메뉴 건너뛰기




Volumn 87, Issue 8-9, 2008, Pages 507-515

Adhesions ring: A structural comparison between podosomes and the immune synapse

Author keywords

Immune synapse; Invadopodia; Podosome

Indexed keywords

ACTIN RELATED PROTEIN; INTEGRIN; PAXILLIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; T LYMPHOCYTE RECEPTOR; TALIN; VINCULIN;

EID: 49049116497     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2008.01.011     Document Type: Short Survey
Times cited : (15)

References (85)
  • 1
    • 0037351084 scopus 로고    scopus 로고
    • Vav1 transduces TCR signals required for LFA-1 function and cell polarization at the immunological synapse
    • Ardouin L., Bracke M., Mathiot A., Pagakis S.N., Norton T., Hogg N., and Tybulewicz V.L. Vav1 transduces TCR signals required for LFA-1 function and cell polarization at the immunological synapse. Eur. J. Immunol. 33 (2003) 790-797
    • (2003) Eur. J. Immunol. , vol.33 , pp. 790-797
    • Ardouin, L.1    Bracke, M.2    Mathiot, A.3    Pagakis, S.N.4    Norton, T.5    Hogg, N.6    Tybulewicz, V.L.7
  • 4
    • 3543072944 scopus 로고    scopus 로고
    • Active Rho is localized to podosomes induced by oncogenic src and is required for their assembly and function
    • Berdeaux R.L., Diaz B., Kim L., and Martin G.S. Active Rho is localized to podosomes induced by oncogenic src and is required for their assembly and function. J. Cell Biol. 166 (2004) 317-323
    • (2004) J. Cell Biol. , vol.166 , pp. 317-323
    • Berdeaux, R.L.1    Diaz, B.2    Kim, L.3    Martin, G.S.4
  • 5
    • 0036711804 scopus 로고    scopus 로고
    • Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain
    • Bhatt A., Kaverina I., Otey C., and Huttenlocher A. Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain. J. Cell Sci. 115 (2002) 3415-3425
    • (2002) J. Cell Sci. , vol.115 , pp. 3415-3425
    • Bhatt, A.1    Kaverina, I.2    Otey, C.3    Huttenlocher, A.4
  • 6
    • 33846626054 scopus 로고    scopus 로고
    • Regulation of T-cell activation by the cytoskeleton
    • Billadeau D.D., Nolz J.C., and Gomez T.S. Regulation of T-cell activation by the cytoskeleton. Nat. Rev. Immunol. 7 (2007) 131-143
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 131-143
    • Billadeau, D.D.1    Nolz, J.C.2    Gomez, T.S.3
  • 7
    • 21844437618 scopus 로고    scopus 로고
    • Dynamin forms a src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity
    • Bruzzaniti A., Neff L., Sanjay A., Horne W.C., De Camilli P., and Baron R. Dynamin forms a src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity. Mol. Biol. Cell 16 (2005) 3301-3313
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3301-3313
    • Bruzzaniti, A.1    Neff, L.2    Sanjay, A.3    Horne, W.C.4    De Camilli, P.5    Baron, R.6
  • 8
    • 3543114271 scopus 로고    scopus 로고
    • Foot and mouth: podosomes, invadopodia and circular dorsal ruffles
    • Buccione R., Orth J.D., and McNiven M.A. Foot and mouth: podosomes, invadopodia and circular dorsal ruffles. Nat. Rev. Mol. Cell Biol. 5 (2004) 647-657
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 647-657
    • Buccione, R.1    Orth, J.D.2    McNiven, M.A.3
  • 9
    • 33745482350 scopus 로고    scopus 로고
    • Inhibition of calpain stabilises podosomes and impairs dendritic cell motility
    • Calle Y., Carragher N.O., Thrasher A.J., and Jones G.E. Inhibition of calpain stabilises podosomes and impairs dendritic cell motility. J. Cell Sci. 119 (2006) 2375-2385
    • (2006) J. Cell Sci. , vol.119 , pp. 2375-2385
    • Calle, Y.1    Carragher, N.O.2    Thrasher, A.J.3    Jones, G.E.4
  • 10
    • 3242762840 scopus 로고    scopus 로고
    • Differential roles for Wiskott-Aldrich syndrome protein in immune synapse formation and IL-2 production
    • Cannon J.L., and Burkhardt J.K. Differential roles for Wiskott-Aldrich syndrome protein in immune synapse formation and IL-2 production. J. Immunol. 173 (2004) 1658-1662
    • (2004) J. Immunol. , vol.173 , pp. 1658-1662
    • Cannon, J.L.1    Burkhardt, J.K.2
  • 12
    • 0036887581 scopus 로고    scopus 로고
    • Calpain: a role in cell transformation and migration
    • Carragher N.O., and Frame M.C. Calpain: a role in cell transformation and migration. Int. J. Biochem. Cell Biol. 34 (2002) 1539-1543
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 1539-1543
    • Carragher, N.O.1    Frame, M.C.2
  • 13
    • 33644943397 scopus 로고    scopus 로고
    • Regulation of podosomes by integrin alphavbeta3 and Rho GTPase-facilitated phosphoinositide signaling
    • Chellaiah M.A. Regulation of podosomes by integrin alphavbeta3 and Rho GTPase-facilitated phosphoinositide signaling. Eur. J. Cell Biol. 85 (2006) 311-317
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 311-317
    • Chellaiah, M.A.1
  • 14
    • 0034695921 scopus 로고    scopus 로고
    • Gelsolin deficiency blocks podosome assembly and produces increased bone mass and strength
    • Chellaiah M., Kizer N., Silva M., Alvarez U., Kwiatkowski D., and Hruska K.A. Gelsolin deficiency blocks podosome assembly and produces increased bone mass and strength. J. Cell Biol. 148 (2000) 665-678
    • (2000) J. Cell Biol. , vol.148 , pp. 665-678
    • Chellaiah, M.1    Kizer, N.2    Silva, M.3    Alvarez, U.4    Kwiatkowski, D.5    Hruska, K.A.6
  • 15
    • 0024414571 scopus 로고
    • Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells
    • Chen W.T. Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells. J. Exp. Zool. 251 (1989) 167-185
    • (1989) J. Exp. Zool. , vol.251 , pp. 167-185
    • Chen, W.T.1
  • 16
    • 0029658219 scopus 로고    scopus 로고
    • Integrin alpha 3 beta 1 participates in the phagocytosis of extracellular matrix molecules by human breast cancer cells
    • Coopman P.J., Thomas D.M., Gehlsen K.R., and Mueller S.C. Integrin alpha 3 beta 1 participates in the phagocytosis of extracellular matrix molecules by human breast cancer cells. Mol. Biol. Cell 7 (1996) 1789-1804
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1789-1804
    • Coopman, P.J.1    Thomas, D.M.2    Gehlsen, K.R.3    Mueller, S.C.4
  • 17
    • 0035864376 scopus 로고    scopus 로고
    • MT1-MMP initiates activation of pro-MMP-2 and integrin alphavbeta3 promotes maturation of MMP-2 in breast carcinoma cells
    • Deryugina E.I., Ratnikov B., Monosov E., Postnova T.I., DiScipio R., Smith J.W., and Strongin A.Y. MT1-MMP initiates activation of pro-MMP-2 and integrin alphavbeta3 promotes maturation of MMP-2 in breast carcinoma cells. Exp. Cell Res. 263 (2001) 209-223
    • (2001) Exp. Cell Res. , vol.263 , pp. 209-223
    • Deryugina, E.I.1    Ratnikov, B.2    Monosov, E.3    Postnova, T.I.4    DiScipio, R.5    Smith, J.W.6    Strongin, A.Y.7
  • 18
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin N., Bhatt A.K., Dutt P., Greer P.A., Arthur J.S., Elce J.S., and Huttenlocher A. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J. Biol. Chem. 276 (2001) 48382-48388
    • (2001) J. Biol. Chem. , vol.276 , pp. 48382-48388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3    Greer, P.A.4    Arthur, J.S.5    Elce, J.S.6    Huttenlocher, A.7
  • 19
    • 0024443411 scopus 로고
    • T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1
    • Dustin M.L., and Springer T.A. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature 341 (1989) 619-624
    • (1989) Nature , vol.341 , pp. 619-624
    • Dustin, M.L.1    Springer, T.A.2
  • 21
    • 0037512351 scopus 로고    scopus 로고
    • Macrophage podosomes assemble at the leading lamella by growth and fragmentation
    • Evans J.G., Correia I., Krasavina O., Watson N., and Matsudaira P. Macrophage podosomes assemble at the leading lamella by growth and fragmentation. J. Cell Biol. 161 (2003) 697-705
    • (2003) J. Cell Biol. , vol.161 , pp. 697-705
    • Evans, J.G.1    Correia, I.2    Krasavina, O.3    Watson, N.4    Matsudaira, P.5
  • 24
    • 21844440052 scopus 로고    scopus 로고
    • Tuning immune responses: diversity and adaptation of the immunological synapse
    • Friedl P., den Boer A.T., and Gunzer M. Tuning immune responses: diversity and adaptation of the immunological synapse. Nat. Rev. Immunol. 5 (2005) 532-545
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 532-545
    • Friedl, P.1    den Boer, A.T.2    Gunzer, M.3
  • 26
    • 0024728927 scopus 로고
    • Ultrastructure and gold-immunolabelling of cell-substratum adhesions (podosomes) in RSV-transformed BHK cells
    • Gavazzi I., Nermut M.V., and Marchisio P.C. Ultrastructure and gold-immunolabelling of cell-substratum adhesions (podosomes) in RSV-transformed BHK cells. J. Cell Sci. 94 (1989) 85-99
    • (1989) J. Cell Sci. , vol.94 , pp. 85-99
    • Gavazzi, I.1    Nermut, M.V.2    Marchisio, P.C.3
  • 29
    • 0036033308 scopus 로고    scopus 로고
    • Conventional protein kinase C mediates phorbol-dibutyrate-induced cytoskeletal remodeling in a7r5 smooth muscle cells
    • Hai C.M., Hahne P., Harrington E.O., and Gimona M. Conventional protein kinase C mediates phorbol-dibutyrate-induced cytoskeletal remodeling in a7r5 smooth muscle cells. Exp. Cell Res. 280 (2002) 64-74
    • (2002) Exp. Cell Res. , vol.280 , pp. 64-74
    • Hai, C.M.1    Hahne, P.2    Harrington, E.O.3    Gimona, M.4
  • 30
    • 33751504690 scopus 로고    scopus 로고
    • Tumour-mediated upregulation of chemoattractants and recruitment of myeloid cells predetermines lung metastasis
    • Hiratsuka S., Watanabe A., Aburatani H., and Maru Y. Tumour-mediated upregulation of chemoattractants and recruitment of myeloid cells predetermines lung metastasis. Nat. Cell Biol. 8 (2006) 1369-1375
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1369-1375
    • Hiratsuka, S.1    Watanabe, A.2    Aburatani, H.3    Maru, Y.4
  • 31
    • 0036227207 scopus 로고    scopus 로고
    • Restoration of podosomes and chemotaxis in Wiskott-Aldrich syndrome macrophages following induced expression of WASp
    • Jones G.E., Zicha D., Dunn G.A., Blundell M., and Thrasher A. Restoration of podosomes and chemotaxis in Wiskott-Aldrich syndrome macrophages following induced expression of WASp. Int. J. Biochem. Cell Biol. 34 (2002) 806-815
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 806-815
    • Jones, G.E.1    Zicha, D.2    Dunn, G.A.3    Blundell, M.4    Thrasher, A.5
  • 32
    • 0348143126 scopus 로고    scopus 로고
    • Podosome formation in cultured A7r5 vascular smooth muscle cells requires Arp2/3-dependent de-novo actin polymerization at discrete microdomains
    • Kaverina I., Stradal T.E., and Gimona M. Podosome formation in cultured A7r5 vascular smooth muscle cells requires Arp2/3-dependent de-novo actin polymerization at discrete microdomains. J. Cell Sci. 116 (2003) 4915-4924
    • (2003) J. Cell Sci. , vol.116 , pp. 4915-4924
    • Kaverina, I.1    Stradal, T.E.2    Gimona, M.3
  • 33
    • 22344453196 scopus 로고    scopus 로고
    • Live imaging of effector cell trafficking and autoantigen recognition within the unfolding autoimmune encephalomyelitis lesion
    • Kawakami N., Nagerl U.V., Odoardi F., Bonhoeffer T., Wekerle H., and Flugel A. Live imaging of effector cell trafficking and autoantigen recognition within the unfolding autoimmune encephalomyelitis lesion. J. Exp. Med. 201 (2005) 1805-1814
    • (2005) J. Exp. Med. , vol.201 , pp. 1805-1814
    • Kawakami, N.1    Nagerl, U.V.2    Odoardi, F.3    Bonhoeffer, T.4    Wekerle, H.5    Flugel, A.6
  • 35
    • 29244432463 scopus 로고    scopus 로고
    • A WAVE2-Abi1 complex mediates CSF-1-induced F-actin-rich membrane protrusions and migration in macrophages
    • Kheir W.A., Gevrey J.C., Yamaguchi H., Isaac B., and Cox D. A WAVE2-Abi1 complex mediates CSF-1-induced F-actin-rich membrane protrusions and migration in macrophages. J. Cell Sci. 118 (2005) 5369-5379
    • (2005) J. Cell Sci. , vol.118 , pp. 5369-5379
    • Kheir, W.A.1    Gevrey, J.C.2    Yamaguchi, H.3    Isaac, B.4    Cox, D.5
  • 36
    • 0034599541 scopus 로고    scopus 로고
    • Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton
    • Krause M., Sechi A.S., Konradt M., Monner D., Gertler F.B., and Wehland J. Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton. J. Cell Biol. 149 (2000) 181-194
    • (2000) J. Cell Biol. , vol.149 , pp. 181-194
    • Krause, M.1    Sechi, A.S.2    Konradt, M.3    Monner, D.4    Gertler, F.B.5    Wehland, J.6
  • 38
  • 40
    • 33847343034 scopus 로고    scopus 로고
    • The matrix corroded: podosomes and invadopodia in extracellular matrix degradation
    • Linder S. The matrix corroded: podosomes and invadopodia in extracellular matrix degradation. Trends Cell Biol. 17 (2007) 107-117
    • (2007) Trends Cell Biol. , vol.17 , pp. 107-117
    • Linder, S.1
  • 41
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: adhesion hot-spots of invasive cells
    • Linder S., and Aepfelbacher M. Podosomes: adhesion hot-spots of invasive cells. Trends Cell Biol. 13 (2003) 376-385
    • (2003) Trends Cell Biol. , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 42
    • 0033578374 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages
    • Linder S., Nelson D., Weiss M., and Aepfelbacher M. Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages. Proc. Natl. Acad. Sci. USA 96 (1999) 9648-9653
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9648-9653
    • Linder, S.1    Nelson, D.2    Weiss, M.3    Aepfelbacher, M.4
  • 43
    • 33845897882 scopus 로고    scopus 로고
    • Involvement of the src-cortactin pathway in podosome formation and turnover during polarization of cultured osteoclasts
    • Luxenburg C., Parsons J.T., Addadi L., and Geiger B. Involvement of the src-cortactin pathway in podosome formation and turnover during polarization of cultured osteoclasts. J. Cell Sci. 119 (2006) 4878-4888
    • (2006) J. Cell Sci. , vol.119 , pp. 4878-4888
    • Luxenburg, C.1    Parsons, J.T.2    Addadi, L.3    Geiger, B.4
  • 46
    • 0347717903 scopus 로고    scopus 로고
    • T-cell priming by dendritic cells in lymph nodes occurs in three distinct phases
    • Mempel T.R., Henrickson S.E., and Von Andrian U.H. T-cell priming by dendritic cells in lymph nodes occurs in three distinct phases. Nature 427 (2004) 154-159
    • (2004) Nature , vol.427 , pp. 154-159
    • Mempel, T.R.1    Henrickson, S.E.2    Von Andrian, U.H.3
  • 49
    • 0036468250 scopus 로고    scopus 로고
    • Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts
    • Mizutani K., Miki H., He H., Maruta H., and Takenawa T. Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts. Cancer Res. 62 (2002) 669-674
    • (2002) Cancer Res. , vol.62 , pp. 669-674
    • Mizutani, K.1    Miki, H.2    He, H.3    Maruta, H.4    Takenawa, T.5
  • 50
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks C.R., Freiberg B.A., Kupfer H., Sciaky N., and Kupfer A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 395 (1998) 82-86
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 51
    • 0026457798 scopus 로고
    • Tyrosine phosphorylation of membrane proteins mediates cellular invasion by transformed cells
    • Mueller S.C., Yeh Y., and Chen W.T. Tyrosine phosphorylation of membrane proteins mediates cellular invasion by transformed cells. J. Cell Biol. 119 (1992) 1309-1325
    • (1992) J. Cell Biol. , vol.119 , pp. 1309-1325
    • Mueller, S.C.1    Yeh, Y.2    Chen, W.T.3
  • 52
    • 0031594710 scopus 로고    scopus 로고
    • Activation of beta1 integrin signaling stimulates tyrosine phosphorylation of p190RhoGAP and membrane-protrusive activities at invadopodia
    • Nakahara H., Mueller S.C., Nomizu M., Yamada Y., Yeh Y., and Chen W.T. Activation of beta1 integrin signaling stimulates tyrosine phosphorylation of p190RhoGAP and membrane-protrusive activities at invadopodia. J. Biol. Chem. 273 (1998) 9-12
    • (1998) J. Biol. Chem. , vol.273 , pp. 9-12
    • Nakahara, H.1    Mueller, S.C.2    Nomizu, M.3    Yamada, Y.4    Yeh, Y.5    Chen, W.T.6
  • 55
  • 56
    • 0021175671 scopus 로고
    • A synaptic basis for T-lymphocyte activation
    • Norcross M.A. A synaptic basis for T-lymphocyte activation. Ann. Immunol. 135D (1984) 113-134
    • (1984) Ann. Immunol. , vol.135 D , pp. 113-134
    • Norcross, M.A.1
  • 57
    • 10344236528 scopus 로고    scopus 로고
    • Thrombospondin induces RhoA inactivation through FAK-dependent signaling to stimulate focal adhesion disassembly
    • Orr A.W., Pallero M.A., Xiong W.C., and Murphy-Ullrich J.E. Thrombospondin induces RhoA inactivation through FAK-dependent signaling to stimulate focal adhesion disassembly. J. Biol. Chem. 279 (2004) 48983-48992
    • (2004) J. Biol. Chem. , vol.279 , pp. 48983-48992
    • Orr, A.W.1    Pallero, M.A.2    Xiong, W.C.3    Murphy-Ullrich, J.E.4
  • 58
    • 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 O.D., Mitchell D., Jager G.C., South S., Murriel C., McBride J., Herzenberg L.A., Kinoshita S., and Nolan G.P. Leukocyte functional antigen 1 lowers T cell activation thresholds and signaling through cytohesin-1 and Jun-activating binding protein 1. Nat. Immunol. 4 (2003) 1083-1092
    • (2003) Nat. Immunol. , vol.4 , pp. 1083-1092
    • Perez, O.D.1    Mitchell, D.2    Jager, G.C.3    South, S.4    Murriel, C.5    McBride, J.6    Herzenberg, L.A.7    Kinoshita, S.8    Nolan, G.P.9
  • 59
    • 29144503720 scopus 로고    scopus 로고
    • A role for phosphatidylinositol 3-kinase in TCR-stimulated ERK activation leading to paxillin phosphorylation and CTL degranulation
    • Robertson L.K., Mireau L.R., and Ostergaard H.L. A role for phosphatidylinositol 3-kinase in TCR-stimulated ERK activation leading to paxillin phosphorylation and CTL degranulation. J. Immunol. 175 (2005) 8138-8145
    • (2005) J. Immunol. , vol.175 , pp. 8138-8145
    • Robertson, L.K.1    Mireau, L.R.2    Ostergaard, H.L.3
  • 60
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins
    • Samelson L.E. Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu. Rev. Immunol. 20 (2002) 371-394
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 61
    • 0038445857 scopus 로고    scopus 로고
    • DOCK2 is essential for antigen-induced translocation of TCR and lipid rafts, but not PKC-theta and LFA-1, in T cells
    • Sanui T., Inayoshi A., Noda M., Iwata E., Oike M., Sasazuki T., and Fukui Y. DOCK2 is essential for antigen-induced translocation of TCR and lipid rafts, but not PKC-theta and LFA-1, in T cells. Immunity 19 (2003) 119-129
    • (2003) Immunity , vol.19 , pp. 119-129
    • Sanui, T.1    Inayoshi, A.2    Noda, M.3    Iwata, E.4    Oike, M.5    Sasazuki, T.6    Fukui, Y.7
  • 62
    • 33751578411 scopus 로고    scopus 로고
    • Talin1 regulates TCR-mediated LFA-1 function
    • Simonson W.T., Franco S.J., and Huttenlocher A. Talin1 regulates TCR-mediated LFA-1 function. J. Immunol. 177 (2006) 7707-7714
    • (2006) J. Immunol. , vol.177 , pp. 7707-7714
    • Simonson, W.T.1    Franco, S.J.2    Huttenlocher, A.3
  • 65
    • 0032193220 scopus 로고    scopus 로고
    • Essential roles of Lyn in fibronectin-mediated filamentous actin assembly and cell motility in mast cells
    • Suzuki T., Shoji S., Yamamoto K., Nada S., Okada M., Yamamoto T., and Honda Z. Essential roles of Lyn in fibronectin-mediated filamentous actin assembly and cell motility in mast cells. J. Immunol. 161 (1998) 3694-3701
    • (1998) J. Immunol. , vol.161 , pp. 3694-3701
    • Suzuki, T.1    Shoji, S.2    Yamamoto, K.3    Nada, S.4    Okada, M.5    Yamamoto, T.6    Honda, Z.7
  • 66
    • 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 G.A., and Saito T. The actin cloud induced by LFA-1-mediated outside-in signals lowers the threshold for T-cell activation. Blood 109 (2007) 168-175
    • (2007) Blood , vol.109 , pp. 168-175
    • Suzuki, J.1    Yamasaki, S.2    Wu, J.3    Koretzky, G.A.4    Saito, T.5
  • 68
    • 33645064530 scopus 로고    scopus 로고
    • A signalling cascade involving PKC, Src and Cdc42 regulates podosome assembly in cultured endothelial cells in response to phorbol ester
    • Tatin F., Varon C., Genot E., and Moreau V. A signalling cascade involving PKC, Src and Cdc42 regulates podosome assembly in cultured endothelial cells in response to phorbol ester. J. Cell Sci. 119 (2006) 769-781
    • (2006) J. Cell Sci. , vol.119 , pp. 769-781
    • Tatin, F.1    Varon, C.2    Genot, E.3    Moreau, V.4
  • 69
    • 33745626457 scopus 로고    scopus 로고
    • Cortactin has an essential and specific role in osteoclast actin assembly
    • Tehrani S., Faccio R., Chandrasekar I., Ross F.P., and Cooper J.A. Cortactin has an essential and specific role in osteoclast actin assembly. Mol. Biol. Cell 17 (2006) 2882-2895
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2882-2895
    • Tehrani, S.1    Faccio, R.2    Chandrasekar, I.3    Ross, F.P.4    Cooper, J.A.5
  • 71
    • 33847376308 scopus 로고    scopus 로고
    • Requirement for a complex of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein in podosome formation in macrophages
    • Tsuboi S. Requirement for a complex of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein in podosome formation in macrophages. J. Immunol. 178 (2007) 2987-2995
    • (2007) J. Immunol. , vol.178 , pp. 2987-2995
    • Tsuboi, S.1
  • 72
    • 0036631548 scopus 로고    scopus 로고
    • Vav proteins as signal integrators for multi-subunit immune-recognition receptors
    • Turner M., and Billadeau D.D. Vav proteins as signal integrators for multi-subunit immune-recognition receptors. Nat. Rev. Immunol. 2 (2002) 476-486
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 476-486
    • Turner, M.1    Billadeau, D.D.2
  • 73
    • 18844449626 scopus 로고    scopus 로고
    • Vav-family proteins in T-cell signalling
    • Tybulewicz V.L. Vav-family proteins in T-cell signalling. Curr. Opin. Immunol. 17 (2005) 267-274
    • (2005) Curr. Opin. Immunol. , vol.17 , pp. 267-274
    • Tybulewicz, V.L.1
  • 74
    • 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., and 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. 181 (1995) 577-584
    • (1995) J. Exp. Med. , vol.181 , pp. 577-584
    • Valitutti, S.1    Dessing, M.2    Aktories, K.3    Gallati, H.4    Lanzavecchia, A.5
  • 75
    • 33746210274 scopus 로고    scopus 로고
    • A critical role for prostaglandin E2 in podosome dissolution and induction of high-speed migration during dendritic cell maturation
    • van Helden S.F., Krooshoop D.J., Broers K.C., Raymakers R.A., Figdor C.G., and van Leeuwen F.N. A critical role for prostaglandin E2 in podosome dissolution and induction of high-speed migration during dendritic cell maturation. J. Immunol. 177 (2006) 1567-1574
    • (2006) J. Immunol. , vol.177 , pp. 1567-1574
    • van Helden, S.F.1    Krooshoop, D.J.2    Broers, K.C.3    Raymakers, R.A.4    Figdor, C.G.5    van Leeuwen, F.N.6
  • 76
    • 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., and Dustin M.L. T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. Immunity 25 (2006) 117-127
    • (2006) Immunity , vol.25 , pp. 117-127
    • Varma, R.1    Campi, G.2    Yokosuka, T.3    Saito, T.4    Dustin, M.L.5
  • 77
    • 18144378805 scopus 로고    scopus 로고
    • Vav activation and function as a rac guanine nucleotide exchange factor in macrophage colony-stimulating factor-induced macrophage chemotaxis
    • Vedham V., Phee H., and Coggeshall K.M. Vav activation and function as a rac guanine nucleotide exchange factor in macrophage colony-stimulating factor-induced macrophage chemotaxis. Mol. Cell. Biol. 25 (2005) 4211-4220
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4211-4220
    • Vedham, V.1    Phee, H.2    Coggeshall, K.M.3
  • 78
    • 33947140891 scopus 로고    scopus 로고
    • Dissecting the functional domain requirements of cortactin in invadopodia formation
    • Webb B.A., Jia L., Eves R., and Mak A.S. Dissecting the functional domain requirements of cortactin in invadopodia formation. Eur. J. Cell Biol. 86 (2007) 189-206
    • (2007) Eur. J. Cell Biol. , vol.86 , pp. 189-206
    • Webb, B.A.1    Jia, L.2    Eves, R.3    Mak, A.S.4
  • 84
    • 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 J.L., Abraham R.T., Way M., Billadeau D.D., Bubeck-Wardenberg J., and Burkhardt J.K. 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. 171 (2003) 1360-1368
    • (2003) J. Immunol. , vol.171 , 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    Burkhardt, J.K.7
  • 85
    • 30044438580 scopus 로고    scopus 로고
    • Role for the Abi/wave protein complex in T cell receptor-mediated proliferation and cytoskeletal remodeling
    • Zipfel P.A., Bunnell S.C., Witherow D.S., Gu J.J., Chislock E.M., Ring C., and Pendergast A.M. Role for the Abi/wave protein complex in T cell receptor-mediated proliferation and cytoskeletal remodeling. Curr. Biol. 16 (2006) 35-46
    • (2006) Curr. Biol. , vol.16 , pp. 35-46
    • Zipfel, P.A.1    Bunnell, S.C.2    Witherow, D.S.3    Gu, J.J.4    Chislock, E.M.5    Ring, C.6    Pendergast, A.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.