherer and back: immunological synapses and kinapses as variations on the theme of amoeboid locomotion. Annu Rev Cell Dev Biol (2008) 24:577-96. doi:10.1146/annurev.cellbio.24.110707.175226
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 577-596
    • Dustin, M.L.1
  • 68
    • 34249013684 scopus 로고    scopus 로고
    • Opposing effects of PKCtheta and WASp on symmetry breaking and relocation of the immunological synapse
    • Sims TN, Soos TJ, Xenias HS, Dubin-Thaler B, Hofman JM, Waite JC, et al. Opposing effects of PKCtheta and WASp on symmetry breaking and relocation of the immunological synapse. Cell (2007) 129(4):773-85. doi:10.1016/j.cell.2007.03.037
    • (2007) Cell , vol.129 , Issue.4 , pp. 773-785
    • Sims, T.N.1    Soos, T.J.2    Xenias, H.S.3    Dubin-Thaler, B.4    Hofman, J.M.5    Waite, J.C.6
  • 69
    • 34547135943 scopus 로고    scopus 로고
    • Peptide-MHC potency governs dynamic interactions between T cells and dendritic cells in lymph nodes
    • Skokos D, Shakhar G, Varma R, Waite JC, Cameron TO, Lindquist RL, et al. Peptide-MHC potency governs dynamic interactions between T cells and dendritic cells in lymph nodes. Nat Immunol (2007) 8(8):835-44. doi:10.1038/ni1490
    • (2007) Nat Immunol , vol.8 , Issue.8 , pp. 835-844
    • Skokos, D.1    Shakhar, G.2    Varma, R.3    Waite, J.C.4    Cameron, T.O.5    Lindquist, R.L.6
  • 70
    • 13944266418 scopus 로고    scopus 로고
    • Calcium oscillations regulate thymocyte motility during positive selection in the three-dimensional thymic environment
    • Bhakta NR, Oh DY, Lewis RS. Calcium oscillations regulate thymocyte motility during positive selection in the three-dimensional thymic environment. Nat Immunol (2005) 6(2):143-51. doi:10.1038/ni1161
    • (2005) Nat Immunol , vol.6 , Issue.2 , pp. 143-151
    • Bhakta, N.R.1    Oh, D.Y.2    Lewis, R.S.3
  • 71
    • 34548658855 scopus 로고    scopus 로고
    • Ca2+ signals in CD4+ T cells during early contacts with antigen-bearing dendritic cells in lymph node
    • Wei SH, Safrina O, Yu Y, Garrod KR, Cahalan MD, Parker I. Ca2+ signals in CD4+ T cells during early contacts with antigen-bearing dendritic cells in lymph node. J Immunol (2007) 179(3):1586-94. doi:10.4049/jimmunol.179.3.1586
    • (2007) J Immunol , vol.179 , Issue.3 , pp. 1586-1594
    • Wei, S.H.1    Safrina, O.2    Yu, Y.3    Garrod, K.R.4    Cahalan, M.D.5    Parker, I.6
  • 72
    • 27544441784 scopus 로고    scopus 로고
    • Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling
    • Campi G, Varma R, Dustin ML. Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling. J Exp Med (2005) 202(8):1031-6. doi:10.1084/jem.20051182
    • (2005) J Exp Med , vol.202 , Issue.8 , pp. 1031-1036
    • Campi, G.1    Varma, R.2    Dustin, M.L.3
  • 73
    • 79959332816 scopus 로고    scopus 로고
    • Dynein-driven transport of T cell receptor microclusters regulates immune synapse formation and T cell activation
    • Hashimoto-Tane A, Yokosuka T, Sakata-Sogawa K, Sakuma M, Ishihara C, Tokunaga M, et al. Dynein-driven transport of T cell receptor microclusters regulates immune synapse formation and T cell activation. Immunity (2011) 34(6):919-31. doi:10.1016/j.immuni.2011.05.012
    • (2011) Immunity , vol.34 , Issue.6 , pp. 919-931
    • Hashimoto-Tane, A.1    Yokosuka, T.2    Sakata-Sogawa, K.3    Sakuma, M.4    Ishihara, C.5    Tokunaga, M.6
  • 74
    • 84863262312 scopus 로고    scopus 로고
    • Characterization of dynamic actin associations with T-cell receptor microclusters in primary T cells
    • Smoligovets AA, Smith AW, Wu HJ, Petit RS, Groves JT. Characterization of dynamic actin associations with T-cell receptor microclusters in primary T cells. J Cell Sci (2012) 125(Pt 3):735-42. doi:10.1242/jcs.092825
    • (2012) J Cell Sci , vol.125 , pp. 735-742
    • Smoligovets, A.A.1    Smith, A.W.2    Wu, H.J.3    Petit, R.S.4    Groves, J.T.5
  • 75
    • 84895891752 scopus 로고    scopus 로고
    • Polarized release of T-cell-receptor-enriched microvesicles at the immunological synapse
    • Choudhuri K, Llodra J, Roth EW, Tsai J, Gordo S, Wucherpfennig KW, et al. Polarized release of T-cell-receptor-enriched microvesicles at the immunological synapse. Nature (2014) 507(7490):118-23. doi:10.1038/nature12951
    • (2014) Nature , vol.507 , Issue.7490 , pp. 118-123
    • Choudhuri, K.1    Llodra, J.2    Roth, E.W.3    Tsai, J.4    Gordo, S.5    Wucherpfennig, K.W.6
  • 76
    • 77951688912 scopus 로고    scopus 로고
    • Essential role of ubiquitin and TSG101 protein in formation and function of the central supramolecular activation cluster
    • Vardhana S, Choudhuri K, Varma R, Dustin ML. Essential role of ubiquitin and TSG101 protein in formation and function of the central supramolecular activation cluster. Immunity (2010) 32(4):531-40. doi:10.1016/j.immuni.2010.04.005
    • (2010) Immunity , vol.32 , Issue.4 , pp. 531-540
    • Vardhana, S.1    Choudhuri, K.2    Varma, R.3    Dustin, M.L.4
  • 77
    • 27944442353 scopus 로고    scopus 로고
    • Altered TCR signaling from geometrically repatterned immunological synapses
    • Mossman KD, Campi G, Groves JT, Dustin ML. Altered TCR signaling from geometrically repatterned immunological synapses. Science (2005) 310(5751):1191-3. doi:10.1126/science.1119238
    • (2005) Science , vol.310 , Issue.5751 , pp. 1191-1193
    • Mossman, K.D.1    Campi, G.2    Groves, J.T.3    Dustin, M.L.4
  • 78
    • 51349131307 scopus 로고    scopus 로고
    • The balance between T cell receptor signaling and degradation at the center of the immunological synapse is determined by antigen quality
    • Cemerski S, Das J, Giurisato E, Markiewicz MA, Allen PM, Chakraborty AK, et al. The balance between T cell receptor signaling and degradation at the center of the immunological synapse is determined by antigen quality. Immunity (2008) 29(3):414-22. doi:10.1016/j.immuni.2008.06.014
    • (2008) Immunity , vol.29 , Issue.3 , pp. 414-422
    • Cemerski, S.1    Das, J.2    Giurisato, E.3    Markiewicz, M.A.4    Allen, P.M.5    Chakraborty, A.K.6
  • 79
    • 79960401707 scopus 로고    scopus 로고
    • Mechanical interactions between dendritic cells and T cells correlate with T cell responsiveness
    • Lim TS, Mortellaro A, Lim CT, Hammerling GJ, Ricciardi-Castagnoli P. Mechanical interactions between dendritic cells and T cells correlate with T cell responsiveness. J Immunol (2011) 187(1):258-65. doi:10.4049/jimmunol.1100267
    • (2011) J Immunol , vol.187 , Issue.1 , pp. 258-265
    • Lim, T.S.1    Mortellaro, A.2    Lim, C.T.3    Hammerling, G.J.4    Ricciardi-Castagnoli, P.5
  • 81
    • 84864131658 scopus 로고    scopus 로고
    • Substrate rigidity regulates human T cell activation and proliferation
    • O'Connor RS, Hao X, Shen K, Bashour K, Akimova T, Hancock WW, et al. Substrate rigidity regulates human T cell activation and proliferation. J Immunol (2012) 189(3):1330-9. doi:10.4049/jimmunol.1102757
    • (2012) J Immunol , vol.189 , Issue.3 , pp. 1330-1339
    • O'Connor, R.S.1    Hao, X.2    Shen, K.3    Bashour, K.4    Akimova, T.5    Hancock, W.W.6
  • 82
    • 79955904928 scopus 로고    scopus 로고
    • Force generation upon T cell receptor engagement
    • Husson J, Chemin K, Bohineust A, Hivroz C, Henry N. Force generation upon T cell receptor engagement. PLoS One (2011) 6(5):e19680. doi:10.1371/journal.pone.0019680
    • (2011) PLoS One , vol.6 , Issue.5
    • Husson, J.1    Chemin, K.2    Bohineust, A.3    Hivroz, C.4    Henry, N.5
  • 83
    • 0033587686 scopus 로고    scopus 로고
    • Mapping the sensitivity of T cells with an optical trap: polarity and minimal number of receptors for Ca(2+) signaling
    • Wei X, Tromberg BJ, Cahalan MD. Mapping the sensitivity of T cells with an optical trap: polarity and minimal number of receptors for Ca(2+) signaling. Proc Natl Acad Sci U S A (1999) 96(15):8471-6. doi:10.1073/pnas.96.15.8471
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.15 , pp. 8471-8476
    • Wei, X.1    Tromberg, B.J.2    Cahalan, M.D.3
  • 84
    • 0005448458 scopus 로고    scopus 로고
    • Polarity of T cell shape, motility, and sensitivity to antigen
    • Negulescu PA, Krasieva TB, Khan A, Kerschbaum HH, Cahalan MD. Polarity of T cell shape, motility, and sensitivity to antigen. Immunity (1996) 4(5):421-30. doi:10.1016/S1074-7613(00)80409-4
    • (1996) Immunity , vol.4 , Issue.5 , pp. 421-430
    • Negulescu, P.A.1    Krasieva, T.B.2    Khan, A.3    Kerschbaum, H.H.4    Cahalan, M.D.5
  • 85
    • 78650599246 scopus 로고    scopus 로고
    • Mechanisms for T cell receptor triggering
    • van der Merwe PA, Dushek O. Mechanisms for T cell receptor triggering. Nat Rev Immunol (2011) 11(1):47-55. doi:10.1038/nri2887
    • (2011) Nat Rev Immunol , vol.11 , Issue.1 , pp. 47-55
    • van der Merwe, P.A.1    Dushek, O.2
  • 86
    • 84887615587 scopus 로고    scopus 로고
    • A single peptide-major histocompatibility complex ligand triggers digital cytokine secretion in CD4(+) T cells
    • Huang J, Brameshuber M, Zeng X, Xie J, Li QJ, Chien YH, et al. A single peptide-major histocompatibility complex ligand triggers digital cytokine secretion in CD4(+) T cells. Immunity (2013) 39(5):846-57. doi:10.1016/j.immuni.2013.08.036
    • (2013) Immunity , vol.39 , Issue.5 , pp. 846-857
    • Huang, J.1    Brameshuber, M.2    Zeng, X.3    Xie, J.4    Li, Q.J.5    Chien, Y.H.6
  • 87
    • 77953911933 scopus 로고    scopus 로고
    • Constitutively active Lck kinase in T cells drives antigen receptor signal transduction
    • Nika K, Soldani C, Salek M, Paster W, Gray A, Etzensperger R, et al. Constitutively active Lck kinase in T cells drives antigen receptor signal transduction. Immunity (2010) 32(6):766-77. doi:10.1016/j.immuni.2010.05.011
    • (2010) Immunity , vol.32 , Issue.6 , pp. 766-777
    • Nika, K.1    Soldani, C.2    Salek, M.3    Paster, W.4    Gray, A.5    Etzensperger, R.6
  • 88
    • 0028140140 scopus 로고
    • Induction of tyrosine phosphorylation and T-cell activation by vanadate peroxide, an inhibitor of protein tyrosine phosphatases
    • Imbert V, Peyron JF, Farahi Far D, Mari B, Auberger P, Rossi B. Induction of tyrosine phosphorylation and T-cell activation by vanadate peroxide, an inhibitor of protein tyrosine phosphatases. Biochem J (1994) 297(Pt 1):163-73. doi:10.1042/bj2970163
    • (1994) Biochem J , vol.297 , pp. 163-173
    • Imbert, V.1    Peyron, J.F.2    Farahi Far, D.3    Mari, B.4    Auberger, P.5    Rossi, B.6
  • 89
    • 0029896636 scopus 로고    scopus 로고
    • Stimulation of the T-cell antigen receptor-CD3 complex signaling pathway by the tyrosine phosphatase inhibitor pervanadate is mediated by inhibition of CD45: evidence for two interconnected Lck/Fyn-or zap-70-dependent signaling pathways
    • Imbert V, Farahifar D, Auberger P, Mary D, Rossi B, Peyron JF. Stimulation of the T-cell antigen receptor-CD3 complex signaling pathway by the tyrosine phosphatase inhibitor pervanadate is mediated by inhibition of CD45: evidence for two interconnected Lck/Fyn-or zap-70-dependent signaling pathways. J Inflamm (1996) 46(2):65-77.
    • (1996) J Inflamm , vol.46 , Issue.2 , pp. 65-77
    • Imbert, V.1    Farahifar, D.2    Auberger, P.3    Mary, D.4    Rossi, B.5    Peyron, J.F.6
  • 90
    • 0027417482 scopus 로고
    • Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events
    • Secrist JP, Burns LA, Karnitz L, Koretzky GA, Abraham RT. Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events. J Biol Chem (1993) 268(8):5886-93.
    • (1993) J Biol Chem , vol.268 , Issue.8 , pp. 5886-5893
    • Secrist, J.P.1    Burns, L.A.2    Karnitz, L.3    Koretzky, G.A.4    Abraham, R.T.5
  • 91
    • 84863482471 scopus 로고    scopus 로고
    • Biophysical mechanism of T-cell receptor triggering in a reconstituted system
    • James JR, Vale RD. Biophysical mechanism of T-cell receptor triggering in a reconstituted system. Nature (2012) 487(7405):64-9. doi:10.1038/nature11220
    • (2012) Nature , vol.487 , Issue.7405 , pp. 64-69
    • James, J.R.1    Vale, R.D.2
  • 92
    • 33746114879 scopus 로고    scopus 로고
    • The kinetic-segregation model: TCR triggering and beyond
    • Davis SJ, van der Merwe PA. The kinetic-segregation model: TCR triggering and beyond. Nat Immunol (2006) 7(8):803-9. doi:10.1038/ni1369
    • (2006) Nat Immunol , vol.7 , Issue.8 , pp. 803-809
    • Davis, S.J.1    van der Merwe, P.A.2
  • 93
    • 84893747396 scopus 로고    scopus 로고
    • In vitro membrane reconstitution of the T-cell receptor proximal signaling network
    • Hui E, Vale RD. In vitro membrane reconstitution of the T-cell receptor proximal signaling network. Nat Struct Mol Biol (2014) 21(2):133-42. doi:10.1038/nsmb.2762
    • (2014) Nat Struct Mol Biol , vol.21 , Issue.2 , pp. 133-142
    • Hui, E.1    Vale, R.D.2
  • 94
    • 84904436467 scopus 로고    scopus 로고
    • The cancer glycocalyx mechanically primes integrin-mediated growth and survival
    • Paszek MJ, DuFort CC, Rossier O, Bainer R, Mouw JK, Godula K, et al. The cancer glycocalyx mechanically primes integrin-mediated growth and survival. Nature (2014) 511(7509):319-25. doi:10.1038/nature13535
    • (2014) Nature , vol.511 , Issue.7509 , pp. 319-325
    • Paszek, M.J.1    DuFort, C.C.2    Rossier, O.3    Bainer, R.4    Mouw, J.K.5    Godula, K.6
  • 95
    • 84880407025 scopus 로고    scopus 로고
    • The large ectodomains of CD45 and CD148 regulate their segregation from and inhibition of ligated T-cell receptor
    • Cordoba SP, Choudhuri K, Zhang H, Bridge M, Basat AB, Dustin ML, et al. The large ectodomains of CD45 and CD148 regulate their segregation from and inhibition of ligated T-cell receptor. Blood (2013) 121(21):4295-302. doi:10.1182/blood-2012-07-442251
    • (2013) Blood , vol.121 , Issue.21 , pp. 4295-4302
    • Cordoba, S.P.1    Choudhuri, K.2    Zhang, H.3    Bridge, M.4    Basat, A.B.5    Dustin, M.L.6
  • 96
    • 0037318863 scopus 로고    scopus 로고
    • CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling
    • Irles C, Symons A, Michel F, Bakker TR, van der Merwe PA, Acuto O. CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling. Nat Immunol (2003) 4(2):189-97. doi:10.1038/ni877
    • (2003) Nat Immunol , vol.4 , Issue.2 , pp. 189-197
    • Irles, C.1    Symons, A.2    Michel, F.3    Bakker, T.R.4    van der Merwe, P.A.5    Acuto, O.6
  • 97
    • 23144455728 scopus 로고    scopus 로고
    • T-cell receptor triggering is critically dependent on the dimensions of its peptide-MHC ligand
    • Choudhuri K, Wiseman D, Brown MH, Gould K, van der Merwe PA. T-cell receptor triggering is critically dependent on the dimensions of its peptide-MHC ligand. Nature (2005) 436(7050):578-82. doi:10.1038/nature03843
    • (2005) Nature , vol.436 , Issue.7050 , pp. 578-582
    • Choudhuri, K.1    Wiseman, D.2    Brown, M.H.3    Gould, K.4    van der Merwe, P.A.5
  • 98
    • 70350035998 scopus 로고    scopus 로고
    • Peptide-major histocompatibility complex dimensions control proximal kinase-phosphatase balance during T cell activation
    • Choudhuri K, Parker M, Milicic A, Cole DK, Shaw MK, Sewell AK, et al. Peptide-major histocompatibility complex dimensions control proximal kinase-phosphatase balance during T cell activation. J Biol Chem (2009) 284(38):26096-105. doi:10.1074/jbc.M109.039966
    • (2009) J Biol Chem , vol.284 , Issue.38 , pp. 26096-26105
    • Choudhuri, K.1    Parker, M.2    Milicic, A.3    Cole, D.K.4    Shaw, M.K.5    Sewell, A.K.6
  • 99
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass AD, Vale RD. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell (2005) 121(6):937-50. doi:10.1016/j.cell.2005.04.009
    • (2005) Cell , vol.121 , Issue.6 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 100
    • 18244364886 scopus 로고    scopus 로고
    • ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse
    • Allenspach EJ, Cullinan P, Tong J, Tang Q, Tesciuba AG, Cannon JL, et al. ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse. Immunity (2001) 15(5):739-50. doi:10.1016/S1074-7613(01)00224-2
    • (2001) Immunity , vol.15 , Issue.5 , pp. 739-750
    • Allenspach, E.J.1    Cullinan, P.2    Tong, J.3    Tang, Q.4    Tesciuba, A.G.5    Cannon, J.L.6
  • 101
    • 78149489327 scopus 로고    scopus 로고
    • Matched sizes of activating and inhibitory receptor/ligand pairs are required for optimal signal integration by human natural killer cells
    • Kohler K, Xiong S, Brzostek J, Mehrabi M, Eissmann P, Harrison A, et al. Matched sizes of activating and inhibitory receptor/ligand pairs are required for optimal signal integration by human natural killer cells. PLoS One (2010) 5(11):e15374. doi:10.1371/journal.pone.0015374
    • (2010) PLoS One , vol.5 , Issue.11
    • Kohler, K.1    Xiong, S.2    Brzostek, J.3    Mehrabi, M.4    Eissmann, P.5    Harrison, A.6
  • 102
    • 33750798761 scopus 로고    scopus 로고
    • Segregation of HLA-C from ICAM-1 at NK cell immune synapses is controlled by its cell surface density
    • Almeida CR, Davis DM. Segregation of HLA-C from ICAM-1 at NK cell immune synapses is controlled by its cell surface density. J Immunol (2006) 177(10):6904-10. doi:10.4049/jimmunol.177.10.6904
    • (2006) J Immunol , vol.177 , Issue.10 , pp. 6904-6910
    • Almeida, C.R.1    Davis, D.M.2
  • 103
    • 84903643106 scopus 로고    scopus 로고
    • TCR microclusters pre-exist and contain molecules necessary for TCR signal transduction
    • Crites TJ, Padhan K, Muller J, Krogsgaard M, Gudla PR, Lockett SJ, et al. TCR microclusters pre-exist and contain molecules necessary for TCR signal transduction. J Immunol (2014) 193(1):56-67. doi:10.4049/jimmunol.1400315
    • (2014) J Immunol , vol.193 , Issue.1 , pp. 56-67
    • Crites, T.J.1    Padhan, K.2    Muller, J.3    Krogsgaard, M.4    Gudla, P.R.5    Lockett, S.J.6
  • 104
    • 0037144842 scopus 로고    scopus 로고
    • T cell receptor ligation induces the formation of dynamically regulated signaling assemblies
    • Bunnell SC, Hong DI, Kardon JR, Yamazaki T, McGlade CJ, Barr VA, et al. T cell receptor ligation induces the formation of dynamically regulated signaling assemblies. J Cell Biol (2002) 158(7):1263-75. doi:10.1083/jcb.200203043
    • (2002) J Cell Biol , vol.158 , Issue.7 , pp. 1263-1275
    • Bunnell, S.C.1    Hong, D.I.2    Kardon, J.R.3    Yamazaki, T.4    McGlade, C.J.5    Barr, V.A.6
  • 105
    • 0029063148 scopus 로고
    • Kinetic proofreading in T-cell receptor signal transduction
    • McKeithan TW. Kinetic proofreading in T-cell receptor signal transduction. Proc Natl Acad Sci U S A (1995) 92(11):5042-6. doi:10.1073/pnas.92.11.5042
    • (1995) Proc Natl Acad Sci U S A , vol.92 , Issue.11 , pp. 5042-5046
    • McKeithan, T.W.1
  • 106
    • 73449105773 scopus 로고    scopus 로고
    • A role for rebinding in rapid and reliable T cell responses to antigen
    • Dushek O, Das R, Coombs D. A role for rebinding in rapid and reliable T cell responses to antigen. PLoS Comput Biol (2009) 5(11):e1000578. doi:10.1371/journal.pcbi.1000578
    • (2009) PLoS Comput Biol , vol.5 , Issue.11
    • Dushek, O.1    Das, R.2    Coombs, D.3
  • 107
    • 77952712883 scopus 로고    scopus 로고
    • Fast on-rates allow short dwell time ligands to activate T cells
    • Govern CC, Paczosa MK, Chakraborty AK, Huseby ES. Fast on-rates allow short dwell time ligands to activate T cells. Proc Natl Acad Sci U S A (2010) 107(19):8724-9. doi:10.1073/pnas.1000966107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.19 , pp. 8724-8729
    • Govern, C.C.1    Paczosa, M.K.2    Chakraborty, A.K.3    Huseby, E.S.4
  • 108
    • 76949085272 scopus 로고    scopus 로고
    • Dependence of T cell antigen recognition on T cell receptor-peptide MHC confinement time
    • Aleksic M, Dushek O, Zhang H, Shenderov E, Chen JL, Cerundolo V, et al. Dependence of T cell antigen recognition on T cell receptor-peptide MHC confinement time. Immunity (2010) 32(2):163-74. doi:10.1016/j.immuni.2009.11.013
    • (2010) Immunity , vol.32 , Issue.2 , pp. 163-174
    • Aleksic, M.1    Dushek, O.2    Zhang, H.3    Shenderov, E.4    Chen, J.L.5    Cerundolo, V.6
  • 109
    • 77249114784 scopus 로고    scopus 로고
    • TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity
    • Huppa JB, Axmann M, Mortelmaier MA, Lillemeier BF, Newell EW, Brameshuber M, et al. TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity. Nature (2010) 463(7283):963-7. doi:10.1038/nature08746
    • (2010) Nature , vol.463 , Issue.7283 , pp. 963-967
    • Huppa, J.B.1    Axmann, M.2    Mortelmaier, M.A.3    Lillemeier, B.F.4    Newell, E.W.5    Brameshuber, M.6
  • 110
    • 77950809538 scopus 로고    scopus 로고
    • The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness
    • Huang J, Zarnitsyna VI, Liu B, Edwards LJ, Jiang N, Evavold BD, et al. The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness. Nature (2010) 464(7290):932-6. doi:10.1038/nature08944
    • (2010) Nature , vol.464 , Issue.7290 , pp. 932-936
    • Huang, J.1    Zarnitsyna, V.I.2    Liu, B.3    Edwards, L.J.4    Jiang, N.5    Evavold, B.D.6
  • 111
    • 84898644308 scopus 로고    scopus 로고
    • Accumulation of dynamic catch bonds between TCR and agonist peptide-MHC triggers T cell signaling
    • Liu B, Chen W, Evavold BD, Zhu C. Accumulation of dynamic catch bonds between TCR and agonist peptide-MHC triggers T cell signaling. Cell (2014) 157(2):357-68. doi:10.1016/j.cell.2014.02.053
    • (2014) Cell , vol.157 , Issue.2 , pp. 357-368
    • Liu, B.1    Chen, W.2    Evavold, B.D.3    Zhu, C.4
  • 112
    • 0029037210 scopus 로고
    • Serial triggering of many T-cell receptors by a few peptide-MHC complexes
    • Valitutti S, Muller S, Cella M, Padovan E, Lanzavecchia A. Serial triggering of many T-cell receptors by a few peptide-MHC complexes. Nature (1995) 375(6527):148-51. doi:10.1038/375148a0
    • (1995) Nature , vol.375 , Issue.6527 , pp. 148-151
    • Valitutti, S.1    Muller, S.2    Cella, M.3    Padovan, E.4    Lanzavecchia, A.5
  • 113
    • 80053130680 scopus 로고    scopus 로고
    • New insights into the T cell synapse from single molecule techniques
    • Dustin ML, Depoil D. New insights into the T cell synapse from single molecule techniques. Nat Rev Immunol (2011) 11(10):672-84. doi:10.1038/nri3066
    • (2011) Nat Rev Immunol , vol.11 , Issue.10 , pp. 672-684
    • Dustin, M.L.1    Depoil, D.2
  • 114
    • 84861991991 scopus 로고    scopus 로고
    • Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules
    • Gowrishankar K, Ghosh S, Saha S, C R, Mayor S, Rao M. Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules. Cell (2012) 149(6):1353-67. doi:10.1016/j.cell.2012.05.008
    • (2012) Cell , vol.149 , Issue.6 , pp. 1353-1367
    • Gowrishankar, K.1    Ghosh, S.2    Saha, S.C.R.3    Mayor, S.4    Rao, M.5
  • 115
    • 0028851581 scopus 로고
    • Tyrosine-phosphorylated T cell receptor zeta chain associates with the actin cytoskeleton upon activation of mature T lymphocytes
    • Rozdzial MM, Malissen B, Finkel TH. Tyrosine-phosphorylated T cell receptor zeta chain associates with the actin cytoskeleton upon activation of mature T lymphocytes. Immunity (1995) 3(5):623-33. doi:10.1016/1074-7613(95)90133-7
    • (1995) Immunity , vol.3 , Issue.5 , pp. 623-633
    • Rozdzial, M.M.1    Malissen, B.2    Finkel, T.H.3
  • 116
    • 84892458771 scopus 로고    scopus 로고
    • Unique zeta-chain motifs mediate a direct TCR-actin linkage critical for immunological synapse formation and T-cell activation
    • Klieger Y, Almogi-Hazan O, Ish-Shalom E, Pato A, Pauker MH, Barda-Saad M, et al. Unique zeta-chain motifs mediate a direct TCR-actin linkage critical for immunological synapse formation and T-cell activation. Eur J Immunol (2014) 44(1):58-68. doi:10.1002/eji.201243099
    • (2014) Eur J Immunol , vol.44 , Issue.1 , pp. 58-68
    • Klieger, Y.1    Almogi-Hazan, O.2    Ish-Shalom, E.3    Pato, A.4    Pauker, M.H.5    Barda-Saad, M.6
  • 117
    • 0032532949 scopus 로고    scopus 로고
    • pp56Lck mediates TCR zeta-chain binding to the microfilament cytoskeleton
    • Rozdzial MM, Pleiman CM, Cambier JC, Finkel TH. pp56Lck mediates TCR zeta-chain binding to the microfilament cytoskeleton. J Immunol (1998) 161(10):5491-9.
    • (1998) J Immunol , vol.161 , Issue.10 , pp. 5491-5499
    • Rozdzial, M.M.1    Pleiman, C.M.2    Cambier, J.C.3    Finkel, T.H.4
  • 118
    • 42049101786 scopus 로고    scopus 로고
    • The receptor deformation model of TCR triggering
    • Ma Z, Janmey PA, Finkel TH. The receptor deformation model of TCR triggering. FASEB J (2008) 22(4):1002-8. doi:10.1096/fj.07-9331hyp
    • (2008) FASEB J , vol.22 , Issue.4 , pp. 1002-1008
    • Ma, Z.1    Janmey, P.A.2    Finkel, T.H.3
  • 119
    • 0348047600 scopus 로고    scopus 로고
    • Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation
    • Krogsgaard M, Prado N, Adams EJ, He XL, Chow DC, Wilson DB, et al. Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation. Mol Cell (2003) 12(6):1367-78. doi:10.1016/S1097-2765(03)00474-X
    • (2003) Mol Cell , vol.12 , Issue.6 , pp. 1367-1378
    • Krogsgaard, M.1    Prado, N.2    Adams, E.J.3    He, X.L.4    Chow, D.C.5    Wilson, D.B.6
  • 120
    • 67349283033 scopus 로고    scopus 로고
    • Antigen ligation triggers a conformational change within the constant domain of the alphabeta T cell receptor
    • Beddoe T, Chen Z, Clements CS, Ely LK, Bushell SR, Vivian JP, et al. Antigen ligation triggers a conformational change within the constant domain of the alphabeta T cell receptor. Immunity (2009) 30(6):777-88. doi:10.1016/j.immuni.2009.03.018
    • (2009) Immunity , vol.30 , Issue.6 , pp. 777-788
    • Beddoe, T.1    Chen, Z.2    Clements, C.S.3    Ely, L.K.4    Bushell, S.R.5    Vivian, J.P.6
  • 121
    • 18344394144 scopus 로고    scopus 로고
    • A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex
    • Reiser JB, Gregoire C, Darnault C, Mosser T, Guimezanes A, Schmitt-Verhulst AM, et al. A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex. Immunity (2002) 16(3):345-54. doi:10.1016/S1074-7613(02)00288-1
    • (2002) Immunity , vol.16 , Issue.3 , pp. 345-354
    • Reiser, J.B.1    Gregoire, C.2    Darnault, C.3    Mosser, T.4    Guimezanes, A.5    Schmitt-Verhulst, A.M.6
  • 122
    • 10644239910 scopus 로고    scopus 로고
    • T cell cross-reactivity and conformational changes during TCR engagement
    • Lee JK, Stewart-Jones G, Dong T, Harlos K, Di Gleria K, Dorrell L, et al. T cell cross-reactivity and conformational changes during TCR engagement. J Exp Med (2004) 200(11):1455-66. doi:10.1084/jem.20041251
    • (2004) J Exp Med , vol.200 , Issue.11 , pp. 1455-1466
    • Lee, J.K.1    Stewart-Jones, G.2    Dong, T.3    Harlos, K.4    Di Gleria, K.5    Dorrell, L.6
  • 123
    • 84859447015 scopus 로고    scopus 로고
    • T cell receptors are structures capable of initiating signaling in the absence of large conformational rearrangements
    • Fernandes RA, Shore DA, Vuong MT, Yu C, Zhu X, Pereira-Lopes S, et al. T cell receptors are structures capable of initiating signaling in the absence of large conformational rearrangements. J Biol Chem (2012) 287(16):13324-35. doi:10.1074/jbc.M111.332783
    • (2012) J Biol Chem , vol.287 , Issue.16 , pp. 13324-13335
    • Fernandes, R.A.1    Shore, D.A.2    Vuong, M.T.3    Yu, C.4    Zhu, X.5    Pereira-Lopes, S.6
  • 124
    • 0033710093 scopus 로고    scopus 로고
    • The relationship of MHC-peptide binding and T cell activation probed using chemically defined MHC class II oligomers
    • Cochran JR, Cameron TO, Stern LJ. The relationship of MHC-peptide binding and T cell activation probed using chemically defined MHC class II oligomers. Immunity (2000) 12(3):241-50. doi:10.1016/S1074-7613(00)80177-6
    • (2000) Immunity , vol.12 , Issue.3 , pp. 241-250
    • Cochran, J.R.1    Cameron, T.O.2    Stern, L.J.3
  • 125
    • 0032476622 scopus 로고    scopus 로고
    • Potent T cell activation with dimeric peptide-major histocompatibility complex class II ligand: the role of CD4 coreceptor
    • Hamad AR, O'Herrin SM, Lebowitz MS, Srikrishnan A, Bieler J, Schneck J, et al. Potent T cell activation with dimeric peptide-major histocompatibility complex class II ligand: the role of CD4 coreceptor. J Exp Med (1998) 188(9):1633-40. doi:10.1084/jem.188.9.1633
    • (1998) J Exp Med , vol.188 , Issue.9 , pp. 1633-1640
    • Hamad, A.R.1    O'Herrin, S.M.2    Lebowitz, M.S.3    Srikrishnan, A.4    Bieler, J.5    Schneck, J.6
  • 126
    • 0034614614 scopus 로고    scopus 로고
    • Kinetics of T-cell receptor binding by bivalent HLA-DR. Peptide complexes that activate antigen-specific human T-cells
    • Appel H, Gauthier L, Pyrdol J, Wucherpfennig KW. Kinetics of T-cell receptor binding by bivalent HLA-DR. Peptide complexes that activate antigen-specific human T-cells. J Biol Chem (2000) 275(1):312-21. doi:10.1074/jbc.275.1.312
    • (2000) J Biol Chem , vol.275 , Issue.1 , pp. 312-321
    • Appel, H.1    Gauthier, L.2    Pyrdol, J.3    Wucherpfennig, K.W.4
  • 127
    • 0032192469 scopus 로고    scopus 로고
    • Initiation of signal transduction through the T cell receptor requires the multivalent engagement of peptide/MHC ligands [corrected]
    • Boniface JJ, Rabinowitz JD, Wulfing C, Hampl J, Reich Z, Altman JD, et al. Initiation of signal transduction through the T cell receptor requires the multivalent engagement of peptide/MHC ligands [corrected]. Immunity (1998) 9(4):459-66. doi:10.1016/S1074-7613(00)80629-9
    • (1998) Immunity , vol.9 , Issue.4 , pp. 459-466
    • Boniface, J.J.1    Rabinowitz, J.D.2    Wulfing, C.3    Hampl, J.4    Reich, Z.5    Altman, J.D.6
  • 128
    • 0033575788 scopus 로고    scopus 로고
    • Antigen-specific signaling by a soluble, dimeric peptide/major histocompatibility complex class II/Fc chimera leading to T helper cell type 2 differentiation
    • Casares S, Zong CS, Radu DL, Miller A, Bona CA, Brumeanu TD. Antigen-specific signaling by a soluble, dimeric peptide/major histocompatibility complex class II/Fc chimera leading to T helper cell type 2 differentiation. J Exp Med (1999) 190(4):543-53. doi:10.1084/jem.190.4.543
    • (1999) J Exp Med , vol.190 , Issue.4 , pp. 543-553
    • Casares, S.1    Zong, C.S.2    Radu, D.L.3    Miller, A.4    Bona, C.A.5    Brumeanu, T.D.6
  • 129
    • 12344272845 scopus 로고    scopus 로고
    • Dynamic molecular interactions linking the T cell antigen receptor to the actin cytoskeleton
    • Barda-Saad M, Braiman A, Titerence R, Bunnell SC, Barr VA, Samelson LE. Dynamic molecular interactions linking the T cell antigen receptor to the actin cytoskeleton. Nat Immunol (2005) 6(1):80-9. doi:10.1038/ni1143
    • (2005) Nat Immunol , vol.6 , Issue.1 , pp. 80-89
    • Barda-Saad, M.1    Braiman, A.2    Titerence, R.3    Bunnell, S.C.4    Barr, V.A.5    Samelson, L.E.6
  • 130
    • 68949163905 scopus 로고    scopus 로고
    • Vav links the T cell antigen receptor to the actin cytoskeleton and T cell activation independently of intrinsic guanine nucleotide exchange activity
    • Miletic AV, Graham DB, Sakata-Sogawa K, Hiroshima M, Hamann MJ, Cemerski S, et al. Vav links the T cell antigen receptor to the actin cytoskeleton and T cell activation independently of intrinsic guanine nucleotide exchange activity. PLoS One (2009) 4(8):e6599. doi:10.1371/journal.pone.0006599
    • (2009) PLoS One , vol.4 , Issue.8
    • Miletic, A.V.1    Graham, D.B.2    Sakata-Sogawa, K.3    Hiroshima, M.4    Hamann, M.J.5    Cemerski, S.6
  • 131
    • 14244262563 scopus 로고    scopus 로고
    • T cell receptor engagement by peptide-MHC ligands induces a conformational change in the CD3 complex of thymocytes
    • Gil D, Schrum AG, Alarcon B, Palmer E. T cell receptor engagement by peptide-MHC ligands induces a conformational change in the CD3 complex of thymocytes. J Exp Med (2005) 201(4):517-22. doi:10.1084/jem.20042036
    • (2005) J Exp Med , vol.201 , Issue.4 , pp. 517-522
    • Gil, D.1    Schrum, A.G.2    Alarcon, B.3    Palmer, E.4
  • 132
    • 40149108609 scopus 로고    scopus 로고
    • Surface-anchored monomeric agonist pMHCs alone trigger TCR with high sensitivity
    • Ma Z, Sharp KA, Janmey PA, Finkel TH. Surface-anchored monomeric agonist pMHCs alone trigger TCR with high sensitivity. PLoS Biol (2008) 6(2):e43. doi:10.1371/journal.pbio.0060043
    • (2008) PLoS Biol , vol.6 , Issue.2
    • Ma, Z.1    Sharp, K.A.2    Janmey, P.A.3    Finkel, T.H.4
  • 133
    • 84862628815 scopus 로고    scopus 로고
    • Photocrosslinkable pMHC monomers stain T cells specifically and cause ligand-bound TCRs to be 'preferentially' transported to the cSMAC
    • Xie J, Huppa JB, Newell EW, Huang J, Ebert PJ, Li QJ, et al. Photocrosslinkable pMHC monomers stain T cells specifically and cause ligand-bound TCRs to be 'preferentially' transported to the cSMAC. Nat Immunol (2012) 13(7):674-80. doi:10.1038/ni.2344
    • (2012) Nat Immunol , vol.13 , Issue.7 , pp. 674-680
    • Xie, J.1    Huppa, J.B.2    Newell, E.W.3    Huang, J.4    Ebert, P.J.5    Li, Q.J.6
  • 134
    • 0028961573 scopus 로고
    • Sustained signaling leading to T cell activation results from prolonged T cell receptor occupancy. Role of T cell actin cytoskeleton
    • Valitutti S, Dessing M, Aktories K, Gallati H, Lanzavecchia A. Sustained signaling leading to T cell activation results from prolonged T cell receptor occupancy. Role of T cell actin cytoskeleton. J Exp Med (1995) 181(2):577-84. doi:10.1084/jem.181.2.577
    • (1995) J Exp Med , vol.181 , Issue.2 , pp. 577-584
    • Valitutti, S.1    Dessing, M.2    Aktories, K.3    Gallati, H.4    Lanzavecchia, A.5
  • 135
    • 0842325726 scopus 로고    scopus 로고
    • Actin cytoskeleton regulates calcium dynamics and NFAT nuclear duration
    • Rivas FV, O'Keefe JP, Alegre ML, Gajewski TF. Actin cytoskeleton regulates calcium dynamics and NFAT nuclear duration. Mol Cell Biol (2004) 24(4):1628-39. doi:10.1128/MCB.24.4.1628-1639.2004
    • (2004) Mol Cell Biol , vol.24 , Issue.4 , pp. 1628-1639
    • Rivas, F.V.1    O'Keefe, J.P.2    Alegre, M.L.3    Gajewski, T.F.4
  • 136
    • 71449090489 scopus 로고    scopus 로고
    • The alphabeta T cell receptor is an anisotropic mechanosensor
    • Kim ST, Takeuchi K, Sun ZY, Touma M, Castro CE, Fahmy A, et al. The alphabeta T cell receptor is an anisotropic mechanosensor. J Biol Chem (2009) 284(45):31028-37. doi:10.1074/jbc.M109.052712
    • (2009) J Biol Chem , vol.284 , Issue.45 , pp. 31028-31037
    • Kim, S.T.1    Takeuchi, K.2    Sun, Z.Y.3    Touma, M.4    Castro, C.E.5    Fahmy, A.6
  • 137
    • 84862978540 scopus 로고    scopus 로고
    • TCR mechanobiology: torques and tunable structures linked to early T cell signaling
    • Kim ST, Shin Y, Brazin K, Mallis RJ, Sun ZY, Wagner G, et al. TCR mechanobiology: torques and tunable structures linked to early T cell signaling. Front Immunol (2012) 3:76. doi:10.3389/fimmu.2012.00076
    • (2012) Front Immunol , vol.3 , pp. 76
    • Kim, S.T.1    Shin, Y.2    Brazin, K.3    Mallis, R.J.4    Sun, Z.Y.5    Wagner, G.6
  • 138
    • 84893837202 scopus 로고    scopus 로고
    • CD28 and CD3 have complementary roles in T-cell traction forces
    • Bashour KT, Gondarenko A, Chen H, Shen K, Liu X, Huse M, et al. CD28 and CD3 have complementary roles in T-cell traction forces. Proc Natl Acad Sci U S A (2014) 111(6):2241-6. doi:10.1073/pnas.1315606111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.6 , pp. 2241-2246
    • Bashour, K.T.1    Gondarenko, A.2    Chen, H.3    Shen, K.4    Liu, X.5    Huse, M.6
  • 139
    • 84922831195 scopus 로고    scopus 로고
    • Cytoskeletal forces during signaling activation in Jurkat T-cells
    • Hui KL, Balagopalan L, Samelson LE, Upadhyaya A. Cytoskeletal forces during signaling activation in Jurkat T-cells. Mol Biol Cell (2015) 26(4):685-95. doi:10.1091/mbc.E14-03-0830
    • (2015) Mol Biol Cell , vol.26 , Issue.4 , pp. 685-695
    • Hui, K.L.1    Balagopalan, L.2    Samelson, L.E.3    Upadhyaya, A.4
  • 140
    • 84903641324 scopus 로고    scopus 로고
    • Accumulation of serial forces on TCR and CD8 frequently applied by agonist antigenic peptides embedded in MHC molecules triggers calcium in T cells
    • Pryshchep S, Zarnitsyna VI, Hong J, Evavold BD, Zhu C. Accumulation of serial forces on TCR and CD8 frequently applied by agonist antigenic peptides embedded in MHC molecules triggers calcium in T cells. J Immunol (2014) 193(1):68-76. doi:10.4049/jimmunol.1303436
    • (2014) J Immunol , vol.193 , Issue.1 , pp. 68-76
    • Pryshchep, S.1    Zarnitsyna, V.I.2    Hong, J.3    Evavold, B.D.4    Zhu, C.5
  • 141
    • 82755165363 scopus 로고    scopus 로고
    • Basic residues in the T-cell receptor zeta cytoplasmic domain mediate membrane association and modulate signaling
    • Zhang H, Cordoba SP, Dushek O, van der Merwe PA. Basic residues in the T-cell receptor zeta cytoplasmic domain mediate membrane association and modulate signaling. Proc Natl Acad Sci U S A (2011) 108(48):19323-8. doi:10.1073/pnas.1108052108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.48 , pp. 19323-19328
    • Zhang, H.1    Cordoba, S.P.2    Dushek, O.3    van der Merwe, P.A.4
  • 142
    • 0033762433 scopus 로고    scopus 로고
    • Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition
    • Aivazian D, Stern LJ. Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition. Nat Struct Biol (2000) 7(11):1023-6. doi:10.1038/80930
    • (2000) Nat Struct Biol , vol.7 , Issue.11 , pp. 1023-1026
    • Aivazian, D.1    Stern, L.J.2
  • 143
    • 79959542722 scopus 로고    scopus 로고
    • The CD3 zeta subunit contains a phosphoinositide-binding motif that is required for the stable accumulation of TCR-CD3 complex at the immunological synapse
    • DeFord-Watts LM, Dougall DS, Belkaya S, Johnson BA, Eitson JL, Roybal KT, et al. The CD3 zeta subunit contains a phosphoinositide-binding motif that is required for the stable accumulation of TCR-CD3 complex at the immunological synapse. J Immunol (2011) 186(12):6839-47. doi:10.4049/jimmunol.1002721
    • (2011) J Immunol , vol.186 , Issue.12 , pp. 6839-6847
    • DeFord-Watts, L.M.1    Dougall, D.S.2    Belkaya, S.3    Johnson, B.A.4    Eitson, J.L.5    Roybal, K.T.6
  • 144
    • 55449138409 scopus 로고    scopus 로고
    • Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif
    • Xu C, Gagnon E, Call ME, Schnell JR, Schwieters CD, Carman CV, et al. Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif. Cell (2008) 135(4):702-13. doi:10.1016/j.cell.2008.09.044
    • (2008) Cell , vol.135 , Issue.4 , pp. 702-713
    • Xu, C.1    Gagnon, E.2    Call, M.E.3    Schnell, J.R.4    Schwieters, C.D.5    Carman, C.V.6
  • 145
    • 0037188899 scopus 로고    scopus 로고
    • Recruitment of Nck by CD3 epsilon reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation
    • Gil D, Schamel WW, Montoya M, Sanchez-Madrid F, Alarcon B. Recruitment of Nck by CD3 epsilon reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation. Cell (2002) 109(7):901-12. doi:10.1016/S0092-8674(02)00799-7
    • (2002) Cell , vol.109 , Issue.7 , pp. 901-912
    • Gil, D.1    Schamel, W.W.2    Montoya, M.3    Sanchez-Madrid, F.4    Alarcon, B.5
  • 146
    • 84896522148 scopus 로고    scopus 로고
    • Relevance of Nck-CD3 epsilon interaction for T cell activation in vivo
    • Borroto A, Arellano I, Blanco R, Fuentes M, Orfao A, Dopfer EP, et al. Relevance of Nck-CD3 epsilon interaction for T cell activation in vivo. J Immunol (2014) 192(5):2042-53. doi:10.4049/jimmunol.1203414
    • (2014) J Immunol , vol.192 , Issue.5 , pp. 2042-2053
    • Borroto, A.1    Arellano, I.2    Blanco, R.3    Fuentes, M.4    Orfao, A.5    Dopfer, E.P.6
  • 147
    • 84872723633 scopus 로고    scopus 로고
    • Nck recruitment to the TCR required for ZAP70 activation during thymic development
    • Borroto A, Arellano I, Dopfer EP, Prouza M, Suchanek M, Fuentes M, et al. Nck recruitment to the TCR required for ZAP70 activation during thymic development. J Immunol (2013) 190(3):1103-12. doi:10.4049/jimmunol.1202055
    • (2013) J Immunol , vol.190 , Issue.3 , pp. 1103-1112
    • Borroto, A.1    Arellano, I.2    Dopfer, E.P.3    Prouza, M.4    Suchanek, M.5    Fuentes, M.6
  • 148
    • 84878566800 scopus 로고    scopus 로고
    • WIP provides an essential link between Nck and N-WASP during Arp2/3-dependent actin polymerization
    • Donnelly SK, Weisswange I, Zettl M, Way M. WIP provides an essential link between Nck and N-WASP during Arp2/3-dependent actin polymerization. Curr Biol (2013) 23(11):999-1006. doi:10.1016/j.cub.2013.04.051
    • (2013) Curr Biol , vol.23 , Issue.11 , pp. 999-1006
    • Donnelly, S.K.1    Weisswange, I.2    Zettl, M.3    Way, M.4
  • 149
    • 0041845112 scopus 로고    scopus 로고
    • SLP-76 coordinates Nck-dependent Wiskott-Aldrich syndrome protein recruitment with Vav-1/Cdc42-dependent Wiskott-Aldrich syndrome protein activation at the T cell-APC contact site
    • Zeng R, Cannon JL, Abraham RT, Way M, Billadeau DD, Bubeck-Wardenberg J, et al. SLP-76 coordinates Nck-dependent Wiskott-Aldrich syndrome protein recruitment with Vav-1/Cdc42-dependent Wiskott-Aldrich syndrome protein activation at the T cell-APC contact site. J Immunol (2003) 171(3):1360-8. doi:10.4049/jimmunol.171.3.1360
    • (2003) J Immunol , vol.171 , Issue.3 , pp. 1360-1368
    • Zeng, R.1    Cannon, J.L.2    Abraham, R.T.3    Way, M.4    Billadeau, D.D.5    Bubeck-Wardenberg, J.6
  • 150
    • 84897386482 scopus 로고    scopus 로고
    • N-WASP-directed actin polymerization activates Cas phosphorylation and lamellipodium spreading
    • Zhang X, Moore SW, Iskratsch T, Sheetz MP. N-WASP-directed actin polymerization activates Cas phosphorylation and lamellipodium spreading. J Cell Sci (2014) 127(Pt 7):1394-405. doi:10.1242/jcs.134692
    • (2014) J Cell Sci , vol.127 , pp. 1394-1405
    • Zhang, X.1    Moore, S.W.2    Iskratsch, T.3    Sheetz, M.P.4
  • 151
    • 40149093643 scopus 로고    scopus 로고
    • Biophysics of catch bonds
    • Thomas WE, Vogel V, Sokurenko E. Biophysics of catch bonds. Annu Rev Biophys (2008) 37:399-416. doi:10.1146/annurev.biophys.37.032807.125804
    • (2008) Annu Rev Biophys , vol.37 , pp. 399-416
    • Thomas, W.E.1    Vogel, V.2    Sokurenko, E.3
  • 152
    • 70449555128 scopus 로고    scopus 로고
    • Immune synapse formation determines interaction forces between T cells and antigen-presenting cells measured by atomic force microscopy
    • Hosseini BH, Louban I, Djandji D, Wabnitz GH, Deeg J, Bulbuc N, et al. Immune synapse formation determines interaction forces between T cells and antigen-presenting cells measured by atomic force microscopy. Proc Natl Acad Sci U S A (2009) 106(42):17852-7. doi:10.1073/pnas.0905384106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.42 , pp. 17852-17857
    • Hosseini, B.H.1    Louban, I.2    Djandji, D.3    Wabnitz, G.H.4    Deeg, J.5    Bulbuc, N.6
  • 153
    • 79952311503 scopus 로고    scopus 로고
    • Single cell force spectroscopy of T cells recognizing a myelin-derived peptide on antigen presenting cells
    • Hoffmann S, Hosseini BH, Hecker M, Louban I, Bulbuc N, Garbi N, et al. Single cell force spectroscopy of T cells recognizing a myelin-derived peptide on antigen presenting cells. Immunol Lett (2011) 136(1):13-20. doi:10.1016/j.imlet.2010.11.005
    • (2011) Immunol Lett , vol.136 , Issue.1 , pp. 13-20
    • Hoffmann, S.1    Hosseini, B.H.2    Hecker, M.3    Louban, I.4    Bulbuc, N.5    Garbi, N.6
  • 154
    • 77955863885 scopus 로고    scopus 로고
    • Affinity, lateral mobility, and clustering contribute independently to beta 2-integrin-mediated adhesion
    • Yu T, Wu X, Gupta KB, Kucik DF. Affinity, lateral mobility, and clustering contribute independently to beta 2-integrin-mediated adhesion. Am J Physiol Cell Physiol (2010) 299(2):C399-410. doi:10.1152/ajpcell.00039.2009
    • (2010) Am J Physiol Cell Physiol , vol.299 , Issue.2 , pp. C399-C410
    • Yu, T.1    Wu, X.2    Gupta, K.B.3    Kucik, D.F.4
  • 155
    • 21844450244 scopus 로고    scopus 로고
    • Intracellular signalling controlling integrin activation in lymphocytes
    • Kinashi T. Intracellular signalling controlling integrin activation in lymphocytes. Nat Rev Immunol (2005) 5(7):546-59. doi:10.1038/nri1646
    • (2005) Nat Rev Immunol , vol.5 , Issue.7 , pp. 546-559
    • Kinashi, T.1
  • 156
    • 79957621253 scopus 로고    scopus 로고
    • The insider's guide to leukocyte integrin signalling and function
    • Hogg N, Patzak I, Willenbrock F. The insider's guide to leukocyte integrin signalling and function. Nat Rev Immunol (2011) 11(6):416-26. doi:10.1038/nri2986
    • (2011) Nat Rev Immunol , vol.11 , Issue.6 , pp. 416-426
    • Hogg, N.1    Patzak, I.2    Willenbrock, F.3
  • 157
    • 80053329700 scopus 로고    scopus 로고
    • Regulation of integrin activation
    • Kim C, Ye F, Ginsberg MH. Regulation of integrin activation. Annu Rev Cell Dev Biol (2011) 27:321-45. doi:10.1146/annurev-cellbio-100109-104104
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 321-345
    • Kim, C.1    Ye, F.2    Ginsberg, M.H.3
  • 158
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo BH, Carman CV, Springer TA. Structural basis of integrin regulation and signaling. Annu Rev Immunol (2007) 25:619-47. doi:10.1146/annurev.immunol.25.022106.141618
    • (2007) Annu Rev Immunol , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 159
    • 84857688656 scopus 로고    scopus 로고
    • Integrin inside-out signaling and the immunological synapse
    • Springer TA, Dustin ML. Integrin inside-out signaling and the immunological synapse. Curr Opin Cell Biol (2012) 24(1):107-15. doi:10.1016/j.ceb.2011.10.004
    • (2012) Curr Opin Cell Biol , vol.24 , Issue.1 , pp. 107-115
    • Springer, T.A.1    Dustin, M.L.2
  • 160
    • 84888440240 scopus 로고    scopus 로고
    • Integrating actin dynamics, mechanotransduction and integrin activation: the multiple functions of actin binding proteins in focal adhesions
    • Ciobanasu C, Faivre B, Le Clainche C. Integrating actin dynamics, mechanotransduction and integrin activation: the multiple functions of actin binding proteins in focal adhesions. Eur J Cell Biol (2013) 92(10-11):339-48. doi:10.1016/j.ejcb.2013.10.009
    • (2013) Eur J Cell Biol , vol.92 , Issue.10-11 , pp. 339-348
    • Ciobanasu, C.1    Faivre, B.2    Le Clainche, C.3
  • 161
    • 1642482866 scopus 로고    scopus 로고
    • Rap1-mediated lymphocyte function-associated antigen-1 activation by the T cell antigen receptor is dependent on phospholipase C-gamma1
    • Katagiri K, Shimonaka M, Kinashi T. Rap1-mediated lymphocyte function-associated antigen-1 activation by the T cell antigen receptor is dependent on phospholipase C-gamma1. J Biol Chem (2004) 279(12):11875-81. doi:10.1074/jbc.M310717200
    • (2004) J Biol Chem , vol.279 , Issue.12 , pp. 11875-11881
    • Katagiri, K.1    Shimonaka, M.2    Kinashi, T.3
  • 163
    • 36349034646 scopus 로고    scopus 로고
    • Essential role for Rap1 GTPase and its guanine exchange factor CalDAG-GEFI in LFA-1 but not VLA-4 integrin mediated human T-cell adhesion
    • Ghandour H, Cullere X, Alvarez A, Luscinskas FW, Mayadas TN. Essential role for Rap1 GTPase and its guanine exchange factor CalDAG-GEFI in LFA-1 but not VLA-4 integrin mediated human T-cell adhesion. Blood (2007) 110(10):3682-90. doi:10.1182/blood-2007-03-077628
    • (2007) Blood , vol.110 , Issue.10 , pp. 3682-3690
    • Ghandour, H.1    Cullere, X.2    Alvarez, A.3    Luscinskas, F.W.4    Mayadas, T.N.5
  • 164
    • 52249086931 scopus 로고    scopus 로고
    • The WAVE2 complex regulates T cell receptor signaling to integrins via Abl-and CrkL-C3G-mediated activation of Rap1
    • Nolz JC, Nacusi LP, Segovis CM, Medeiros RB, Mitchell JS, Shimizu Y, et al. The WAVE2 complex regulates T cell receptor signaling to integrins via Abl-and CrkL-C3G-mediated activation of Rap1. J Cell Biol (2008) 182(6):1231-44. doi:10.1083/jcb.200801121
    • (2008) J Cell Biol , vol.182 , Issue.6 , pp. 1231-1244
    • Nolz, J.C.1    Nacusi, L.P.2    Segovis, C.M.3    Medeiros, R.B.4    Mitchell, J.S.5    Shimizu, Y.6
  • 165
    • 64149100431 scopus 로고    scopus 로고
    • RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences
    • Lee HS, Lim CJ, Puzon-McLaughlin W, Shattil SJ, Ginsberg MH. RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences. J Biol Chem (2009) 284(8):5119-27. doi:10.1074/jbc.M807117200
    • (2009) J Biol Chem , vol.284 , Issue.8 , pp. 5119-5127
    • Lee, H.S.1    Lim, C.J.2    Puzon-McLaughlin, W.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 166
    • 33751578411 scopus 로고    scopus 로고
    • Talin1 regulates TCR-mediated LFA-1 function
    • Simonson WT, Franco SJ, Huttenlocher A. Talin1 regulates TCR-mediated LFA-1 function. J Immunol (2006) 177(11):7707-14. doi:10.4049/jimmunol.177.11.7707
    • (2006) J Immunol , vol.177 , Issue.11 , pp. 7707-7714
    • Simonson, W.T.1    Franco, S.J.2    Huttenlocher, A.3
  • 167
    • 0033213922 scopus 로고    scopus 로고
    • The talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation
    • Calderwood DA, Zent R, Grant R, Rees DJ, Hynes RO, Ginsberg MH. The talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation. J Biol Chem (1999) 274(40):28071-4. doi:10.1074/jbc.274.40.28071
    • (1999) J Biol Chem , vol.274 , Issue.40 , pp. 28071-28074
    • Calderwood, D.A.1    Zent, R.2    Grant, R.3    Rees, D.J.4    Hynes, R.O.5    Ginsberg, M.H.6
  • 168
    • 0029966310 scopus 로고    scopus 로고
    • Breaking the integrin hinge. A defined structural constraint regulates integrin signaling
    • Hughes PE, Diaz-Gonzalez F, Leong L, Wu C, McDonald JA, Shattil SJ, et al. Breaking the integrin hinge. A defined structural constraint regulates integrin signaling. J Biol Chem (1996) 271(12):6571-4.
    • (1996) J Biol Chem , vol.271 , Issue.12 , pp. 6571-6574
    • Hughes, P.E.1    Diaz-Gonzalez, F.2    Leong, L.3    Wu, C.4    McDonald, J.A.5    Shattil, S.J.6
  • 169
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M, Carman CV, Springer TA. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science (2003) 301(5640):1720-5. doi:10.1126/science.1084174
    • (2003) Science , vol.301 , Issue.5640 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 170
    • 0038644597 scopus 로고    scopus 로고
    • Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations
    • Li R, Mitra N, Gratkowski H, Vilaire G, Litvinov R, Nagasami C, et al. Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations. Science (2003) 300(5620):795-8. doi:10.1126/science.1079441
    • (2003) Science , vol.300 , Issue.5620 , pp. 795-798
    • Li, R.1    Mitra, N.2    Gratkowski, H.3    Vilaire, G.4    Litvinov, R.5    Nagasami, C.6
  • 171
    • 14844346910 scopus 로고    scopus 로고
    • Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering
    • Luo BH, Carman CV, Takagi J, Springer TA. Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering. Proc Natl Acad Sci U S A (2005) 102(10):3679-84. doi:10.1073/pnas.0409440102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.10 , pp. 3679-3684
    • Luo, B.H.1    Carman, C.V.2    Takagi, J.3    Springer, T.A.4
  • 172
    • 14844323604 scopus 로고    scopus 로고
    • Transmembrane domain helix packing stabilizes integrin alphaIIbbeta3 in the low affinity state
    • Partridge AW, Liu S, Kim S, Bowie JU, Ginsberg MH. Transmembrane domain helix packing stabilizes integrin alphaIIbbeta3 in the low affinity state. J Biol Chem (2005) 280(8):7294-300. doi:10.1074/jbc.M412701200
    • (2005) J Biol Chem , vol.280 , Issue.8 , pp. 7294-7300
    • Partridge, A.W.1    Liu, S.2    Kim, S.3    Bowie, J.U.4    Ginsberg, M.H.5
  • 173
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin beta tails: a final common step in integrin activation
    • Tadokoro S, Shattil SJ, Eto K, Tai V, Liddington RC, de Pereda JM, et al. Talin binding to integrin beta tails: a final common step in integrin activation. Science (2003) 302(5642):103-6. doi:10.1126/science.1086652
    • (2003) Science , vol.302 , Issue.5642 , pp. 103-106
    • Tadokoro, S.1    Shattil, S.J.2    Eto, K.3    Tai, V.4    Liddington, R.C.5    de Pereda, J.M.6
  • 174
    • 84862598504 scopus 로고    scopus 로고
    • Talin activates integrins by altering the topology of the beta transmembrane domain
    • Kim C, Ye F, Hu X, Ginsberg MH. Talin activates integrins by altering the topology of the beta transmembrane domain. J Cell Biol (2012) 197(5):605-11. doi:10.1083/jcb.201112141
    • (2012) J Cell Biol , vol.197 , Issue.5 , pp. 605-611
    • Kim, C.1    Ye, F.2    Hu, X.3    Ginsberg, M.H.4
  • 175
    • 82455189778 scopus 로고    scopus 로고
    • Regulation of integrin affinity on cell surfaces
    • Schurpf T, Springer TA. Regulation of integrin affinity on cell surfaces. EMBO J (2011) 30(23):4712-27. doi:10.1038/emboj.2011.333
    • (2011) EMBO J , vol.30 , Issue.23 , pp. 4712-4727
    • Schurpf, T.1    Springer, T.A.2
  • 176
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J, Petre BM, Walz T, Springer TA. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell (2002) 110(5):599-611. doi:10.1016/S0092-8674(02)00935-2
    • (2002) Cell , vol.110 , Issue.5 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 177
    • 33749522074 scopus 로고    scopus 로고
    • Activation of leukocyte beta2 integrins by conversion from bent to extended conformations
    • Nishida N, Xie C, Shimaoka M, Cheng Y, Walz T, Springer TA. Activation of leukocyte beta2 integrins by conversion from bent to extended conformations. Immunity (2006) 25(4):583-94. doi:10.1016/j.immuni.2006.07.016
    • (2006) Immunity , vol.25 , Issue.4 , pp. 583-594
    • Nishida, N.1    Xie, C.2    Shimaoka, M.3    Cheng, Y.4    Walz, T.5    Springer, T.A.6
  • 178
    • 34548241344 scopus 로고    scopus 로고
    • The cytosolic protein talin induces an intermediate affinity integrin alphaLbeta2
    • Li YF, Tang RH, Puan KJ, Law SK, Tan SM. The cytosolic protein talin induces an intermediate affinity integrin alphaLbeta2. J Biol Chem (2007) 282(33):24310-9. doi:10.1074/jbc.M701860200
    • (2007) J Biol Chem , vol.282 , Issue.33 , pp. 24310-24319
    • Li, Y.F.1    Tang, R.H.2    Puan, K.J.3    Law, S.K.4    Tan, S.M.5
  • 179
    • 79959858924 scopus 로고    scopus 로고
    • Kindlin-3 is required for the stabilization of TCR-stimulated LFA-1:ICAM-1 bonds critical for lymphocyte arrest and spreading on dendritic cells
    • Feigelson SW, Grabovsky V, Manevich-Mendelson E, Pasvolsky R, Shulman Z, Shinder V, et al. Kindlin-3 is required for the stabilization of TCR-stimulated LFA-1:ICAM-1 bonds critical for lymphocyte arrest and spreading on dendritic cells. Blood (2011) 117(26):7042-52. doi:10.1182/blood-2010-12-322859
    • (2011) Blood , vol.117 , Issue.26 , pp. 7042-7052
    • Feigelson, S.W.1    Grabovsky, V.2    Manevich-Mendelson, E.3    Pasvolsky, R.4    Shulman, Z.5    Shinder, V.6
  • 180
    • 0029913643 scopus 로고    scopus 로고
    • Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes
    • Kucik DF, Dustin ML, Miller JM, Brown EJ. Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. J Clin Invest (1996) 97(9):2139-44. doi:10.1172/JCI118651
    • (1996) J Clin Invest , vol.97 , Issue.9 , pp. 2139-2144
    • Kucik, D.F.1    Dustin, M.L.2    Miller, J.M.3    Brown, E.J.4
  • 181
    • 0035971155 scopus 로고    scopus 로고
    • A single amino acid in the cytoplasmic domain of the beta 2 integrin lymphocyte function-associated antigen-1 regulates avidity-dependent inside-out signaling
    • Bleijs DA, van Duijnhoven GC, van Vliet SJ, Thijssen JP, Figdor CG, van Kooyk Y. A single amino acid in the cytoplasmic domain of the beta 2 integrin lymphocyte function-associated antigen-1 regulates avidity-dependent inside-out signaling. J Biol Chem (2001) 276(13):10338-46. doi:10.1074/jbc.M008967200
    • (2001) J Biol Chem , vol.276 , Issue.13 , pp. 10338-10346
    • Bleijs, D.A.1    van Duijnhoven, G.C.2    van Vliet, S.J.3    Thijssen, J.P.4    Figdor, C.G.5    van Kooyk, Y.6
  • 182
    • 0032498543 scopus 로고    scopus 로고
    • LFA-1-mediated adhesion is regulated by cytoskeletal restraint and by a Ca2+-dependent protease, calpain
    • Stewart MP, McDowall A, Hogg N. LFA-1-mediated adhesion is regulated by cytoskeletal restraint and by a Ca2+-dependent protease, calpain. J Cell Biol (1998) 140(3):699-707. doi:10.1083/jcb.140.3.699
    • (1998) J Cell Biol , vol.140 , Issue.3 , pp. 699-707
    • Stewart, M.P.1    McDowall, A.2    Hogg, N.3
  • 184
    • 11244274075 scopus 로고    scopus 로고
    • The primacy of affinity over clustering in regulation of adhesiveness of the integrin {alpha}L{beta}2
    • Kim M, Carman CV, Yang W, Salas A, Springer TA. The primacy of affinity over clustering in regulation of adhesiveness of the integrin {alpha}L{beta}2. J Cell Biol (2004) 167(6):1241-53. doi:10.1083/jcb.200404160
    • (2004) J Cell Biol , vol.167 , Issue.6 , pp. 1241-1253
    • Kim, M.1    Carman, C.V.2    Yang, W.3    Salas, A.4    Springer, T.A.5
  • 185
    • 38049136514 scopus 로고    scopus 로고
    • Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells
    • Kaizuka Y, Douglass AD, Varma R, Dustin ML, Vale RD. Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells. Proc Natl Acad Sci U S A (2007) 104(51):20296-301. doi:10.1073/pnas.0710258105
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.51 , pp. 20296-20301
    • Kaizuka, Y.1    Douglass, A.D.2    Varma, R.3    Dustin, M.L.4    Vale, R.D.5
  • 186
    • 0037428080 scopus 로고    scopus 로고
    • Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation
    • Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, et al. Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation. Cell (2003) 112(1):99-111. doi:10.1016/S0092-8674(02)01257-6
    • (2003) Cell , vol.112 , Issue.1 , pp. 99-111
    • Shimaoka, M.1    Xiao, T.2    Liu, J.H.3    Yang, Y.4    Dong, Y.5    Jun, C.D.6
  • 187
    • 82755162374 scopus 로고    scopus 로고
    • The C-terminal alphaI domain linker as a critical structural element in the conformational activation of alphaI integrins
    • Weitz-Schmidt G, Schurpf T, Springer TA. The C-terminal alphaI domain linker as a critical structural element in the conformational activation of alphaI integrins. J Biol Chem (2011) 286(49):42115-22. doi:10.1074/jbc.M111.282830
    • (2011) J Biol Chem , vol.286 , Issue.49 , pp. 42115-42122
    • Weitz-Schmidt, G.1    Schurpf, T.2    Springer, T.A.3
  • 188
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • Zhu J, Luo BH, Xiao T, Zhang C, Nishida N, Springer TA. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol Cell (2008) 32(6):849-61. doi:10.1016/j.molcel.2008.11.018
    • (2008) Mol Cell , vol.32 , Issue.6 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6
  • 189
    • 84880008208 scopus 로고    scopus 로고
    • Complete integrin headpiece opening in eight steps
    • Zhu J, Zhu J, Springer TA. Complete integrin headpiece opening in eight steps. J Cell Biol (2013) 201(7):1053-68. doi:10.1083/jcb.201212037
    • (2013) J Cell Biol , vol.201 , Issue.7 , pp. 1053-1068
    • Zhu, J.1    Zhu, J.2    Springer, T.A.3
  • 190
    • 77957034686 scopus 로고    scopus 로고
    • Requirement of open headpiece conformation for activation of leukocyte integrin alphaXbeta2
    • Chen X, Xie C, Nishida N, Li Z, Walz T, Springer TA. Requirement of open headpiece conformation for activation of leukocyte integrin alphaXbeta2. Proc Natl Acad Sci U S A (2010) 107(33):14727-32. doi:10.1073/pnas.1008663107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.33 , pp. 14727-14732
    • Chen, X.1    Xie, C.2    Nishida, N.3    Li, Z.4    Walz, T.5    Springer, T.A.6
  • 191
    • 79952477290 scopus 로고    scopus 로고
    • Molecular dynamics simulations of forced unbending of integrin alpha(v)beta(3)
    • Chen W, Lou J, Hsin J, Schulten K, Harvey SC, Zhu C. Molecular dynamics simulations of forced unbending of integrin alpha(v)beta(3). PLoS Comput Biol (2011) 7(2):e1001086. doi:10.1371/journal.pcbi.1001086
    • (2011) PLoS Comput Biol , vol.7 , Issue.2
    • Chen, W.1    Lou, J.2    Hsin, J.3    Schulten, K.4    Harvey, S.C.5    Zhu, C.6
  • 192
    • 33747091892 scopus 로고    scopus 로고
    • Cytoskeletal regulation couples LFA-1 conformational changes to receptor lateral mobility and clustering
    • Cairo CW, Mirchev R, Golan DE. Cytoskeletal regulation couples LFA-1 conformational changes to receptor lateral mobility and clustering. Immunity (2006) 25(2):297-308. doi:10.1016/j.immuni.2006.06.012
    • (2006) Immunity , vol.25 , Issue.2 , pp. 297-308
    • Cairo, C.W.1    Mirchev, R.2    Golan, D.E.3
  • 193
    • 84924655493 scopus 로고    scopus 로고
    • F-actin flow drives affinity maturation and spatial organization of LFA-1 at the immunological synapse
    • Comrie WA, Babich A, Burkhardt JK. F-actin flow drives affinity maturation and spatial organization of LFA-1 at the immunological synapse. J Cell Biol (2015) 208(4):475-91. doi:10.1083/jcb.201406121
    • (2015) J Cell Biol , vol.208 , Issue.4 , pp. 475-491
    • Comrie, W.A.1    Babich, A.2    Burkhardt, J.K.3
  • 194
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • Kong F, Garcia AJ, Mould AP, Humphries MJ, Zhu C. Demonstration of catch bonds between an integrin and its ligand. J Cell Biol (2009) 185(7):1275-84. doi:10.1083/jcb.200810002
    • (2009) J Cell Biol , vol.185 , Issue.7 , pp. 1275-1284
    • Kong, F.1    Garcia, A.J.2    Mould, A.P.3    Humphries, M.J.4    Zhu, C.5
  • 195
    • 84869127061 scopus 로고    scopus 로고
    • Observing force-regulated conformational changes and ligand dissociation from a single integrin on cells
    • Chen W, Lou J, Evans EA, Zhu C. Observing force-regulated conformational changes and ligand dissociation from a single integrin on cells. J Cell Biol (2012) 199(3):497-512. doi:10.1083/jcb.201201091
    • (2012) J Cell Biol , vol.199 , Issue.3 , pp. 497-512
    • Chen, W.1    Lou, J.2    Evans, E.A.3    Zhu, C.4
  • 196
    • 78149245953 scopus 로고    scopus 로고
    • Forcing switch from short-to intermediate-and long-lived states of the alphaA domain generates LFA-1/ICAM-1 catch bonds
    • Chen W, Lou J, Zhu C. Forcing switch from short-to intermediate-and long-lived states of the alphaA domain generates LFA-1/ICAM-1 catch bonds. J Biol Chem (2010) 285(46):35967-78. doi:10.1074/jbc.M110.155770
    • (2010) J Biol Chem , vol.285 , Issue.46 , pp. 35967-35978
    • Chen, W.1    Lou, J.2    Zhu, C.3
  • 197
    • 50249122663 scopus 로고    scopus 로고
    • Catch bonds in adhesion
    • Thomas W. Catch bonds in adhesion. Annu Rev Biomed Eng (2008) 10:39-57. doi:10.1146/annurev.bioeng.10.061807.160427
    • (2008) Annu Rev Biomed Eng , vol.10 , pp. 39-57
    • Thomas, W.1
  • 198
    • 84875803668 scopus 로고    scopus 로고
    • Cyclic mechanical reinforcement of integrin-ligand interactions
    • Kong F, Li Z, Parks WM, Dumbauld DW, Garcia AJ, Mould AP, et al. Cyclic mechanical reinforcement of integrin-ligand interactions. Mol Cell (2013) 49(6):1060-8. doi:10.1016/j.molcel.2013.01.015
    • (2013) Mol Cell , vol.49 , Issue.6 , pp. 1060-1068
    • Kong, F.1    Li, Z.2    Parks, W.M.3    Dumbauld, D.W.4    Garcia, A.J.5    Mould, A.P.6
  • 199
    • 84869102195 scopus 로고    scopus 로고
    • Finding the weakest link: exploring integrin-mediated mechanical molecular pathways
    • Roca-Cusachs P, Iskratsch T, Sheetz MP. Finding the weakest link: exploring integrin-mediated mechanical molecular pathways. J Cell Sci (2012) 125(Pt 13):3025-38. doi:10.1242/jcs.095794
    • (2012) J Cell Sci , vol.125 , pp. 3025-3038
    • Roca-Cusachs, P.1    Iskratsch, T.2    Sheetz, M.P.3
  • 201
    • 84898491914 scopus 로고    scopus 로고
    • Force-dependent vinculin binding to talin in live cells: a crucial step in anchoring the actin cytoskeleton to focal adhesions
    • Hirata H, Tatsumi H, Lim CT, Sokabe M. Force-dependent vinculin binding to talin in live cells: a crucial step in anchoring the actin cytoskeleton to focal adhesions. Am J Physiol Cell Physiol (2014) 306(6):C607-20. doi:10.1152/ajpcell.00122.2013
    • (2014) Am J Physiol Cell Physiol , vol.306 , Issue.6 , pp. C607-C620
    • Hirata, H.1    Tatsumi, H.2    Lim, C.T.3    Sokabe, M.4
  • 202
    • 0027956825 scopus 로고
    • Characterization of an F-actin-binding domain in the cytoskeletal protein vinculin
    • Menkel AR, Kroemker M, Bubeck P, Ronsiek M, Nikolai G, Jockusch BM. Characterization of an F-actin-binding domain in the cytoskeletal protein vinculin. J Cell Biol (1994) 126(5):1231-40. doi:10.1083/jcb.126.5.1231
    • (1994) J Cell Biol , vol.126 , Issue.5 , pp. 1231-1240
    • Menkel, A.R.1    Kroemker, M.2    Bubeck, P.3    Ronsiek, M.4    Nikolai, G.5    Jockusch, B.M.6
  • 203
    • 84855163922 scopus 로고    scopus 로고
    • Mechanotransduction in vivo by repeated talin stretch-relaxation events depends upon vinculin
    • Margadant F, Chew LL, Hu X, Yu H, Bate N, Zhang X, et al. Mechanotransduction in vivo by repeated talin stretch-relaxation events depends upon vinculin. PLoS Biol (2011) 9(12):e1001223. doi:10.1371/journal.pbio.1001223
    • (2011) PLoS Biol , vol.9 , Issue.12
    • Margadant, F.1    Chew, L.L.2    Hu, X.3    Yu, H.4    Bate, N.5    Zhang, X.6
  • 204
    • 84898457452 scopus 로고    scopus 로고
    • Actomyosin-dependent formation of the mechanosensitive talin-vinculin complex reinforces actin anchoring
    • Ciobanasu C, Faivre B, Le Clainche C. Actomyosin-dependent formation of the mechanosensitive talin-vinculin complex reinforces actin anchoring. Nat Commun (2014) 5:3095. doi:10.1038/ncomms4095
    • (2014) Nat Commun , vol.5 , pp. 3095
    • Ciobanasu, C.1    Faivre, B.2    Le Clainche, C.3
  • 205
    • 84878541453 scopus 로고    scopus 로고
    • Mechanosensitivity and compositional dynamics of cell-matrix adhesions
    • Schiller HB, Fassler R. Mechanosensitivity and compositional dynamics of cell-matrix adhesions. EMBO Rep (2013) 14(6):509-19. doi:10.1038/embor.2013.49
    • (2013) EMBO Rep , vol.14 , Issue.6 , pp. 509-519
    • Schiller, H.B.1    Fassler, R.2
  • 206
    • 34548259213 scopus 로고    scopus 로고
    • WAVE2 regulates high-affinity integrin binding by recruiting vinculin and talin to the immunological synapse
    • Nolz JC, Medeiros RB, Mitchell JS, Zhu P, Freedman BD, Shimizu Y, et al. WAVE2 regulates high-affinity integrin binding by recruiting vinculin and talin to the immunological synapse. Mol Cell Biol (2007) 27(17):5986-6000. doi:10.1128/MCB.00136-07
    • (2007) Mol Cell Biol , vol.27 , Issue.17 , pp. 5986-6000
    • Nolz, J.C.1    Medeiros, R.B.2    Mitchell, J.S.3    Zhu, P.4    Freedman, B.D.5    Shimizu, Y.6
  • 207
    • 67649814709 scopus 로고    scopus 로고
    • LFA-1 affinity regulation is necessary for the activation and proliferation of naive T cells
    • Wang Y, Li D, Nurieva R, Yang J, Sen M, Carreno R, et al. LFA-1 affinity regulation is necessary for the activation and proliferation of naive T cells. J Biol Chem (2009) 284(19):12645-53. doi:10.1074/jbc.M807207200
    • (2009) J Biol Chem , vol.284 , Issue.19 , pp. 12645-12653
    • Wang, Y.1    Li, D.2    Nurieva, R.3    Yang, J.4    Sen, M.5    Carreno, R.6
  • 208
    • 34948882323 scopus 로고    scopus 로고
    • Requirement of alpha and beta subunit transmembrane helix separation for integrin outside-in signaling
    • Zhu J, Carman CV, Kim M, Shimaoka M, Springer TA, Luo BH. Requirement of alpha and beta subunit transmembrane helix separation for integrin outside-in signaling. Blood (2007) 110(7):2475-83. doi:10.1182/blood-2007-03-080077
    • (2007) Blood , vol.110 , Issue.7 , pp. 2475-2483
    • Zhu, J.1    Carman, C.V.2    Kim, M.3    Shimaoka, M.4    Springer, T.A.5    Luo, B.H.6
  • 209
    • 0028351807 scopus 로고
    • Serine phosphorylation of a 67-kDa protein in human T lymphocytes represents an accessory receptor-mediated signaling event
    • Henning SW, Meuer SC, Samstag Y. Serine phosphorylation of a 67-kDa protein in human T lymphocytes represents an accessory receptor-mediated signaling event. J Immunol (1994) 152(10):4808-15.
    • (1994) J Immunol , vol.152 , Issue.10 , pp. 4808-4815
    • Henning, S.W.1    Meuer, S.C.2    Samstag, Y.3
  • 210
    • 33749147602 scopus 로고    scopus 로고
    • A large T cell invagination with CD2 enrichment resets receptor engagement in the immunological synapse
    • Singleton K, Parvaze N, Dama KR, Chen KS, Jennings P, Purtic B, et al. A large T cell invagination with CD2 enrichment resets receptor engagement in the immunological synapse. J Immunol (2006) 177(7):4402-13. doi:10.4049/jimmunol.177.7.4402
    • (2006) J Immunol , vol.177 , Issue.7 , pp. 4402-4413
    • Singleton, K.1    Parvaze, N.2    Dama, K.R.3    Chen, K.S.4    Jennings, P.5    Purtic, B.6
  • 211
    • 34147144013 scopus 로고    scopus 로고
    • Costimulation induced phosphorylation of L-plastin facilitates surface transport of the T cell activation molecules CD69 and CD25
    • Wabnitz GH, Kocher T, Lohneis P, Stober C, Konstandin MH, Funk B, et al. Costimulation induced phosphorylation of L-plastin facilitates surface transport of the T cell activation molecules CD69 and CD25. Eur J Immunol (2007) 37(3):649-62. doi:10.1002/eji.200636320
    • (2007) Eur J Immunol , vol.37 , Issue.3 , pp. 649-662
    • Wabnitz, G.H.1    Kocher, T.2    Lohneis, P.3    Stober, C.4    Konstandin, M.H.5    Funk, B.6
  • 212
    • 54949103906 scopus 로고    scopus 로고
    • Spatiotemporal regulation of T cell costimulation by TCR-CD28 microclusters and protein kinase C theta translocation
    • Yokosuka T, Kobayashi W, Sakata-Sogawa K, Takamatsu M, Hashimoto-Tane A, Dustin ML, et al. Spatiotemporal regulation of T cell costimulation by TCR-CD28 microclusters and protein kinase C theta translocation. Immunity (2008) 29(4):589-601. doi:10.1016/j.immuni.2008.08.011
    • (2008) Immunity , vol.29 , Issue.4 , pp. 589-601
    • Yokosuka, T.1    Kobayashi, W.2    Sakata-Sogawa, K.3    Takamatsu, M.4    Hashimoto-Tane, A.5    Dustin, M.L.6
  • 213
    • 84866350356 scopus 로고    scopus 로고
    • CD80 and CD86 differentially regulate mechanical interactions of T-cells with antigen-presenting dendritic cells and B-cells
    • Lim TS, Goh JK, Mortellaro A, Lim CT, Hammerling GJ, Ricciardi-Castagnoli P. CD80 and CD86 differentially regulate mechanical interactions of T-cells with antigen-presenting dendritic cells and B-cells. PLoS One (2012) 7(9):e45185. doi:10.1371/journal.pone.0045185
    • (2012) PLoS One , vol.7 , Issue.9
    • Lim, T.S.1    Goh, J.K.2    Mortellaro, A.3    Lim, C.T.4    Hammerling, G.J.5    Ricciardi-Castagnoli, P.6
  • 214
    • 33750533178 scopus 로고    scopus 로고
    • CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse
    • Tavano R, Contento RL, Baranda SJ, Soligo M, Tuosto L, Manes S, et al. CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. Nat Cell Biol (2006) 8(11):1270-6. doi:10.1038/ncb1492
    • (2006) Nat Cell Biol , vol.8 , Issue.11 , pp. 1270-1276
    • Tavano, R.1    Contento, R.L.2    Baranda, S.J.3    Soligo, M.4    Tuosto, L.5    Manes, S.6
  • 215
    • 78650858755 scopus 로고    scopus 로고
    • Filamin A mediates interactions between cytoskeletal proteins that control cell adhesion
    • Kim H, McCulloch CA. Filamin A mediates interactions between cytoskeletal proteins that control cell adhesion. FEBS Lett (2011) 585(1):18-22. doi:10.1016/j.febslet.2010.11.033
    • (2011) FEBS Lett , vol.585 , Issue.1 , pp. 18-22
    • Kim, H.1    McCulloch, C.A.2
  • 216
  • 217
    • 80054043810 scopus 로고    scopus 로고
    • Mechanical strain in actin networks regulates FilGAP and integrin binding to filamin A
    • Ehrlicher AJ, Nakamura F, Hartwig JH, Weitz DA, Stossel TP. Mechanical strain in actin networks regulates FilGAP and integrin binding to filamin A. Nature (2011) 478(7368):260-3. doi:10.1038/nature10430
    • (2011) Nature , vol.478 , Issue.7368 , pp. 260-263
    • Ehrlicher, A.J.1    Nakamura, F.2    Hartwig, J.H.3    Weitz, D.A.4    Stossel, T.P.5
  • 218
    • 81855224596 scopus 로고    scopus 로고
    • Cellular mechanotransduction: filamin A strains to regulate motility
    • Lynch CD, Sheetz MP. Cellular mechanotransduction: filamin A strains to regulate motility. Curr Biol (2011) 21(22):R916-8. doi:10.1016/j.cub.2011.10.020
    • (2011) Curr Biol , vol.21 , Issue.22 , pp. R916-R918
    • Lynch, C.D.1    Sheetz, M.P.2
  • 219
    • 33751335857 scopus 로고    scopus 로고
    • Force sensing by mechanical extension of the Src family kinase substrate p130Cas
    • Sawada Y, Tamada M, Dubin-Thaler BJ, Cherniavskaya O, Sakai R, Tanaka S, et al. Force sensing by mechanical extension of the Src family kinase substrate p130Cas. Cell (2006) 127(5):1015-26. doi:10.1016/j.cell.2006.09.044
    • (2006) Cell , vol.127 , Issue.5 , pp. 1015-1026
    • Sawada, Y.1    Tamada, M.2    Dubin-Thaler, B.J.3    Cherniavskaya, O.4    Sakai, R.5    Tanaka, S.6
  • 220
    • 7744232293 scopus 로고    scopus 로고
    • Activation of a signaling cascade by cytoskeleton stretch
    • Tamada M, Sheetz MP, Sawada Y. Activation of a signaling cascade by cytoskeleton stretch. Dev Cell (2004) 7(5):709-18. doi:10.1016/j.devcel.2004.08.021
    • (2004) Dev Cell , vol.7 , Issue.5 , pp. 709-718
    • Tamada, M.1    Sheetz, M.P.2    Sawada, Y.3
  • 221
    • 84863040809 scopus 로고    scopus 로고
    • Myosin IIA modulates T cell receptor transport and CasL phosphorylation during early immunological synapse formation
    • Yu Y, Fay NC, Smoligovets AA, Wu HJ, Groves JT. Myosin IIA modulates T cell receptor transport and CasL phosphorylation during early immunological synapse formation. PLoS One (2012) 7(2):e30704. doi:10.1371/journal.pone.0030704
    • (2012) PLoS One , vol.7 , Issue.2
    • Yu, Y.1    Fay, N.C.2    Smoligovets, A.A.3    Wu, H.J.4    Groves, J.T.5
  • 222
    • 84874207192 scopus 로고    scopus 로고
    • T lymphocyte myosin IIA is required for maturation of the immunological synapse
    • Kumari S, Vardhana S, Cammer M, Curado S, Santos L, Sheetz MP, et al. T lymphocyte myosin IIA is required for maturation of the immunological synapse. Front Immunol (2012) 3:230. doi:10.3389/fimmu.2012.00230
    • (2012) Front Immunol , vol.3 , pp. 230
    • Kumari, S.1    Vardhana, S.2    Cammer, M.3    Curado, S.4    Santos, L.5    Sheetz, M.P.6
  • 223
    • 84877946982 scopus 로고    scopus 로고
    • Defining single molecular forces required to activate integrin and notch signaling
    • Wang X, Ha T. Defining single molecular forces required to activate integrin and notch signaling. Science (2013) 340(6135):991-4. doi:10.1126/science.1231041
    • (2013) Science , vol.340 , Issue.6135 , pp. 991-994
    • Wang, X.1    Ha, T.2
  • 224
    • 84888437737 scopus 로고    scopus 로고
    • Mechanical perturbation of filamin A immunoglobulin repeats 20-21 reveals potential non-equilibrium mechanochemical partner binding function
    • Chen H, Chandrasekar S, Sheetz MP, Stossel TP, Nakamura F, Yan J. Mechanical perturbation of filamin A immunoglobulin repeats 20-21 reveals potential non-equilibrium mechanochemical partner binding function. Sci Rep (2013) 3:1642. doi:10.1038/srep01642
    • (2013) Sci Rep , vol.3 , pp. 1642
    • Chen, H.1    Chandrasekar, S.2    Sheetz, M.P.3    Stossel, T.P.4    Nakamura, F.5    Yan, J.6
  • 225
    • 84898467976 scopus 로고    scopus 로고
    • Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation
    • Yao M, Goult BT, Chen H, Cong P, Sheetz MP, Yan J. Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation. Sci Rep (2014) 4:4610. doi:10.1038/srep04610
    • (2014) Sci Rep , vol.4 , pp. 4610
    • Yao, M.1    Goult, B.T.2    Chen, H.3    Cong, P.4    Sheetz, M.P.5    Yan, J.6
  • 226
    • 33745431529 scopus 로고    scopus 로고
    • T cell-dendritic cell immunological synapses
    • Dustin ML, Tseng SY, Varma R, Campi G. T cell-dendritic cell immunological synapses. Curr Opin Immunol (2006) 18(4):512-6. doi:10.1016/j.coi.2006.05.017
    • (2006) Curr Opin Immunol , vol.18 , Issue.4 , pp. 512-516
    • Dustin, M.L.1    Tseng, S.Y.2    Varma, R.3    Campi, G.4
  • 227
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: a molecular machine controlling T cell activation
    • Grakoui A, Bromley SK, Sumen C, Davis MM, Shaw AS, Allen PM, et al. The immunological synapse: a molecular machine controlling T cell activation. Science (1999) 285(5425):221-7. doi:10.1126/science.285.5425.221
    • (1999) Science , vol.285 , Issue.5425 , pp. 221-227
    • Grakoui, A.1    Bromley, S.K.2    Sumen, C.3    Davis, M.M.4    Shaw, A.S.5    Allen, P.M.6
  • 228
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks CR, Freiberg BA, Kupfer H, Sciaky N, Kupfer A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature (1998) 395(6697):82-6. doi:10.1038/25764
    • (1998) Nature , vol.395 , Issue.6697 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 230
    • 0142242134 scopus 로고    scopus 로고
    • Cutting edge: dendritic cell actin cytoskeletal polarization during immunological synapse formation is highly antigen-dependent
    • Al-Alwan MM, Liwski RS, Haeryfar SM, Baldridge WH, Hoskin DW, Rowden G, et al. Cutting edge: dendritic cell actin cytoskeletal polarization during immunological synapse formation is highly antigen-dependent. J Immunol (2003) 171(9):4479-83. doi:10.4049/jimmunol.171.9.4479
    • (2003) J Immunol , vol.171 , Issue.9 , pp. 4479-4483
    • Al-Alwan, M.M.1    Liwski, R.S.2    Haeryfar, S.M.3    Baldridge, W.H.4    Hoskin, D.W.5    Rowden, G.6
  • 231
    • 0035253596 scopus 로고    scopus 로고
    • The dendritic cell cytoskeleton is critical for the formation of the immunological synapse
    • Al-Alwan MM, Rowden G, Lee TD, West KA. The dendritic cell cytoskeleton is critical for the formation of the immunological synapse. J Immunol (2001) 166(3):1452-6. doi:10.4049/jimmunol.166.3.1452
    • (2001) J Immunol , vol.166 , Issue.3 , pp. 1452-1456
    • Al-Alwan, M.M.1    Rowden, G.2    Lee, T.D.3    West, K.A.4
  • 232
    • 4143132014 scopus 로고    scopus 로고
    • Requirement of Rac1 and Rac2 expression by mature dendritic cells for T cell priming
    • Benvenuti F, Hugues S, Walmsley M, Ruf S, Fetler L, Popoff M, et al. Requirement of Rac1 and Rac2 expression by mature dendritic cells for T cell priming. Science (2004) 305(5687):1150-3. doi:10.1126/science.1099159
    • (2004) Science , vol.305 , Issue.5687 , pp. 1150-1153
    • Benvenuti, F.1    Hugues, S.2    Walmsley, M.3    Ruf, S.4    Fetler, L.5    Popoff, M.6
  • 233
    • 33845593313 scopus 로고    scopus 로고
    • Structure and duration of contact between dendritic cells and T cells are controlled by T cell activation state
    • Rothoeft T, Balkow S, Krummen M, Beissert S, Varga G, Loser K, et al. Structure and duration of contact between dendritic cells and T cells are controlled by T cell activation state. Eur J Immunol (2006) 36(12):3105-17. doi:10.1002/eji.200636145
    • (2006) Eur J Immunol , vol.36 , Issue.12 , pp. 3105-3117
    • Rothoeft, T.1    Balkow, S.2    Krummen, M.3    Beissert, S.4    Varga, G.5    Loser, K.6
  • 234
    • 33749147817 scopus 로고    scopus 로고
    • Cutting edge: rho activation and actin polarization are dependent on plexin-A1 in dendritic cells
    • Eun SY, O'Connor BP, Wong AW, van Deventer HW, Taxman DJ, Reed W, et al. Cutting edge: rho activation and actin polarization are dependent on plexin-A1 in dendritic cells. J Immunol (2006) 177(7):4271-5. doi:10.4049/jimmunol.177.7.4271
    • (2006) J Immunol , vol.177 , Issue.7 , pp. 4271-4275
    • Eun, S.Y.1    O'Connor, B.P.2    Wong, A.W.3    van Deventer, H.W.4    Taxman, D.J.5    Reed, W.6
  • 235
    • 80052408047 scopus 로고    scopus 로고
    • Cytoskeletal remodeling mediated by WASp in dendritic cells is necessary for normal immune synapse formation and T-cell priming
    • Bouma G, Mendoza-Naranjo A, Blundell MP, de Falco E, Parsley KL, Burns SO, et al. Cytoskeletal remodeling mediated by WASp in dendritic cells is necessary for normal immune synapse formation and T-cell priming. Blood (2011) 118(9):2492-501. doi:10.1182/blood-2011-03-340265
    • (2011) Blood , vol.118 , Issue.9 , pp. 2492-2501
    • Bouma, G.1    Mendoza-Naranjo, A.2    Blundell, M.P.3    de Falco, E.4    Parsley, K.L.5    Burns, S.O.6
  • 236
    • 49049103195 scopus 로고    scopus 로고
    • Expression of Wiskott-Aldrich syndrome protein in dendritic cells regulates synapse formation and activation of naive CD8+ T cells
    • Pulecio J, Tagliani E, Scholer A, Prete F, Fetler L, Burrone OR, et al. Expression of Wiskott-Aldrich syndrome protein in dendritic cells regulates synapse formation and activation of naive CD8+ T cells. J Immunol (2008) 181(2):1135-42. doi:10.4049/jimmunol.181.2.1135
    • (2008) J Immunol , vol.181 , Issue.2 , pp. 1135-1142
    • Pulecio, J.1    Tagliani, E.2    Scholer, A.3    Prete, F.4    Fetler, L.5    Burrone, O.R.6
  • 237
    • 0033778649 scopus 로고    scopus 로고
    • Expression of the actin-bundling protein fascin in cultured human dendritic cells correlates with dendritic morphology and cell differentiation
    • Ross R, Jonuleit H, Bros M, Ross XL, Yamashiro S, Matsumura F, et al. Expression of the actin-bundling protein fascin in cultured human dendritic cells correlates with dendritic morphology and cell differentiation. J Invest Dermatol (2000) 115(4):658-63. doi:10.1046/j.1523-1747.2000.00112.x
    • (2000) J Invest Dermatol , vol.115 , Issue.4 , pp. 658-663
    • Ross, R.1    Jonuleit, H.2    Bros, M.3    Ross, X.L.4    Yamashiro, S.5    Matsumura, F.6
  • 238
    • 0042591370 scopus 로고    scopus 로고
    • The human fascin gene promoter is highly active in mature dendritic cells due to a stage-specific enhancer
    • Bros M, Ross XL, Pautz A, Reske-Kunz AB, Ross R. The human fascin gene promoter is highly active in mature dendritic cells due to a stage-specific enhancer. J Immunol (2003) 171(4):1825-34. doi:10.4049/jimmunol.171.4.1825
    • (2003) J Immunol , vol.171 , Issue.4 , pp. 1825-1834
    • Bros, M.1    Ross, X.L.2    Pautz, A.3    Reske-Kunz, A.B.4    Ross, R.5
  • 239
    • 1642554817 scopus 로고    scopus 로고
    • Morphological changes during dendritic cell maturation correlate with cofilin activation and translocation to the cell membrane
    • Verdijk P, van Veelen PA, de Ru AH, Hensbergen PJ, Mizuno K, Koerten HK, et al. Morphological changes during dendritic cell maturation correlate with cofilin activation and translocation to the cell membrane. Eur J Immunol (2004) 34(1):156-64. doi:10.1002/eji.200324241
    • (2004) Eur J Immunol , vol.34 , Issue.1 , pp. 156-164
    • Verdijk, P.1    van Veelen, P.A.2    de Ru, A.H.3    Hensbergen, P.J.4    Mizuno, K.5    Koerten, H.K.6
  • 240
    • 84924668103 scopus 로고    scopus 로고
    • The dendritic cell cytoskeleton promotes T cell adhesion and activation by constraining ICAM-1 mobility
    • Comrie WA, Li S, Boyle S, Burkhardt JK. The dendritic cell cytoskeleton promotes T cell adhesion and activation by constraining ICAM-1 mobility. J Cell Biol (2015) 208(4):457-73. doi:10.1083/jcb.201406120
    • (2015) J Cell Biol , vol.208 , Issue.4 , pp. 457-473
    • Comrie, W.A.1    Li, S.2    Boyle, S.3    Burkhardt, J.K.4
  • 242
    • 0034604337 scopus 로고    scopus 로고
    • Developmental control of endocytosis in dendritic cells by Cdc42
    • Garrett WS, Chen LM, Kroschewski R, Ebersold M, Turley S, Trombetta S, et al. Developmental control of endocytosis in dendritic cells by Cdc42. Cell (2000) 102(3):325-34. doi:10.1016/S0092-8674(00)00038-6
    • (2000) Cell , vol.102 , Issue.3 , pp. 325-334
    • Garrett, W.S.1    Chen, L.M.2    Kroschewski, R.3    Ebersold, M.4    Turley, S.5    Trombetta, S.6
  • 244
    • 84857495688 scopus 로고    scopus 로고
    • Ligand mobility modulates immunological synapse formation and T cell activation
    • Hsu CJ, Hsieh WT, Waldman A, Clarke F, Huseby ES, Burkhardt JK, et al. Ligand mobility modulates immunological synapse formation and T cell activation. PLoS One (2012) 7(2):e32398. doi:10.1371/journal.pone.0032398
    • (2012) PLoS One , vol.7 , Issue.2
    • Hsu, C.J.1    Hsieh, W.T.2    Waldman, A.3    Clarke, F.4    Huseby, E.S.5    Burkhardt, J.K.6
  • 245
    • 77955623486 scopus 로고    scopus 로고
    • Altered actin centripetal retrograde flow in physically restricted immunological synapses
    • Yu CH, Wu HJ, Kaizuka Y, Vale RD, Groves JT. Altered actin centripetal retrograde flow in physically restricted immunological synapses. PLoS One (2010) 5(7):e11878. doi:10.1371/journal.pone.0011878
    • (2010) PLoS One , vol.5 , Issue.7
    • Yu, C.H.1    Wu, H.J.2    Kaizuka, Y.3    Vale, R.D.4    Groves, J.T.5
  • 246
    • 0026071833 scopus 로고
    • Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale membrane domains
    • Edidin M, Stroynowski I. Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale membrane domains. J Cell Biol (1991) 112(6):1143-50. doi:10.1083/jcb.112.6.1143
    • (1991) J Cell Biol , vol.112 , Issue.6 , pp. 1143-1150
    • Edidin, M.1    Stroynowski, I.2
  • 247
    • 0345564815 scopus 로고    scopus 로고
    • Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4, 5-bisphosphate-dependent organization of cell actin
    • Kwik J, Boyle S, Fooksman D, Margolis L, Sheetz MP, Edidin M. Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4, 5-bisphosphate-dependent organization of cell actin. Proc Natl Acad Sci U S A (2003) 100(24):13964-9. doi:10.1073/pnas.2336102100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.24 , pp. 13964-13969
    • Kwik, J.1    Boyle, S.2    Fooksman, D.3    Margolis, L.4    Sheetz, M.P.5    Edidin, M.6
  • 248
    • 84859378549 scopus 로고    scopus 로고
    • Lifetime of major histocompatibility complex class-I membrane clusters is controlled by the actin cytoskeleton
    • Lavi Y, Gov N, Edidin M, Gheber LA. Lifetime of major histocompatibility complex class-I membrane clusters is controlled by the actin cytoskeleton. Biophys J (2012) 102(7):1543-50. doi:10.1016/j.bpj.2012.01.042
    • (2012) Biophys J , vol.102 , Issue.7 , pp. 1543-1550
    • Lavi, Y.1    Gov, N.2    Edidin, M.3    Gheber, L.A.4
  • 249
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls alpha5beta1 function
    • Friedland JC, Lee MH, Boettiger D. Mechanically activated integrin switch controls alpha5beta1 function. Science (2009) 323(5914):642-4. doi:10.1126/science.1168441
    • (2009) Science , vol.323 , Issue.5914 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 250
    • 78650661881 scopus 로고    scopus 로고
    • Occupancy of lymphocyte LFA-1 by surface-immobilized ICAM-1 is critical for TCR-but not for chemokine-triggered LFA-1 conversion to an open headpiece high-affinity state
    • Feigelson SW, Pasvolsky R, Cemerski S, Shulman Z, Grabovsky V, Ilani T, et al. Occupancy of lymphocyte LFA-1 by surface-immobilized ICAM-1 is critical for TCR-but not for chemokine-triggered LFA-1 conversion to an open headpiece high-affinity state. J Immunol (2010) 185(12):7394-404. doi:10.4049/jimmunol.1002246
    • (2010) J Immunol , vol.185 , Issue.12 , pp. 7394-7404
    • Feigelson, S.W.1    Pasvolsky, R.2    Cemerski, S.3    Shulman, Z.4    Grabovsky, V.5    Ilani, T.6
  • 251
    • 78049354941 scopus 로고    scopus 로고
    • Tethering of intercellular adhesion molecule on target cells is required for LFA-1-dependent NK cell adhesion and granule polarization
    • Gross CC, Brzostowski JA, Liu D, Long EO. Tethering of intercellular adhesion molecule on target cells is required for LFA-1-dependent NK cell adhesion and granule polarization. J Immunol (2010) 185(5):2918-26. doi:10.4049/jimmunol.1000761
    • (2010) J Immunol , vol.185 , Issue.5 , pp. 2918-2926
    • Gross, C.C.1    Brzostowski, J.A.2    Liu, D.3    Long, E.O.4
  • 252
    • 33748510575 scopus 로고    scopus 로고
    • Evidence of a functional role for interaction between ICAM-1 and nonmuscle alpha-actinins in leukocyte diapedesis
    • Celli L, Ryckewaert JJ, Delachanal E, Duperray A. Evidence of a functional role for interaction between ICAM-1 and nonmuscle alpha-actinins in leukocyte diapedesis. J Immunol (2006) 177(6):4113-21. doi:10.4049/jimmunol.177.6.4113
    • (2006) J Immunol , vol.177 , Issue.6 , pp. 4113-4121
    • Celli, L.1    Ryckewaert, J.J.2    Delachanal, E.3    Duperray, A.4
  • 253
    • 34250336879 scopus 로고    scopus 로고
    • RKIKK motif in the intracellular domain is critical for spatial and dynamic organization of ICAM-1: functional implication for the leukocyte adhesion and transmigration
    • Oh HM, Lee S, Na BR, Wee H, Kim SH, Choi SC, et al. RKIKK motif in the intracellular domain is critical for spatial and dynamic organization of ICAM-1: functional implication for the leukocyte adhesion and transmigration. Mol Biol Cell (2007) 18(6):2322-35. doi:10.1091/mbc.E06-08-0744
    • (2007) Mol Biol Cell , vol.18 , Issue.6 , pp. 2322-2335
    • Oh, H.M.1    Lee, S.2    Na, B.R.3    Wee, H.4    Kim, S.H.5    Choi, S.C.6
  • 254
    • 29144467684 scopus 로고    scopus 로고
    • CD80 cytoplasmic domain controls localization of CD28, CTLA-4, and protein kinase Ctheta in the immunological synapse
    • Tseng SY, Liu M, Dustin ML. CD80 cytoplasmic domain controls localization of CD28, CTLA-4, and protein kinase Ctheta in the immunological synapse. J Immunol (2005) 175(12):7829-36. doi:10.4049/jimmunol.175.12.7829
    • (2005) J Immunol , vol.175 , Issue.12 , pp. 7829-7836
    • Tseng, S.Y.1    Liu, M.2    Dustin, M.L.3
  • 255
    • 0032530373 scopus 로고    scopus 로고
    • Two regions in the CD80 cytoplasmic tail regulate CD80 redistribution and T cell costimulation
    • Doty RT, Clark EA. Two regions in the CD80 cytoplasmic tail regulate CD80 redistribution and T cell costimulation. J Immunol (1998) 161(6):2700-7.
    • (1998) J Immunol , vol.161 , Issue.6 , pp. 2700-2707
    • Doty, R.T.1    Clark, E.A.2
  • 256
    • 84862837101 scopus 로고    scopus 로고
    • A conserved polylysine motif in CD86 cytoplasmic tail is necessary for cytoskeletal association and effective co-stimulation
    • Girard T, El-Far M, Gaucher D, Acuto O, Beaule G, Michel F, et al. A conserved polylysine motif in CD86 cytoplasmic tail is necessary for cytoskeletal association and effective co-stimulation. Biochem Biophys Res Commun (2012) 423(2):301-7. doi:10.1016/j.bbrc.2012.05.116
    • (2012) Biochem Biophys Res Commun , vol.423 , Issue.2 , pp. 301-307
    • Girard, T.1    El-Far, M.2    Gaucher, D.3    Acuto, O.4    Beaule, G.5    Michel, F.6
  • 257
    • 0032559637 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
    • Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, et al. Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. J Cell Biol (1998) 140(4):885-95. doi:10.1083/jcb.140.4.885
    • (1998) J Cell Biol , vol.140 , Issue.4 , pp. 885-895
    • Yonemura, S.1    Hirao, M.2    Doi, Y.3    Takahashi, N.4    Kondo, T.5    Tsukita, S.6
  • 258
    • 0037166942 scopus 로고    scopus 로고
    • Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes
    • Barreiro O, Yanez-Mo M, Serrador JM, Montoya MC, Vicente-Manzanares M, Tejedor R, et al. Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. J Cell Biol (2002) 157(7):1233-45. doi:10.1083/jcb.200112126
    • (2002) J Cell Biol , vol.157 , Issue.7 , pp. 1233-1245
    • Barreiro, O.1    Yanez-Mo, M.2    Serrador, J.M.3    Montoya, M.C.4    Vicente-Manzanares, M.5    Tejedor, R.6
  • 259
    • 30744433331 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin proteins are phosphorylated by TNF-alpha and modulate permeability increases in human pulmonary microvascular endothelial cells
    • Koss M, Pfeiffer GR II, Wang Y, Thomas ST, Yerukhimovich M, Gaarde WA, et al. Ezrin/radixin/moesin proteins are phosphorylated by TNF-alpha and modulate permeability increases in human pulmonary microvascular endothelial cells. J Immunol (2006) 176(2):1218-27. doi:10.4049/jimmunol.176.2.1218
    • (2006) J Immunol , vol.176 , Issue.2 , pp. 1218-1227
    • Koss, M.1    Pfeiffer, G.R.2    Wang, Y.3    Thomas, S.T.4    Yerukhimovich, M.5    Gaarde, W.A.6
  • 260
    • 77953473256 scopus 로고    scopus 로고
    • Cutting edge: mechanical forces acting on T cells immobilized via the TCR complex can trigger TCR signaling
    • Li YC, Chen BM, Wu PC, Cheng TL, Kao LS, Tao MH, et al. Cutting edge: mechanical forces acting on T cells immobilized via the TCR complex can trigger TCR signaling. J Immunol (2010) 184(11):5959-63. doi:10.4049/jimmunol.0900775
    • (2010) J Immunol , vol.184 , Issue.11 , pp. 5959-5963
    • Li, Y.C.1    Chen, B.M.2    Wu, P.C.3    Cheng, T.L.4    Kao, L.S.5    Tao, M.H.6
  • 261
    • 77954486800 scopus 로고    scopus 로고
    • Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
    • Grashoff C, Hoffman BD, Brenner MD, Zhou R, Parsons M, Yang MT, et al. Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics. Nature (2010) 466(7303):263-6. doi:10.1038/nature09198
    • (2010) Nature , vol.466 , Issue.7303 , pp. 263-266
    • Grashoff, C.1    Hoffman, B.D.2    Brenner, M.D.3    Zhou, R.4    Parsons, M.5    Yang, M.T.6
  • 262
    • 84936084959 scopus 로고    scopus 로고
    • Lighting up the force: investigating mechanisms of mechanotransduction using fluorescent tension probes
    • Jurchenko C, Salaita KS. Lighting up the force: investigating mechanisms of mechanotransduction using fluorescent tension probes. Mol Cell Biol (2015) 35(15):2570-82. doi:10.1128/MCB.00195-15
    • (2015) Mol Cell Biol , vol.35 , Issue.15 , pp. 2570-2582
    • Jurchenko, C.1    Salaita, K.S.2
  • 263
    • 80054758789 scopus 로고    scopus 로고
    • Monitoring integrin activation by fluorescence resonance energy transfer
    • Lefort CT, Hyun YM, Kim M. Monitoring integrin activation by fluorescence resonance energy transfer. Methods Mol Biol (2012) 757:205-14. doi:10.1007/978-1-61779-166-6_14
    • (2012) Methods Mol Biol , vol.757 , pp. 205-214
    • Lefort, C.T.1    Hyun, Y.M.2    Kim, M.3
  • 264
    • 84884243072 scopus 로고    scopus 로고
    • Molecular tension sensors report forces generated by single integrin molecules in living cells
    • Morimatsu M, Mekhdjian AH, Adhikari AS, Dunn AR. Molecular tension sensors report forces generated by single integrin molecules in living cells. Nano Lett (2013) 13(9):3985-9. doi:10.1021/nl4005145
    • (2013) Nano Lett , vol.13 , Issue.9 , pp. 3985-3989
    • Morimatsu, M.1    Mekhdjian, A.H.2    Adhikari, A.S.3    Dunn, A.R.4
  • 265
    • 84856440471 scopus 로고    scopus 로고
    • Visualizing mechanical tension across membrane receptors with a fluorescent sensor
    • Stabley DR, Jurchenko C, Marshall SS, Salaita KS. Visualizing mechanical tension across membrane receptors with a fluorescent sensor. Nat Methods (2012) 9(1):64-7. doi:10.1038/nmeth.1747
    • (2012) Nat Methods , vol.9 , Issue.1 , pp. 64-67
    • Stabley, D.R.1    Jurchenko, C.2    Marshall, S.S.3    Salaita, K.S.4
  • 266
    • 84880733312 scopus 로고    scopus 로고
    • Adoptive T cell transfer for cancer immunotherapy in the era of synthetic biology
    • Kalos M, June CH. Adoptive T cell transfer for cancer immunotherapy in the era of synthetic biology. Immunity (2013) 39(1):49-60. doi:10.1016/j.immuni.2013.07.002
    • (2013) Immunity , vol.39 , Issue.1 , pp. 49-60
    • Kalos, M.1    June, C.H.2
  • 267
    • 84858758766 scopus 로고    scopus 로고
    • Adoptive immunotherapy for cancer: harnessing the T cell response
    • Restifo NP, Dudley ME, Rosenberg SA. Adoptive immunotherapy for cancer: harnessing the T cell response. Nat Rev Immunol (2012) 12(4):269-81. doi:10.1038/nri3191
    • (2012) Nat Rev Immunol , vol.12 , Issue.4 , pp. 269-281
    • Restifo, N.P.1    Dudley, M.E.2    Rosenberg, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.