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Volumn 24, Issue 1, 2012, Pages 107-115

Integrin inside-out signaling and the immunological synapse

Author keywords

[No Author keywords available]

Indexed keywords

ALPHAIIB BETA 3 INTEGRIN; ALPHALBETA2 INTEGRIN; ARGINYLGLYCYLASPARTIC ACID; ASPARTIC ACID; BETA1 INTEGRIN; BETA2 INTEGRIN; BETA3 INTEGRIN; CD28 ANTIGEN; CHEMOKINE RECEPTOR CCR7; EZRIN; GLUTAMINE; GLYCOPROTEIN P 15095; INTEGRIN; INTERCELLULAR ADHESION MOLECULE 1; INTERCELLULAR ADHESION MOLECULE 2; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; MAGNESIUM ION; MOESIN; RADIXIN; SECONDARY LYMPHOID TISSUE CHEMOKINE; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 5; VITRONECTIN RECEPTOR;

EID: 84857688656     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2011.10.004     Document Type: Review
Times cited : (318)

References (53)
  • 3
    • 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 B.H., Xiao T., Zhang C., Nishida N., Springer T.A. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol Cell 2008, 32:849-861.
    • (2008) Mol Cell , vol.32 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6
  • 4
    • 76349099822 scopus 로고    scopus 로고
    • Structure of an integrin with an αI domain, complement receptor type 4
    • Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A. Structure of an integrin with an αI domain, complement receptor type 4. EMBO J 2010, 29:666-679.
    • (2010) EMBO J , vol.29 , pp. 666-679
    • Xie, C.1    Zhu, J.2    Chen, X.3    Mi, L.4    Nishida, N.5    Springer, T.A.6
  • 5
    • 0037593914 scopus 로고    scopus 로고
    • High affinity ligand binding by integrins does not involve head separation
    • Luo B.-H., Springer T.A., Takagi J. High affinity ligand binding by integrins does not involve head separation. J Biol Chem 2003, 278:17185-17189.
    • (2003) J Biol Chem , vol.278 , pp. 17185-17189
    • Luo, B.-H.1    Springer, T.A.2    Takagi, J.3
  • 6
    • 34249685565 scopus 로고    scopus 로고
    • Tests of the extension and deadbolt models of integrin activation
    • Zhu J., Boylan B., Luo B.-H., Newman P.J., Springer T.A. Tests of the extension and deadbolt models of integrin activation. J Biol Chem 2007, 282:11914-11920.
    • (2007) J Biol Chem , vol.282 , pp. 11914-11920
    • Zhu, J.1    Boylan, B.2    Luo, B.-H.3    Newman, P.J.4    Springer, T.A.5
  • 7
    • 35648936537 scopus 로고    scopus 로고
    • A structural hypothesis for the transition between bent and extended conformations of the leukocyte β2 integrins
    • Shi M., Foo S.Y., Tan S.M., Mitchell E.P., Law S.K., Lescar J. A structural hypothesis for the transition between bent and extended conformations of the leukocyte β2 integrins. J Biol Chem 2007, 282:30198-30206.
    • (2007) J Biol Chem , vol.282 , pp. 30198-30206
    • Shi, M.1    Foo, S.Y.2    Tan, S.M.3    Mitchell, E.P.4    Law, S.K.5    Lescar, J.6
  • 8
    • 77958477970 scopus 로고    scopus 로고
    • Modulation of integrin activation by an entropic spring in the β-knee
    • Smagghe B., Huang P., Ban Y.-E., Baker D., Springer T.A. Modulation of integrin activation by an entropic spring in the β-knee. J Biol Chem 2010, 285:32954-32966.
    • (2010) J Biol Chem , vol.285 , pp. 32954-32966
    • Smagghe, B.1    Huang, P.2    Ban, Y.-E.3    Baker, D.4    Springer, T.A.5
  • 9
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo B.-H., Carman C.V., Springer T.A. Structural basis of integrin regulation and signaling. Annu Rev Immunol 2007, 25:619-647.
    • (2007) Annu Rev Immunol , vol.25 , pp. 619-647
    • Luo, B.-H.1    Carman, C.V.2    Springer, T.A.3
  • 10
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding of fibrinogen-mimetic therapeutics
    • Xiao T., Takagi J., Wang J.-h., Coller B.S., Springer T.A. Structural basis for allostery in integrins and binding of fibrinogen-mimetic therapeutics. Nature 2004, 432:59-67.
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Wang, J.-H.3    Coller, B.S.4    Springer, T.A.5
  • 13
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J., Petre B.M., Walz T., Springer T.A. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 2002, 110:599-611.
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 15
    • 3042602113 scopus 로고    scopus 로고
    • Allosteric β1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain
    • Luo B.-H., Strokovich K., Walz T., Springer T.A., Takagi J. Allosteric β1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain. J Biol Chem 2004, 279:27466-27471.
    • (2004) J Biol Chem , vol.279 , pp. 27466-27471
    • Luo, B.-H.1    Strokovich, K.2    Walz, T.3    Springer, T.A.4    Takagi, J.5
  • 20
    • 0013307787 scopus 로고    scopus 로고
    • Conformational changes in the integrin bA domain provide a mechanism for signal transduction via hybrid domain movement
    • Mould A.P., Barton S.J., Askari J.A., McEwan P.A., Buckley P.A., Craig S.E., Humphries M.J. Conformational changes in the integrin bA domain provide a mechanism for signal transduction via hybrid domain movement. J Biol Chem 2003, 278:17028-17035.
    • (2003) J Biol Chem , vol.278 , pp. 17028-17035
    • Mould, A.P.1    Barton, S.J.2    Askari, J.A.3    McEwan, P.A.4    Buckley, P.A.5    Craig, S.E.6    Humphries, M.J.7
  • 23
    • 80053434774 scopus 로고    scopus 로고
    • Intact αIIbβ3 extends after activation measured by solution X-ray scattering and electron microscopy
    • Eng E., Smagghe B., Walz T., Springer TA Intact αIIbβ3 extends after activation measured by solution X-ray scattering and electron microscopy. J Biol Chem 2011, 40:35218-35226.
    • (2011) J Biol Chem , vol.40 , pp. 35218-35226
    • Eng, E.1    Smagghe, B.2    Walz, T.3    Springer, T.A.4
  • 24
    • 76249113509 scopus 로고    scopus 로고
    • 3 activation in Chinese hamster ovary cells and platelets increases clustering rather than affinity
    • 3 activation in Chinese hamster ovary cells and platelets increases clustering rather than affinity. J Biol Chem 2010, 285:1841-1849.
    • (2010) J Biol Chem , vol.285 , pp. 1841-1849
    • Bunch, T.A.1
  • 25
    • 82455189778 scopus 로고    scopus 로고
    • Regulation of integrin affinity on cell surfaces
    • (Epub ahead of print). doi:10.1038/emboj.2011.333
    • Schurpf T, Springer TA: Regulation of integrin affinity on cell surfaces. EMBO J 2011, (Epub ahead of print). doi:10.1038/emboj.2011.333.
    • (2011) EMBO J
    • Schurpf, T.1    Springer, T.A.2
  • 26
    • 0031571726 scopus 로고    scopus 로고
    • Low affinity of cell surface lymphocyte function-associated antigen-1 (LFA-1) generates selectivity for cell-cell interactions
    • Ganpule G., Knorr R., Miller J.M., Carron C.P., Dustin M.L. Low affinity of cell surface lymphocyte function-associated antigen-1 (LFA-1) generates selectivity for cell-cell interactions. J Immunol 1997, 159:2685-2692.
    • (1997) J Immunol , vol.159 , pp. 2685-2692
    • Ganpule, G.1    Knorr, R.2    Miller, J.M.3    Carron, C.P.4    Dustin, M.L.5
  • 28
    • 0025806144 scopus 로고
    • Regulation of adhesion to ICAM-1 by the cytoplasmic domain of LFA-1 integrin β subunit
    • Hibbs M.L., Xu H., Stacker S.A., Springer T.A. Regulation of adhesion to ICAM-1 by the cytoplasmic domain of LFA-1 integrin β subunit. Science 1991, 251:1611-1613.
    • (1991) Science , vol.251 , pp. 1611-1613
    • Hibbs, M.L.1    Xu, H.2    Stacker, S.A.3    Springer, T.A.4
  • 29
    • 0025990521 scopus 로고
    • The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 β subunit: sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site
    • Hibbs M.L., Jakes S., Stacker S.A., Wallace R.W., Springer T.A. The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 β subunit: sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site. J Exp Med 1991, 174:1227-1238.
    • (1991) J Exp Med , vol.174 , pp. 1227-1238
    • Hibbs, M.L.1    Jakes, S.2    Stacker, S.A.3    Wallace, R.W.4    Springer, T.A.5
  • 31
    • 38949174996 scopus 로고    scopus 로고
    • Intercellular adhesion molecule-1-dependent stable interactions between T cells and dendritic cells determine CD8(+) T cell memory
    • Scholer A., Hugues S., Boissonnas A., Fetler L., Amigorena S. Intercellular adhesion molecule-1-dependent stable interactions between T cells and dendritic cells determine CD8(+) T cell memory. Immunity 2008, 28:258-270.
    • (2008) Immunity , vol.28 , pp. 258-270
    • Scholer, A.1    Hugues, S.2    Boissonnas, A.3    Fetler, L.4    Amigorena, S.5
  • 33
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks C.R.F., Freiberg B.A., Kupfer H., Sciaky N., Kupfer A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 1998, 394:82-86.
    • (1998) Nature , vol.394 , pp. 82-86
    • Monks, C.R.F.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 35
    • 0035655587 scopus 로고    scopus 로고
    • The immunological synapse of CTL contains a secretory domain and membrane bridges
    • Stinchcombe J.C., Bossi G., Booth S., Griffiths G.M. The immunological synapse of CTL contains a secretory domain and membrane bridges. Immunity 2001, 15:751-761.
    • (2001) Immunity , vol.15 , pp. 751-761
    • Stinchcombe, J.C.1    Bossi, G.2    Booth, S.3    Griffiths, G.M.4
  • 37
    • 58149280838 scopus 로고    scopus 로고
    • T cell-dendritic cell immunological synapses contain TCR-dependent CD28-CD80 clusters that recruit protein kinase Ctheta
    • Tseng S.Y., Waite J.C., Liu M., Vardhana S., Dustin M.L. T cell-dendritic cell immunological synapses contain TCR-dependent CD28-CD80 clusters that recruit protein kinase Ctheta. J Immunol 2008, 181:4852-4863.
    • (2008) J Immunol , vol.181 , pp. 4852-4863
    • Tseng, S.Y.1    Waite, J.C.2    Liu, M.3    Vardhana, S.4    Dustin, M.L.5
  • 38
    • 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 C.C., Brzostowski J.A., Liu D., Long E.O. Tethering of intercellular adhesion molecule on target cells is required for LFA-1-dependent NK cell adhesion and granule polarization. J Immunol 2010, 185:2918-2926.
    • (2010) J Immunol , vol.185 , pp. 2918-2926
    • Gross, C.C.1    Brzostowski, J.A.2    Liu, D.3    Long, E.O.4
  • 39
    • 0030061494 scopus 로고    scopus 로고
    • Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area
    • Dustin M.L., Ferguson L.M., Chan P.-Y., Springer T.A., Golan D.E. Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area. J Cell Biol 1996, 132:465-474.
    • (1996) J Cell Biol , vol.132 , pp. 465-474
    • Dustin, M.L.1    Ferguson, L.M.2    Chan, P.-Y.3    Springer, T.A.4    Golan, D.E.5
  • 41
  • 43
    • 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 A.D., Varma R., Dustin M.L., Vale R.D. 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, 104:20296-20301.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 20296-20301
    • Kaizuka, Y.1    Douglass, A.D.2    Varma, R.3    Dustin, M.L.4    Vale, R.D.5
  • 44
    • 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 S.W., Pasvolsky R., Cemerski S., Shulman Z., Grabovsky V., Ilani T., Sagiv A., Lemaitre F., Laudanna C., Shaw A.S., 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, 185:7394-7404.
    • (2010) J Immunol , vol.185 , pp. 7394-7404
    • Feigelson, S.W.1    Pasvolsky, R.2    Cemerski, S.3    Shulman, Z.4    Grabovsky, V.5    Ilani, T.6    Sagiv, A.7    Lemaitre, F.8    Laudanna, C.9    Shaw, A.S.10
  • 45
    • 33751578411 scopus 로고    scopus 로고
    • Talin1 regulates TCR-mediated LFA-1 function
    • Simonson W.T., Franco S.J., Huttenlocher A. Talin1 regulates TCR-mediated LFA-1 function. J Immunol 2006, 177:7707-7714.
    • (2006) J Immunol , vol.177 , pp. 7707-7714
    • Simonson, W.T.1    Franco, S.J.2    Huttenlocher, A.3
  • 46
  • 47
    • 33947372536 scopus 로고    scopus 로고
    • CCR7 ligands stimulate the intranodal motility of T lymphocytes in vivo
    • Worbs T., Mempel T.R., Bolter J., von Andrian U.H., Forster R. CCR7 ligands stimulate the intranodal motility of T lymphocytes in vivo. J Exp Med 2007, 204:489-495.
    • (2007) J Exp Med , vol.204 , pp. 489-495
    • Worbs, T.1    Mempel, T.R.2    Bolter, J.3    von Andrian, U.H.4    Forster, R.5
  • 49
    • 34548780292 scopus 로고    scopus 로고
    • Lymph node chemokines promote sustained T lymphocyte motility without triggering stable integrin adhesiveness in the absence of shear forces
    • Woolf E., Grigorova I., Sagiv A., Grabovsky V., Feigelson S.W., Shulman Z., Hartmann T., Sixt M., Cyster J.G., Alon R. Lymph node chemokines promote sustained T lymphocyte motility without triggering stable integrin adhesiveness in the absence of shear forces. Nat Immunol 2007, 8:1076-1085.
    • (2007) Nat Immunol , vol.8 , pp. 1076-1085
    • Woolf, E.1    Grigorova, I.2    Sagiv, A.3    Grabovsky, V.4    Feigelson, S.W.5    Shulman, Z.6    Hartmann, T.7    Sixt, M.8    Cyster, J.G.9    Alon, R.10
  • 50
    • 61449225547 scopus 로고    scopus 로고
    • Myosin-IIA and ICAM-1 regulate the interchange between two distinct modes of T cell migration
    • Jacobelli J., Bennett F.C., Pandurangi P., Tooley A.J., Krummel M.F. Myosin-IIA and ICAM-1 regulate the interchange between two distinct modes of T cell migration. J Immunol 2009, 182:2041-2050.
    • (2009) J Immunol , vol.182 , pp. 2041-2050
    • Jacobelli, J.1    Bennett, F.C.2    Pandurangi, P.3    Tooley, A.J.4    Krummel, M.F.5
  • 51
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer T.A. Adhesion receptors of the immune system. Nature 1990, 346:425-433.
    • (1990) Nature , vol.346 , pp. 425-433
    • Springer, T.A.1
  • 52
    • 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 M.H., Gould K., van der Merwe P.A. T-cell receptor triggering is critically dependent on the dimensions of its peptide-MHC ligand. Nature 2005, 436:578-582.
    • (2005) Nature , vol.436 , pp. 578-582
    • Choudhuri, K.1    Wiseman, D.2    Brown, M.H.3    Gould, K.4    van der Merwe, P.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.