메뉴 건너뛰기




Volumn 191, Issue , 2003, Pages 220-236

All roads lead to actin: The intimate relationship between TCR signaling and the cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADAPTOR PROTEIN; COLCHICINE; CYTOCHALASIN D; INTEGRIN; PROTEIN KINASE ZAP 70; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

EID: 0037304542     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-065X.2003.00004.x     Document Type: Review
Times cited : (61)

References (174)
  • 1
    • 0034232037 scopus 로고    scopus 로고
    • The immunological synapse and the actin cytoskeleton: Molecular hardware for T cell signaling
    • Dustin ML, Cooper JA. The immunological synapse and the actin cytoskeleton: molecular hardware for T cell signaling. Nat Immunol 2000;1:23-29.
    • (2000) Nat Immunol , vol.1 , pp. 23-29
    • Dustin, M.L.1    Cooper, J.A.2
  • 2
    • 0037067657 scopus 로고    scopus 로고
    • Shmoos, rafts, and uropods - The many facets of cell polarity
    • Dustin ML. Shmoos, rafts, and uropods - the many facets of cell polarity. Cell 2002; 110: 13-18.
    • (2002) Cell , vol.110 , pp. 13-18
    • Dustin, M.L.1
  • 3
    • 0036467376 scopus 로고    scopus 로고
    • Dynamics of the immunological synapse: Finding, establishing and solidifying a connection
    • Krummel MF, Davis MM. Dynamics of the immunological synapse: finding, establishing and solidifying a connection. Curr Opin Immunol 2002;14:66-74.
    • (2002) Curr Opin Immunol , vol.14 , pp. 66-74
    • Krummel, M.F.1    Davis, M.M.2
  • 4
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • Ridley AJ. Rho family proteins: coordinating cell responses. Trends Cell Biol 2001;11: 471-477.
    • (2001) Trends Cell Biol , vol.11 , pp. 471-477
    • Ridley, A.J.1
  • 5
    • 0037144842 scopus 로고    scopus 로고
    • T cell receptor ligation induces the formation of dynamically regulated signaling assemblies
    • Bunnell SC, et al. T cell receptor ligation induces the formation of dynamically regulated signaling assemblies. J Biol Chem 2002;158:1-14.
    • (2002) J Biol Chem , vol.158 , pp. 1-14
    • Bunnell, S.C.1
  • 6
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: The role of adapter proteins
    • Samelson LE. Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu Rev Immunol 2002;20: 371-394.
    • (2002) Annu Rev Immunol , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 7
    • 0029809142 scopus 로고    scopus 로고
    • Normal T cells express two T cell antigen receptor populations, one of which is linked to the cytoskeleton via zeta chain and displays a unique activation-dependent phosphorylation pattern
    • Caplan S, Baniyash M. Normal T cells express two T cell antigen receptor populations, one of which is linked to the cytoskeleton via zeta chain and displays a unique activation-dependent phosphorylation pattern. J Biol Chem 1996; 271:20705-20712.
    • (1996) J Biol Chem , vol.271 , pp. 20705-20712
    • Caplan, S.1    Baniyash, M.2
  • 8
    • 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: 5491-5499.
    • (1998) J Immunol , vol.161 , pp. 5491-5499
    • Rozdzial, M.M.1    Pleiman, C.M.2    Cambier, J.C.3    Finkel, T.H.4
  • 9
    • 0034026493 scopus 로고    scopus 로고
    • Searching for significance in TCR-cytoskeleton interactions
    • Caplan S, Baniyash M. Searching for significance in TCR-cytoskeleton interactions. Immunol Today 2000;21:223-228.
    • (2000) Immunol Today , vol.21 , pp. 223-228
    • Caplan, S.1    Baniyash, M.2
  • 10
    • 0025735032 scopus 로고
    • Association of various T cell-surface molecules with the cytoskeleton. Effect of cross-linking and activation
    • Geppert TD, Lipsky PE. Association of various T cell-surface molecules with the cytoskeleton. Effect of cross-linking and activation. J Immunol 1991;146:3298-3305.
    • (1991) J Immunol , vol.146 , pp. 3298-3305
    • Geppert, T.D.1    Lipsky, P.E.2
  • 11
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T cell activation
    • Grakoui A, et al. The immunological synapse: a molecular machine controlling T cell activation. Science 1999;285:221-227.
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1
  • 12
    • 0034005120 scopus 로고    scopus 로고
    • Cytoskeletal polarization and redistribution of cell-surface molecules during T cell antigen recognition
    • van der Merwe PA, Davis SJ, Shaw AS, Dustin ML. Cytoskeletal polarization and redistribution of cell-surface molecules during T cell antigen recognition. Semin Immunol 2000;12:5-21.
    • (2000) Semin Immunol , vol.12 , pp. 5-21
    • Van Der Merwe, P.A.1    Davis, S.J.2    Shaw, A.S.3    Dustin, M.L.4
  • 13
    • 0034644505 scopus 로고    scopus 로고
    • Signaling takes shape in the immune system
    • Dustin ML, Chan AC. Signaling takes shape in the immune system. Cell 2000;103: 283-294.
    • (2000) Cell , vol.103 , pp. 283-294
    • Dustin, M.L.1    Chan, A.C.2
  • 14
    • 0036644617 scopus 로고    scopus 로고
    • Assembly of the immunological synapse for T cells and NK cells
    • Davis DM. Assembly of the immunological synapse for T cells and NK cells. Trends Immunol 2002;23:356-363.
    • (2002) Trends Immunol , vol.23 , pp. 356-363
    • Davis, D.M.1
  • 15
    • 34247557390 scopus 로고    scopus 로고
    • The immunological synapse
    • Dustin ML. The immunological synapse. Arthritis Res 2002;4:S119-S125.
    • (2002) Arthritis Res , vol.4
    • Dustin, M.L.1
  • 16
    • 0036604984 scopus 로고    scopus 로고
    • Formation and function of the immunological synapse
    • van der Merwe PA. Formation and function of the immunological synapse. Curr Opin Immunol 2002;14:293-298.
    • (2002) Curr Opin Immunol , vol.14 , pp. 293-298
    • Van Der Merwe, P.A.1
  • 17
    • 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;395:82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 18
    • 0035655587 scopus 로고    scopus 로고
    • The immunological synapse of CTL contains a secretory domain and membrane bridges
    • Stinchcombe JC, Bossi G, Booth S, Griffiths GM. 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
  • 19
    • 0035940426 scopus 로고    scopus 로고
    • Formation of supramolecular activation clusters on fresh ex vivo CD8+ T cells after engagement of the T cell antigen receptor and CD8 by antigen-presenting cells
    • Potter TA, Grebe K, Freiberg B, Kupfer A. Formation of supramolecular activation clusters on fresh ex vivo CD8+ T cells after engagement of the T cell antigen receptor and CD8 by antigen-presenting cells. Proc Natl Acad Sci USA 2001;98:12624-12629.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12624-12629
    • Potter, T.A.1    Grebe, K.2    Freiberg, B.3    Kupfer, A.4
  • 21
    • 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 USA 1999;96:8471-8476.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8471-8476
    • Wei, X.1    Tromberg, B.J.2    Cahalan, M.D.3
  • 22
    • 0036195934 scopus 로고    scopus 로고
    • Regulation of Lck activity by CD4 and CD28 in the immunological synapse
    • Holdorf AD, Lee KH, Burack WR, Allen PM, Shaw AS. Regulation of Lck activity by CD4 and CD28 in the immunological synapse. Nat Immunol 2002;3:259-264.
    • (2002) Nat Immunol , vol.3 , pp. 259-264
    • Holdorf, A.D.1    Lee, K.H.2    Burack, W.R.3    Allen, P.M.4    Shaw, A.S.5
  • 23
    • 0030996848 scopus 로고    scopus 로고
    • ZAP-70 protein tyrosine kinase is constitutively targeted to the T cell cortex independently of its SH2 domains
    • Huby RD, Iwashima M, Weiss A, Ley SC. ZAP-70 protein tyrosine kinase is constitutively targeted to the T cell cortex independently of its SH2 domains. J Cell Biol 1997;137:1639-1649.
    • (1997) J Cell Biol , vol.137 , pp. 1639-1649
    • Huby, R.D.1    Iwashima, M.2    Weiss, A.3    Ley, S.C.4
  • 24
  • 25
    • 0032534304 scopus 로고    scopus 로고
    • TCR signaling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site
    • Sperling AI, Sedy JR, Manjunath N, Kupfer A, Ardman B, Burkhardt JK. TCR signaling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site. J Immunol 1998;161:6459-6462.
    • (1998) J Immunol , vol.161 , pp. 6459-6462
    • Sperling, A.I.1    Sedy, J.R.2    Manjunath, N.3    Kupfer, A.4    Ardman, B.5    Burkhardt, J.K.6
  • 26
    • 0034730188 scopus 로고    scopus 로고
    • A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation
    • Johnson KG, Bromley SK, Dustin ML, Thomas ML. A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation. Proc Natl Acad Sci USA 2000;97:10138-10143.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10138-10143
    • Johnson, K.G.1    Bromley, S.K.2    Dustin, M.L.3    Thomas, M.L.4
  • 28
    • 0034720166 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases
    • Kawabuchi M, et al. Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. Nature 2000;404:999-1003.
    • (2000) Nature , vol.404 , pp. 999-1003
    • Kawabuchi, M.1
  • 29
    • 0342313755 scopus 로고    scopus 로고
    • Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adapter protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation
    • Brdicka T, et al. Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adapter protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J Exp Med 2000;191:1591-1604.
    • (2000) J Exp Med , vol.191 , pp. 1591-1604
    • Brdicka, T.1
  • 30
    • 0035955452 scopus 로고    scopus 로고
    • Interaction between two adapter proteins, PAG and EBP50: A possible link between membrane rafts and actin cytoskeleton
    • Brdickova N, et al. Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton. FEBS Lett 2001;507:133-136.
    • (2001) FEBS Lett , vol.507 , pp. 133-136
    • Brdickova, N.1
  • 31
    • 0037080345 scopus 로고    scopus 로고
    • Cutting edge: Negative regulation of immune synapse formation by anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly
    • Itoh K, et al. Cutting edge: negative regulation of immune synapse formation by anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly. J Immunol 2002;168:541-544.
    • (2002) J Immunol , vol.168 , pp. 541-544
    • Itoh, K.1
  • 32
    • 0036063264 scopus 로고    scopus 로고
    • Immature CD4(+)CD8(+) thymocytes form a multifocal immunological synapse with sustained tyrosine phosphorylation
    • Hailman E, Burack WR, Shaw AS, Dustin ML, Allen PM. Immature CD4(+)CD8(+) thymocytes form a multifocal immunological synapse with sustained tyrosine phosphorylation. Immunity 2002;16:839-848.
    • (2002) Immunity , vol.16 , pp. 839-848
    • Hailman, E.1    Burack, W.R.2    Shaw, A.S.3    Dustin, M.L.4    Allen, P.M.5
  • 34
    • 0032545218 scopus 로고    scopus 로고
    • A receptor/cytoskeletal movement triggered by costimulation during T cell activation
    • Wulfing C, Davis MM. A receptor/cytoskeletal movement triggered by costimulation during T cell activation. Science 1998;282:2266-2269.
    • (1998) Science , vol.282 , pp. 2266-2269
    • Wulfing, C.1    Davis, M.M.2
  • 35
    • 0032568580 scopus 로고    scopus 로고
    • Visualizing the dynamics of T cell activation: Intracellular adhesion molecule 1 migrates rapidly to the T cell/B cell interface and acts to sustain calcium levels
    • Wulfing C, Sjaastad MD, Davis MM, Visualizing the dynamics of T cell activation: intracellular adhesion molecule 1 migrates rapidly to the T cell/B cell interface and acts to sustain calcium levels. Proc Natl Acad Sci USA 1998;95:6302-6307.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6302-6307
    • Wulfing, C.1    Sjaastad, M.D.2    Davis, M.M.3
  • 36
    • 0034714184 scopus 로고    scopus 로고
    • Differential clustering of CD4 and CD3zeta during T cell recognition
    • Krummel MF, Sjaastad MD, Wulfing C, Davis MM. Differential clustering of CD4 and CD3zeta during T cell recognition. Science 2000;289:1349-1352.
    • (2000) Science , vol.289 , pp. 1349-1352
    • Krummel, M.F.1    Sjaastad, M.D.2    Wulfing, C.3    Davis, M.M.4
  • 37
    • 0034687873 scopus 로고    scopus 로고
    • LAT, the linker for activation of T cells: A bridge between T cell-specific and general signaling pathways
    • Wange RL. LAT, the linker for activation of T cells: a bridge between T cell-specific and general signaling pathways. Sci STKE 2000;2000:RE1.
    • (2000) Sci STKE , vol.2000
    • Wange, R.L.1
  • 38
    • 0033997322 scopus 로고    scopus 로고
    • The role of membrane-associated adapters in T cell receptor signalling
    • Zhang W, Samelson LE. The role of membrane-associated adapters in T cell receptor signalling. Semin Immunol 2000;12:35-41.
    • (2000) Semin Immunol , vol.12 , pp. 35-41
    • Zhang, W.1    Samelson, L.E.2
  • 39
    • 0033678973 scopus 로고    scopus 로고
    • LAT is essential for Fc (epsilon)RI-mediated mast cell activation
    • Saitoh S, et al. LAT is essential for Fc (epsilon)RI-mediated mast cell activation. Immunity 2000;12:525-535.
    • (2000) Immunity , vol.12 , pp. 525-535
    • Saitoh, S.1
  • 40
    • 0035075507 scopus 로고    scopus 로고
    • Dynamic actin polymerization drives T cell receptor-induced spreading: A role for the signal transduction adapter LAT
    • Bunnell SC, Kapoor V, Trible RP, Zhang W, Samelson LE. Dynamic actin polymerization drives T cell receptor-induced spreading: a role for the signal transduction adapter LAT. Immunity 2001;14:315-329.
    • (2001) Immunity , vol.14 , pp. 315-329
    • Bunnell, S.C.1    Kapoor, V.2    Trible, R.P.3    Zhang, W.4    Samelson, L.E.5
  • 41
    • 0034536632 scopus 로고    scopus 로고
    • Rho regulates T cell receptor ITAM-induced lymphocyte spreading in an integrin-independent manner
    • Borroto A, et al. Rho regulates T cell receptor ITAM-induced lymphocyte spreading in an integrin-independent manner. Eur J Immunol 2000;30:3403-3410.
    • (2000) Eur J Immunol , vol.30 , pp. 3403-3410
    • Borroto, A.1
  • 42
    • 0035525572 scopus 로고    scopus 로고
    • Positive and negative regulation of T-cell activation by adapter proteins
    • Koretzky GA, Myung PS. Positive and negative regulation of T-cell activation by adapter proteins. Nat Rev Immunol 2001;1:95-107.
    • (2001) Nat Rev Immunol , vol.1 , pp. 95-107
    • Koretzky, G.A.1    Myung, P.S.2
  • 43
    • 0034768532 scopus 로고    scopus 로고
    • Mechanisms of signaling by the hematopoietic-specific adapter proteins, SLP-76 and LAT and their B cell counterpart, BLNK/SLP-65
    • Yablonski D, Weiss A. Mechanisms of signaling by the hematopoietic-specific adapter proteins, SLP-76 and LAT and their B cell counterpart, BLNK/SLP-65. Adv Immunol 2001;79:93-128.
    • (2001) Adv Immunol , vol.79 , pp. 93-128
    • Yablonski, D.1    Weiss, A.2
  • 44
    • 0036162250 scopus 로고    scopus 로고
    • Signalling scaffolds and adapters in T-cell immunity
    • Geng L, Rudd CE. Signalling scaffolds and adapters in T-cell immunity. Br J Haematol 2002;116:19-27.
    • (2002) Br J Haematol , vol.116 , pp. 19-27
    • Geng, L.1    Rudd, C.E.2
  • 45
    • 0035937128 scopus 로고    scopus 로고
    • The molecular adapter SLP-76 relays signals from platelet integrin alphaIIbbeta3 to the actin cytoskeleton
    • Obergfell A, Judd BA, del Pozo MA, Schwartz MA, Koretzky GA, Shattil SJ. The molecular adapter SLP-76 relays signals from platelet integrin alphaIIbbeta3 to the actin cytoskeleton. J Biol Chem 2001;276: 5916-5923.
    • (2001) J Biol Chem , vol.276 , pp. 5916-5923
    • Obergfell, A.1    Judd, B.A.2    Del Pozo, M.A.3    Schwartz, M.A.4    Koretzky, G.A.5    Shattil, S.J.6
  • 46
    • 0036631548 scopus 로고    scopus 로고
    • VAV proteins as signal integrators for multi-subunit immune-recognition receptors
    • Turner M, Billadeau DD. VAV proteins as signal integrators for multi-subunit immune-recognition receptors. Nat Rev Immunol 2002;2:476-486.
    • (2002) Nat Rev Immunol , vol.2 , pp. 476-486
    • Turner, M.1    Billadeau, D.D.2
  • 47
    • 13144259727 scopus 로고    scopus 로고
    • Vav is a regulator of cytoskeletal reorganization mediated by the T-cell receptor
    • Fischer KD, et al. Vav is a regulator of cytoskeletal reorganization mediated by the T-cell receptor. Curr Biol 1998;8:554-562.
    • (1998) Curr Biol , vol.8 , pp. 554-562
    • Fischer, K.D.1
  • 48
    • 0031034050 scopus 로고    scopus 로고
    • Lck regulates Vav activation of members of the Rho family of GTPases
    • Han J, et al. Lck regulates Vav activation of members of the Rho family of GTPases. Mol Cell Biol 1997;17:1346-1353.
    • (1997) Mol Cell Biol , vol.17 , pp. 1346-1353
    • Han, J.1
  • 49
    • 0034292369 scopus 로고    scopus 로고
    • CD28 utilizes Vav-1 to enhance TCR-proximal signaling and NF-AT activation
    • Michel F, et al. CD28 utilizes Vav-1 to enhance TCR-proximal signaling and NF-AT activation. J Immunol 2000;165:3820-3829.
    • (2000) J Immunol , vol.165 , pp. 3820-3829
    • Michel, F.1
  • 50
    • 0037029653 scopus 로고    scopus 로고
    • Vav1 transduces T cell receptor signals to the activation of phospholipase C-gamma1 via phosphoinositide 3-kinase-dependent and -independent pathways
    • Reynolds LF, et al. Vav1 transduces T cell receptor signals to the activation of phospholipase C-gamma1 via phosphoinositide 3-kinase-dependent and -independent pathways. J Exp Med 2002;195:1103-1114.
    • (2002) J Exp Med , vol.195 , pp. 1103-1114
    • Reynolds, L.F.1
  • 51
    • 0028956337 scopus 로고
    • Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav
    • Tarakhovsky A, et al. Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav. Nature 1995;374: 467-470.
    • (1995) Nature , vol.374 , pp. 467-470
    • Tarakhovsky, A.1
  • 52
    • 0032493028 scopus 로고    scopus 로고
    • Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction
    • Holsinger LJ, et al. Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction. Curr Biol 1998;8:563-572.
    • (1998) Curr Biol , vol.8 , pp. 563-572
    • Holsinger, L.J.1
  • 53
    • 0034730182 scopus 로고    scopus 로고
    • The vav exchange factor is an essential regulator in actin-dependent receptor translocation to the lymphocyte-antigen-presenting cell interface
    • Wulfing C, Bauch A, Crabtree GR, Davis MM. The vav exchange factor is an essential regulator in actin-dependent receptor translocation to the lymphocyte-antigen-presenting cell interface. Proc Natl Acad Sci USA 2000;97:10150-10155.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10150-10155
    • Wulfing, C.1    Bauch, A.2    Crabtree, G.R.3    Davis, M.M.4
  • 54
    • 0035851918 scopus 로고    scopus 로고
    • Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells
    • Villalba M, Bi K, Rodriguez F, Tanaka Y, Schoenberger S, Altman A. Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells. J Cell Biol 2001;155:331-338.
    • (2001) J Cell Biol , vol.155 , pp. 331-338
    • Villalba, M.1    Bi, K.2    Rodriguez, F.3    Tanaka, Y.4    Schoenberger, S.5    Altman, A.6
  • 55
    • 0036180783 scopus 로고    scopus 로고
    • Vav cooperates with CD28 to induce NF-kappaB activation via a pathway involving Rac-1 and mitogen-activated kinase kinase 1
    • Marinari B, et al. Vav cooperates with CD28 to induce NF-kappaB activation via a pathway involving Rac-1 and mitogen-activated kinase kinase 1. Eur J Immunol 2002;32:447-456.
    • (2002) Eur J Immunol , vol.32 , pp. 447-456
    • Marinari, B.1
  • 56
    • 0036179031 scopus 로고    scopus 로고
    • F-actin dynamics control segregation of the TCR signaling cascade to clustered lipid rafts
    • Valensin S, et al. F-actin dynamics control segregation of the TCR signaling cascade to clustered lipid rafts. Eur J Immunol 2002;32:435-446.
    • (2002) Eur J Immunol , vol.32 , pp. 435-446
    • Valensin, S.1
  • 57
    • 0037081677 scopus 로고    scopus 로고
    • The Rho GTPase family: A Racs to Wrchs story
    • Wherlock M, Mellor H. The Rho GTPase family: a Racs to Wrchs story. J Cell Sci 2002;115:239-240.
    • (2002) J Cell Sci , vol.115 , pp. 239-240
    • Wherlock, M.1    Mellor, H.2
  • 58
    • 0034983715 scopus 로고    scopus 로고
    • WASP and WAVE family proteins: Key molecules for rapid rearrangement of cortical actin filaments and cell movement
    • Takenawa T, Miki H. WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement. J Cell Sci 2001;114: 1801-1809.
    • (2001) J Cell Sci , vol.114 , pp. 1801-1809
    • Takenawa, T.1    Miki, H.2
  • 59
    • 0034877142 scopus 로고    scopus 로고
    • Wasp recruitment to the T cell: APC contact site occurs independently of Cdc42 activation
    • Cannon JL, et al. Wasp recruitment to the T cell: APC contact site occurs independently of Cdc42 activation. Immunity 2001;15: 249-259.
    • (2001) Immunity , vol.15 , pp. 249-259
    • Cannon, J.L.1
  • 60
    • 0037046378 scopus 로고    scopus 로고
    • ADAP-ting TCR signaling to integrins
    • Griffiths EK, Penninger JM. ADAP-ting TCR signaling to integrins. Sci STKE 2002;2002:RE3.
    • (2002) Sci STKE , vol.2002
    • Griffiths, E.K.1    Penninger, J.M.2
  • 61
    • 0036604987 scopus 로고    scopus 로고
    • Communication between the TCR and integrins: Role of the molecular adapter ADAP/Fyb/Slap
    • Griffiths EK, Penninger JM. Communication between the TCR and integrins: role of the molecular adapter ADAP/Fyb/Slap. Curr Opin Immunol 2002;14:317-322.
    • (2002) Curr Opin Immunol , vol.14 , pp. 317-322
    • Griffiths, E.K.1    Penninger, J.M.2
  • 62
    • 0030737886 scopus 로고    scopus 로고
    • Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production
    • da Silva AJ, Li Z, de Vera C, Canto E, Findell P, Rudd CE. Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production. Proc Natl Acad Sci USA 1997;94:7493-7498.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7493-7498
    • Da Silva, A.J.1    Li, Z.2    De Vera, C.3    Canto, E.4    Findell, P.5    Rudd, C.E.6
  • 63
    • 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 AS, Konradt M, Monner D, Gertler FB, 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 2000;149:181-194.
    • (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
  • 64
    • 0035929128 scopus 로고    scopus 로고
    • Positive regulation of T cell activation and integrin adhesion by the adapter Fyb/Slap
    • Griffiths EK, et al. Positive regulation of T cell activation and integrin adhesion by the adapter Fyb/Slap. Science 2001;293:2260-2263.
    • (2001) Science , vol.293 , pp. 2260-2263
    • Griffiths, E.K.1
  • 65
    • 0035929222 scopus 로고    scopus 로고
    • Coupling of the TCR to integrin activation by Slap-130/Fyb
    • Peterson EJ, et al. Coupling of the TCR to integrin activation by Slap-130/Fyb. Science 2001;293:2263-2265.
    • (2001) Science , vol.293 , pp. 2263-2265
    • Peterson, E.J.1
  • 66
    • 0029126878 scopus 로고
    • Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains
    • Rivero-Lezcano OM, Marcilla A, Sameshima JH, Robbins KC. Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains. Mol Cell Biol 1995;15:5725-5731.
    • (1995) Mol Cell Biol , vol.15 , pp. 5725-5731
    • Rivero-Lezcano, O.M.1    Marcilla, A.2    Sameshima, J.H.3    Robbins, K.C.4
  • 67
    • 0032516877 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adapter protein Nck
    • Anton IM, Lu W, Mayer BJ, Ramesh N, Geha RS. The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adapter protein Nck. J Biol Chem 1998;273:20992-20995.
    • (1998) J Biol Chem , vol.273 , pp. 20992-20995
    • Anton, I.M.1    Lu, W.2    Mayer, B.J.3    Ramesh, N.4    Geha, R.S.5
  • 68
    • 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;109:901-912.
    • (2002) Cell , vol.109 , pp. 901-912
    • Gil, D.1    Schamel, W.W.2    Montoya, M.3    Sanchez-Madrid, F.4    Alarcon, B.5
  • 69
    • 0037047353 scopus 로고    scopus 로고
    • A new trigger for T cells
    • Davis M. A new trigger for T cells. Cell 2002;110:285.
    • (2002) Cell , vol.110 , pp. 285
    • Davis, M.1
  • 70
    • 0033960791 scopus 로고    scopus 로고
    • How WASP-family proteins and the Arp2/3 complex convert intracellular signals into cytoskeletal structures
    • Mullins RD. How WASP-family proteins and the Arp2/3 complex convert intracellular signals into cytoskeletal structures. Curr Opin Cell Biol 2000;12:91-96.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 91-96
    • Mullins, R.D.1
  • 71
    • 0035846598 scopus 로고    scopus 로고
    • Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities
    • Zalevsky J, Lempert L, Kranitz H, Mullins RD. Different WASP family proteins stimulate different Arp2/3 complex-dependent actinnucleating activities. Curr Biol 2001;11: 1903-1913.
    • (2001) Curr Biol , vol.11 , pp. 1903-1913
    • Zalevsky, J.1    Lempert, L.2    Kranitz, H.3    Mullins, R.D.4
  • 72
    • 0034776550 scopus 로고    scopus 로고
    • The Arp2/3 complex: A central regulator of the actin cytoskeleton
    • May RC. The Arp2/3 complex: a central regulator of the actin cytoskeleton. Cell Mol Life Sci 2001;58:1607-1626.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1607-1626
    • May, R.C.1
  • 73
    • 0035911160 scopus 로고    scopus 로고
    • Rab27a is required for regulated secretion in cytotoxic T lymphocytes
    • Stinchcombe JC, et al. Rab27a is required for regulated secretion in cytotoxic T lymphocytes. J Cell Biol 2001;152:825-834.
    • (2001) J Cell Biol , vol.152 , pp. 825-834
    • Stinchcombe, J.C.1
  • 74
    • 0035757636 scopus 로고    scopus 로고
    • Linking cellular activation to cytoskeletal reorganization: Wiskott-Aldrich syndrome as a model
    • Stewart DM, Tian L, Nelson DL. Linking cellular activation to cytoskeletal reorganization: Wiskott-Aldrich syndrome as a model. Curr Opin Allergy Clin Immunol 2001;1:525-533.
    • (2001) Curr Opin Allergy Clin Immunol , vol.1 , pp. 525-533
    • Stewart, D.M.1    Tian, L.2    Nelson, D.L.3
  • 75
    • 0036468733 scopus 로고    scopus 로고
    • Regulation of Wiskott-Aldrich syndrome protein and related molecules
    • Caron E. Regulation of Wiskott-Aldrich syndrome protein and related molecules. Curr Opin Cell Biol 2002;14:82-87.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 82-87
    • Caron, E.1
  • 76
    • 0036717243 scopus 로고    scopus 로고
    • Wasp in immune-system organization and function
    • Thrasher AJ. Wasp in immune-system organization and function. Nat Rev Immunol 2002;2:635-646.
    • (2002) Nat Rev Immunol , vol.2 , pp. 635-646
    • Thrasher, A.J.1
  • 77
    • 0022893107 scopus 로고
    • Morphological abnormalities in the lymphocytes of patients with the Wiskott-Aldrich syndrome
    • Kenney D, Cairns L, Remold-O'Donnell E, Peterson J, Rosen FS, Parkman R. Morphological abnormalities in the lymphocytes of patients with the Wiskott-Aldrich syndrome. Blood 1986;68:1329-1332.
    • (1986) Blood , vol.68 , pp. 1329-1332
    • Kenney, D.1    Cairns, L.2    Remold-O'Donnell, E.3    Peterson, J.4    Rosen, F.S.5    Parkman, R.6
  • 78
    • 0029844719 scopus 로고    scopus 로고
    • Multiple antigens are altered on T and B lymphocytes from peripheral blood and spleen of patients with Wiskott-Aldrich syndrome
    • Gerwin N, Friedrich C, Perez-Atayde A, Rosen FS, Gutierrez-Ramos JC. Multiple antigens are altered on T and B lymphocytes from peripheral blood and spleen of patients with Wiskott-Aldrich syndrome. Clin Exp Immunol 1996;106:208-217.
    • (1996) Clin Exp Immunol , vol.106 , pp. 208-217
    • Gerwin, N.1    Friedrich, C.2    Perez-Atayde, A.3    Rosen, F.S.4    Gutierrez-Ramos, J.C.5
  • 79
    • 0037138362 scopus 로고    scopus 로고
    • EVH1 domains: Structure, function and interactions
    • Ball LJ, Jarchau T, Oschkinat H, Walter U. EVH1 domains: structure, function and interactions. FEBS Lett 2002;513:45-52.
    • (2002) FEBS Lett , vol.513 , pp. 45-52
    • Ball, L.J.1    Jarchau, T.2    Oschkinat, H.3    Walter, U.4
  • 80
    • 0035887776 scopus 로고    scopus 로고
    • Overexpression of the Wiskott-Aldrich syndrome protein N-terminal domain in transgenic mice inhibits T cell proliferative responses via TCR signaling without affecting cytoskeletal rearrangements
    • Sato M, et al. Overexpression of the Wiskott-Aldrich syndrome protein N-terminal domain in transgenic mice inhibits T cell proliferative responses via TCR signaling without affecting cytoskeletal rearrangements. J Immunol 2001;167:4701-4709.
    • (2001) J Immunol , vol.167 , pp. 4701-4709
    • Sato, M.1
  • 81
    • 0035003138 scopus 로고    scopus 로고
    • WIP regulates N-WASP-mediated actin polymerization and filopodium formation
    • Martinez-Quiles N, et al. WIP regulates N-WASP-mediated actin polymerization and filopodium formation. Nat Cell Biol 2001;3:484-491.
    • (2001) Nat Cell Biol , vol.3 , pp. 484-491
    • Martinez-Quiles, N.1
  • 82
    • 0036198683 scopus 로고    scopus 로고
    • WIP deficiency reveals a differential role for WIP and the actin cytoskeleton in T and B cell activation
    • Anton IM, et al. WIP deficiency reveals a differential role for WIP and the actin cytoskeleton in T and B cell activation. Immunity 2002;16:193-204.
    • (2002) Immunity , vol.16 , pp. 193-204
    • Anton, I.M.1
  • 83
    • 0034654348 scopus 로고    scopus 로고
    • Cutting edge: WIP, a binding partner for Wiskott-Aldrich syndrome protein, cooperates with Vav in the regulation of T cell activation
    • Savoy DN, Billadeau DD, Leibson PJ. Cutting edge: WIP, a binding partner for Wiskott-Aldrich syndrome protein, cooperates with Vav in the regulation of T cell activation. J Immunol 2000;164:2866-2870.
    • (2000) J Immunol , vol.164 , pp. 2866-2870
    • Savoy, D.N.1    Billadeau, D.D.2    Leibson, P.J.3
  • 84
    • 0035877803 scopus 로고    scopus 로고
    • A role for Wiskott-Aldrich syndrome protein in T-cell receptor-mediated transcriptional activation independent of actin polymerization
    • Silvin C, Belisle B, Abo A. A role for Wiskott-Aldrich syndrome protein in T-cell receptor-mediated transcriptional activation independent of actin polymerization. J Biol Chem 2001;276:21450-21457.
    • (2001) J Biol Chem , vol.276 , pp. 21450-21457
    • Silvin, C.1    Belisle, B.2    Abo, A.3
  • 85
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 2000;404: 151-158.
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 86
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate
    • Rohatgi R, Ho HY, Kirschner MW. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate. J Cell Biol 2000;150:1299-1310.
    • (2000) J Cell Biol , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 87
    • 0036199184 scopus 로고    scopus 로고
    • Vav1 controls integrin clustering and MHC/peptide-specific cell adhesion to antigen-presenting
    • Krawczyk C, et al. Vav1 controls integrin clustering and MHC/peptide-specific cell adhesion to antigen-presenting Immunity 2002;16:331-343.
    • (2002) Immunity , vol.16 , pp. 331-343
    • Krawczyk, C.1
  • 88
    • 0030793720 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells
    • She HY, et al. Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells. Mol Biol Cell 1997;8:1709-1721.
    • (1997) Mol Biol Cell , vol.8 , pp. 1709-1721
    • She, H.Y.1
  • 89
    • 0030221475 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases
    • Banin S, Truong O, Katz DR, Waterfield MD, Brickell PM, Gout I. Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases. Curr Biol 1996;6:981-988.
    • (1996) Curr Biol , vol.6 , pp. 981-988
    • Banin, S.1    Truong, O.2    Katz, D.R.3    Waterfield, M.D.4    Brickell, P.M.5    Gout, I.6
  • 91
    • 0030000795 scopus 로고    scopus 로고
    • Identification of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains
    • Finan PM, et al. Identification of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains. J Biol Chem 1996;271:26291-26295.
    • (1996) J Biol Chem , vol.271 , pp. 26291-26295
    • Finan, P.M.1
  • 92
    • 0035809163 scopus 로고    scopus 로고
    • A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42
    • Fukuoka M, Suetsugu S, Miki H, Fukami K, Endo T, Takenawa T. A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42. J Cell Biol 2001;152:471-482.
    • (2001) J Cell Biol , vol.152 , pp. 471-482
    • Fukuoka, M.1    Suetsugu, S.2    Miki, H.3    Fukami, K.4    Endo, T.5    Takenawa, T.6
  • 93
    • 0037133297 scopus 로고    scopus 로고
    • WASp verprolin homology, cofilin homology, and acidic region domain-mediated actin polymerization is required for T cell development
    • Zhang J, Shi F, Badour K, Deng Y, McGavin MK, Siminovitch KA. WASp verprolin homology, cofilin homology, and acidic region domain-mediated actin polymerization is required for T cell development. Proc Natl Acad Sci USA 2002;99:2240-2245.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2240-2245
    • Zhang, J.1    Shi, F.2    Badour, K.3    Deng, Y.4    McGavin, M.K.5    Siminovitch, K.A.6
  • 94
    • 0037138384 scopus 로고    scopus 로고
    • WH2 domain: A small, versatile adapter for actin monomers
    • Paunola E, Mattila PK, Lappalainen P. WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett 2002;513:92-97.
    • (2002) FEBS Lett , vol.513 , pp. 92-97
    • Paunola, E.1    Mattila, P.K.2    Lappalainen, P.3
  • 95
    • 0035905308 scopus 로고    scopus 로고
    • The intersectin 2 adapter links Wiskott Aldrich Syndrome protein (WASp)-mediated actin polymerization to T cell antigen receptor endocytosis
    • McGavin MK, Badour K, Hardy LA, Kubiseski TJ, Zhang J, Siminovitch KA. The intersectin 2 adapter links Wiskott Aldrich Syndrome protein (WASp)-mediated actin polymerization to T cell antigen receptor endocytosis. J Exp Med 2001;194:1777-1787.
    • (2001) J Exp Med , vol.194 , pp. 1777-1787
    • McGavin, M.K.1    Badour, K.2    Hardy, L.A.3    Kubiseski, T.J.4    Zhang, J.5    Siminovitch, K.A.6
  • 96
    • 0035475450 scopus 로고    scopus 로고
    • Cortactin: Coupling membrane dynamics to cortical actin assembly
    • Weed SA, Parsons JT. Cortactin: coupling membrane dynamics to cortical actin assembly. Oncogene 2001;20:6418-6434.
    • (2001) Oncogene , vol.20 , pp. 6418-6434
    • Weed, S.A.1    Parsons, J.T.2
  • 98
    • 0029009255 scopus 로고
    • LckBP1, a proline-rich protein expressed in haematopoietic lineage cells, directly associates with the SH3 domain of protein tyrosine kinase p56lck
    • Takemoto Y, Furuta M, Li XK, Strong-Sparks WJ, Hashimoto Y. LckBP1, a proline-rich protein expressed in haematopoietic lineage cells, directly associates with the SH3 domain of protein tyrosine kinase p56lck. EMBO J 1995;14:3403-3414.
    • (1995) EMBO J , vol.14 , pp. 3403-3414
    • Takemoto, Y.1    Furuta, M.2    Li, X.K.3    Strong-Sparks, W.J.4    Hashimoto, Y.5
  • 99
    • 0029828378 scopus 로고    scopus 로고
    • Distinct binding patterns of HS1 to the Src SH2 and SH3 domains reflect possible mechanisms of recruitment and activation of downstream molecules
    • Takemoto Y, Sato M, Furuta M, Hashimoto Y. Distinct binding patterns of HS1 to the Src SH2 and SH3 domains reflect possible mechanisms of recruitment and activation of downstream molecules. Int Immunol 1996;8:1699-1705.
    • (1996) Int Immunol , vol.8 , pp. 1699-1705
    • Takemoto, Y.1    Sato, M.2    Furuta, M.3    Hashimoto, Y.4
  • 100
    • 0033406870 scopus 로고    scopus 로고
    • Isolation and characterization of a novel HS1 SH3 domain binding protein, HS1BP3
    • Takemoto Y, Furuta M, Sato M, Kubo M, Hashimoto Y. Isolation and characterization of a novel HS1 SH3 domain binding protein, HS1BP3. Int Immunol 1999;11:1957-1964.
    • (1999) Int Immunol , vol.11 , pp. 1957-1964
    • Takemoto, Y.1    Furuta, M.2    Sato, M.3    Kubo, M.4    Hashimoto, Y.5
  • 101
    • 18444389953 scopus 로고    scopus 로고
    • Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility
    • Bear JE, et al. Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility. Cell 2002;109:509-521.
    • (2002) Cell , vol.109 , pp. 509-521
    • Bear, J.E.1
  • 102
    • 0035211279 scopus 로고    scopus 로고
    • Evidence for a molecular complex consisting of Fyb/SLAP, SLP-76, Nck, VASP and WASP that links the actin cytoskeleton to Fcgamma receptor signalling during phagocytosis
    • Coppolino MG, et al. Evidence for a molecular complex consisting of Fyb/SLAP, SLP-76, Nck, VASP and WASP that links the actin cytoskeleton to Fcgamma receptor signalling during phagocytosis. J Cell Sci 2001;114:4307-4318.
    • (2001) J Cell Sci , vol.114 , pp. 4307-4318
    • Coppolino, M.G.1
  • 103
    • 0034680938 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains
    • Lambrechts A, et al. cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains. J Biol Chem 2000;275:36143-36151.
    • (2000) J Biol Chem , vol.275 , pp. 36143-36151
    • Lambrechts, A.1
  • 104
    • 0034683671 scopus 로고    scopus 로고
    • Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex
    • Higgs HN, Pollard TD. Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J Cell Biol 2000;150:1311-1320.
    • (2000) J Cell Biol , vol.150 , pp. 1311-1320
    • Higgs, H.N.1    Pollard, T.D.2
  • 105
  • 107
    • 0033965314 scopus 로고    scopus 로고
    • Control of actin assembly and disassembly at filament ends
    • Cooper JA, Schafer DA. Control of actin assembly and disassembly at filament ends. Curr Opin Cell Biol 2000;12:97-103.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 97-103
    • Cooper, J.A.1    Schafer, D.A.2
  • 108
    • 0032966363 scopus 로고    scopus 로고
    • Functions of gelsolin: Motility, signaling, apoptosis, cancer
    • Kwiatkowski DJ. Functions of gelsolin: motility, signaling, apoptosis, cancer. Curr Opin Cell Biol 1999;11:103-108.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 103-108
    • Kwiatkowski, D.J.1
  • 109
    • 0032538888 scopus 로고    scopus 로고
    • The essential role of profilin in the assembly of actin for microspike formation
    • Suetsugu S, Miki H, Takenawa T. The essential role of profilin in the assembly of actin for microspike formation. EMBO J 1998;17:6516-6526.
    • (1998) EMBO J , vol.17 , pp. 6516-6526
    • Suetsugu, S.1    Miki, H.2    Takenawa, T.3
  • 110
    • 0033853360 scopus 로고    scopus 로고
    • Regulating actin dynamics in neuronal growth cones by ADF/cofilin and rho family GTPases
    • Kuhn TB, et al. Regulating actin dynamics in neuronal growth cones by ADF/cofilin and rho family GTPases. J Neurobiol 2000;44:126-144.
    • (2000) J Neurobiol , vol.44 , pp. 126-144
    • Kuhn, T.B.1
  • 111
    • 0034004460 scopus 로고    scopus 로고
    • Cofilin: A missing link between T cell co-stimulation and rearrangement of the actin cytoskeleton
    • Lee KH, Meuer SC, Samstag Y. Cofilin: a missing link between T cell co-stimulation and rearrangement of the actin cytoskeleton. Eur J Immunol 2000;30:892-899.
    • (2000) Eur J Immunol , vol.30 , pp. 892-899
    • Lee, K.H.1    Meuer, S.C.2    Samstag, Y.3
  • 112
    • 0034536444 scopus 로고    scopus 로고
    • The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes
    • Ambach A, Saunus J, Konstandin M, Wesselborg S, Meuer SC, Samstag Y. The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes. Eur J Immunol 2000;30:3422-3431.
    • (2000) Eur J Immunol , vol.30 , pp. 3422-3431
    • Ambach, A.1    Saunus, J.2    Konstandin, M.3    Wesselborg, S.4    Meuer, S.C.5    Samstag, Y.6
  • 113
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards DC, Sanders LC, Bokoch GM, Gill GN. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat Cell Biol 1999;1:253-259.
    • (1999) Nat Cell Biol , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 114
    • 0033529620 scopus 로고    scopus 로고
    • Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase
    • Maekawa M, et al. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 1999;285:895-898.
    • (1999) Science , vol.285 , pp. 895-898
    • Maekawa, M.1
  • 116
    • 0036223236 scopus 로고    scopus 로고
    • p21-activated kinases: Three more join the Pak
    • Jaffer ZM, Chernoff J. p21-activated kinases: three more join the Pak. Int J Biochem Cell Biol 2002;34:713-717.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 713-717
    • Jaffer, Z.M.1    Chernoff, J.2
  • 117
    • 0034715885 scopus 로고    scopus 로고
    • Regulation and functions of Rho-associated kinase
    • Amano M, Fukata Y, Kaibuchi K. Regulation and functions of Rho-associated kinase. Exp Cell Res 2000;261:44-51.
    • (2000) Exp Cell Res , vol.261 , pp. 44-51
    • Amano, M.1    Fukata, Y.2    Kaibuchi, K.3
  • 118
    • 0032188987 scopus 로고    scopus 로고
    • A Nck-Pak1 signaling module is required for T-cell receptor-mediated activation of NFAT, but not of JNK
    • Yablonski D, Kane LP, Qian D, Weiss A. A Nck-Pak1 signaling module is required for T-cell receptor-mediated activation of NFAT, but not of JNK. EMBO J 1998;17:5647-5657.
    • (1998) EMBO J , vol.17 , pp. 5647-5657
    • Yablonski, D.1    Kane, L.P.2    Qian, D.3    Weiss, A.4
  • 119
    • 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;20:457-465.
    • (2001) EMBO J , vol.20 , pp. 457-465
    • Ku, G.M.1    Yablonski, D.2    Manser, E.3    Lim, L.4    Weiss, A.5
  • 120
    • 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, 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;157:1233-1245.
    • (2002) J Cell Biol , vol.157 , pp. 1233-1245
    • Barreiro, O.1
  • 121
    • 0035652354 scopus 로고    scopus 로고
    • Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adapter moesin
    • Delon J, Kaibuchi K, Germain RN. Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adapter moesin. Immunity 2001;15:691-701.
    • (2001) Immunity , vol.15 , pp. 691-701
    • Delon, J.1    Kaibuchi, K.2    Germain, R.N.3
  • 122
    • 0035654721 scopus 로고    scopus 로고
    • The membrane-microfilament linker ezrin is involved in the formation of the immunological synapse and in T cell activation
    • Roumier A, et al. The membrane-microfilament linker ezrin is involved in the formation of the immunological synapse and in T cell activation. Immunity 2001;15:715-728.
    • (2001) Immunity , vol.15 , pp. 715-728
    • Roumier, A.1
  • 123
    • 0036346708 scopus 로고    scopus 로고
    • ERM proteins and merlin: Integrators at the cell cortex
    • Bretscher A, Edwards K, Fehon RG. ERM proteins and merlin: integrators at the cell cortex. Nat Rev Mol Cell Biol 2002;3:586-599.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 586-599
    • Bretscher, A.1    Edwards, K.2    Fehon, R.G.3
  • 124
    • 0033677862 scopus 로고    scopus 로고
    • The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane
    • Sechi AS, Wehland J. The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane. J Cell Sci 2000;113:3685-3695.
    • (2000) J Cell Sci , vol.113 , pp. 3685-3695
    • Sechi, A.S.1    Wehland, J.2
  • 125
    • 0033953888 scopus 로고    scopus 로고
    • Functional cooperation between the microtubule and actin cytoskeletons
    • Goode BL, Drubin DG, Barnes G. Functional cooperation between the microtubule and actin cytoskeletons. Curr Opin Cell Biol 2000;12:63-71.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 63-71
    • Goode, B.L.1    Drubin, D.G.2    Barnes, G.3
  • 126
    • 0020365635 scopus 로고
    • Spatial relationships of microtubule-organizing centers and the contact area of cytotoxic T lymphocytes and target cells
    • Geiger B, Rosen D, Berke G. Spatial relationships of microtubule-organizing centers and the contact area of cytotoxic T lymphocytes and target cells. J Cell Biol 1982;95:137-143.
    • (1982) J Cell Biol , vol.95 , pp. 137-143
    • Geiger, B.1    Rosen, D.2    Berke, G.3
  • 127
    • 0022362235 scopus 로고
    • The reorientation of the Golgi apparatus and the microtubule-organizing center in the cytotoxic effector cell is a prerequisite in the lysis of bound target cells
    • Kupfer A, Dennert G, Singer SJ. The reorientation of the Golgi apparatus and the microtubule-organizing center in the cytotoxic effector cell is a prerequisite in the lysis of bound target cells. J Mol Cell Immunol 1985;2:37-49.
    • (1985) J Mol Cell Immunol , vol.2 , pp. 37-49
    • Kupfer, A.1    Dennert, G.2    Singer, S.J.3
  • 128
    • 0025978984 scopus 로고
    • Polarized expression of cytokines in cell conjugates of helper T cells and splenic B cells
    • Kupfer A, Mosmann TR, Kupfer H. Polarized expression of cytokines in cell conjugates of helper T cells and splenic B cells. Proc Natl Acad Sci USA 1991;88:775-779.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 775-779
    • Kupfer, A.1    Mosmann, T.R.2    Kupfer, H.3
  • 129
    • 0035911150 scopus 로고    scopus 로고
    • Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice
    • Haddad EK, Wu X, Hammer JA 3rd, Henkart PA. Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice. J Cell Biol 2001;152:835-842.
    • (2001) J Cell Biol , vol.152 , pp. 835-842
    • Haddad, E.K.1    Wu, X.2    Hammer J.A. III3    Henkart, P.A.4
  • 130
    • 0035652265 scopus 로고    scopus 로고
    • FERMing up the synapse
    • Shaw AS. FERMing up the synapse. Immunity 2001;15:683-686.
    • (2001) Immunity , vol.15 , pp. 683-686
    • Shaw, A.S.1
  • 131
    • 18244364886 scopus 로고    scopus 로고
    • ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse
    • Allenspach EJ, et al. ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse. Immunity 2001;15:739-750.
    • (2001) Immunity , vol.15 , pp. 739-750
    • Allenspach, E.J.1
  • 132
    • 0034644538 scopus 로고    scopus 로고
    • Translocation and reversible localization of signaling proteins: A dynamic future for signal transduction
    • Teruel MN, Meyer T. Translocation and reversible localization of signaling proteins: a dynamic future for signal transduction. Cell 2000;103:181-184.
    • (2000) Cell , vol.103 , pp. 181-184
    • Teruel, M.N.1    Meyer, T.2
  • 133
    • 0036595397 scopus 로고    scopus 로고
    • Cytotoxic T lymphocytes: All roads lead to death
    • Barry M, Bleackley RC. Cytotoxic T lymphocytes: all roads lead to death. Nat Rev Immunol 2002;2:401-409.
    • (2002) Nat Rev Immunol , vol.2 , pp. 401-409
    • Barry, M.1    Bleackley, R.C.2
  • 134
    • 0022592627 scopus 로고
    • On the mechanism of unidirectional killing in mixtures of two cytotoxic T lymphocytes. Unidirectional polarization of cytoplasmic organelles and the membrane-associated cytoskeleton in the effector cell
    • Kupfer A, Singer SJ, Dennert G. On the mechanism of unidirectional killing in mixtures of two cytotoxic T lymphocytes. Unidirectional polarization of cytoplasmic organelles and the membrane-associated cytoskeleton in the effector cell. J Exp Med 1986;163:489-498.
    • (1986) J Exp Med , vol.163 , pp. 489-498
    • Kupfer, A.1    Singer, S.J.2    Dennert, G.3
  • 135
    • 0024327897 scopus 로고
    • Cell biology of cytotoxic and helper T cell functions: Immunofluorescence microscopic studies of single cells and cell couples
    • Kupfer A, Singer SJ. Cell biology of cytotoxic and helper T cell functions: immunofluorescence microscopic studies of single cells and cell couples. Annu Rev Immunol 1989;7:309-337.
    • (1989) Annu Rev Immunol , vol.7 , pp. 309-337
    • Kupfer, A.1    Singer, S.J.2
  • 136
    • 0028354216 scopus 로고
    • Small splenic B cells that bind to antigen-specific T helper (Th) cells and face the site of cytokine production in the Th cells selectively proliferate: Immunofluorescence microscopic studies of Th-B antigen-presenting cell interactions
    • Kupfer H, Monks CR, Kupfer A. Small splenic B cells that bind to antigen-specific T helper (Th) cells and face the site of cytokine production in the Th cells selectively proliferate: immunofluorescence microscopic studies of Th-B antigen-presenting cell interactions. J Exp Med 1994;179:1507-1515.
    • (1994) J Exp Med , vol.179 , pp. 1507-1515
    • Kupfer, H.1    Monks, C.R.2    Kupfer, A.3
  • 137
    • 0029008280 scopus 로고
    • Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42
    • Stowers L, Yelon D, Berg LJ, Chant J. Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42. Proc Natl Acad Sci USA 1995;92:5027-5031.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5027-5031
    • Stowers, L.1    Yelon, D.2    Berg, L.J.3    Chant, J.4
  • 138
    • 0026008413 scopus 로고
    • Cytoskeletal function in CD8- and T cell receptor-mediated interaction of cytotoxic T lymphocytes with class I protein
    • O'Rourke AM, Apgar JR, Kane KP, Martz E, Mescher MF. Cytoskeletal function in CD8- and T cell receptor-mediated interaction of cytotoxic T lymphocytes with class I protein. J Exp Med 1991;173:241-249.
    • (1991) J Exp Med , vol.173 , pp. 241-249
    • O'Rourke, A.M.1    Apgar, J.R.2    Kane, K.P.3    Martz, E.4    Mescher, M.F.5
  • 140
    • 0035500642 scopus 로고    scopus 로고
    • CD8(+) tumor-infiltrating T cells are deficient in perforin-mediated cytolytic activity due to defective microtubule-organizing center mobilization and lytic granule exocytosis
    • Radoja S, Saio M, Schaer D, Koneru M, Vukmanovic S, Frey AB. CD8(+) tumor-infiltrating T cells are deficient in perforin-mediated cytolytic activity due to defective microtubule-organizing center mobilization and lytic granule exocytosis. J Immunol 2001;167:5042-5051.
    • (2001) J Immunol , vol.167 , pp. 5042-5051
    • Radoja, S.1    Saio, M.2    Schaer, D.3    Koneru, M.4    Vukmanovic, S.5    Frey, A.B.6
  • 141
    • 0029582940 scopus 로고
    • Interactions between the protein-tyrosine kinase ZAP-70, the proto-oncoprotein Vav, and tubulin in Jurkat T cells
    • Huby RD, Carlile GW, Ley SC. Interactions between the protein-tyrosine kinase ZAP-70, the proto-oncoprotein Vav, and tubulin in Jurkat T cells. J Biol Chem 1995;270:30241-30244.
    • (1995) J Biol Chem , vol.270 , pp. 30241-30244
    • Huby, R.D.1    Carlile, G.W.2    Ley, S.C.3
  • 142
    • 0032524614 scopus 로고    scopus 로고
    • Nocodazole inhibits signal transduction by the T cell antigen receptor
    • Huby RD, Weiss A, Ley SC. Nocodazole inhibits signal transduction by the T cell antigen receptor. J Biol Chem 1998;273:12024-12031.
    • (1998) J Biol Chem , vol.273 , pp. 12024-12031
    • Huby, R.D.1    Weiss, A.2    Ley, S.C.3
  • 143
    • 0036166541 scopus 로고    scopus 로고
    • Dynamic polarization of the microtubule cytoskeleton during CTL-mediated killing
    • Kuhn JR, Poenie M. Dynamic polarization of the microtubule cytoskeleton during CTL-mediated killing. Immunity 2002;16:111-121.
    • (2002) Immunity , vol.16 , pp. 111-121
    • Kuhn, J.R.1    Poenie, M.2
  • 144
    • 0031785762 scopus 로고    scopus 로고
    • Prevention of antigen-induced microtubule organizing center reorientation in cytotoxic T cells by modulation of protein kinase C activity
    • Nesic D, Henderson S, Vukmanovic S. Prevention of antigen-induced microtubule organizing center reorientation in cytotoxic T cells by modulation of protein kinase C activity. Int Immunol 1998;10:1741-1746.
    • (1998) Int Immunol , vol.10 , pp. 1741-1746
    • Nesic, D.1    Henderson, S.2    Vukmanovic, S.3
  • 145
    • 0031179387 scopus 로고    scopus 로고
    • Interaction between cytolytic T-cells and immobilized renal tubular epithelial cells. Evidence of polarity on both effector and targeT cells
    • Papadimitriou JC, Drachenberg CB, Hadley GA, Bartlett ST, Trump BF. Interaction between cytolytic T-cells and immobilized renal tubular epithelial cells. evidence of polarity on both effector and targeT cells. J Submicrosc Cytol Pathol 1997;29:379-386.
    • (1997) J Submicrosc Cytol Pathol , vol.29 , pp. 379-386
    • Papadimitriou, J.C.1    Drachenberg, C.B.2    Hadley, G.A.3    Bartlett, S.T.4    Trump, B.F.5
  • 146
    • 0025959534 scopus 로고
    • The intracellular distribution of cell organelles in natural killer cells during the cytolysis of bound tumor cells, with special reference to the rod-cored vesicles
    • Kaneda K, Kataoka M, Kishiye T, Yamamoto H, Wake K. The intracellular distribution of cell organelles in natural killer cells during the cytolysis of bound tumor cells, with special reference to the rod-cored vesicles. Arch Histol Cytol 1991;54:69-79.
    • (1991) Arch Histol Cytol , vol.54 , pp. 69-79
    • Kaneda, K.1    Kataoka, M.2    Kishiye, T.3    Yamamoto, H.4    Wake, K.5
  • 147
    • 0036230351 scopus 로고    scopus 로고
    • How Rab proteins link motors to membranes
    • Goud B. How Rab proteins link motors to membranes. Nat Cell Biol 2002;4:E77-E78.
    • (2002) Nat Cell Biol , vol.4
    • Goud, B.1
  • 150
    • 0035575614 scopus 로고    scopus 로고
    • Tir - Nck's new afficionado
    • Egile C. Tir - Nck's new afficionado. Trends Cell Biol 2001;11:461.
    • (2001) Trends Cell Biol , vol.11 , pp. 461
    • Egile, C.1
  • 151
    • 0034842129 scopus 로고    scopus 로고
    • Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells
    • Gruenheid S, et al. Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells. Nat Cell Biol 2001;3:856-859.
    • (2001) Nat Cell Biol , vol.3 , pp. 856-859
    • Gruenheid, S.1
  • 153
    • 0037205230 scopus 로고    scopus 로고
    • Tumor suppressor PTEN mediates sensing of chemoattractant gradients
    • Iijima M, Devreotes P. Tumor suppressor PTEN mediates sensing of chemoattractant gradients. Cell 2002;109:599-610.
    • (2002) Cell , vol.109 , pp. 599-610
    • Iijima, M.1    Devreotes, P.2
  • 154
    • 0037205265 scopus 로고    scopus 로고
    • Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis
    • Funamoto S, Meili R, Lee S, Parry L, Firtel RA. Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis. Cell 2002;109:611-623.
    • (2002) Cell , vol.109 , pp. 611-623
    • Funamoto, S.1    Meili, R.2    Lee, S.3    Parry, L.4    Firtel, R.A.5
  • 155
    • 0037205266 scopus 로고    scopus 로고
    • PI 3-kinases and PTEN: How opposites chemoattract
    • Comer FI, Parent CA. PI 3-kinases and PTEN: how opposites chemoattract. Cell 2002;109:541-544.
    • (2002) Cell , vol.109 , pp. 541-544
    • Comer, F.I.1    Parent, C.A.2
  • 156
    • 0036174455 scopus 로고    scopus 로고
    • Actin' up (and down)
    • Hyams JS. Actin' up (and down). Trends Cell Biol 2002;12:4-5.
    • (2002) Trends Cell Biol , vol.12 , pp. 4-5
    • Hyams, J.S.1
  • 157
    • 0030592559 scopus 로고    scopus 로고
    • Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics
    • Gertler FB, Niebuhr K, Reinhard M, Wehland J, Soriano P. Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. Cell 1996;87:227-239.
    • (1996) Cell , vol.87 , pp. 227-239
    • Gertler, F.B.1    Niebuhr, K.2    Reinhard, M.3    Wehland, J.4    Soriano, P.5
  • 158
    • 0033082452 scopus 로고    scopus 로고
    • Mena is required for neurulation and commissure formation
    • Lanier LM, et al. Mena is required for neurulation and commissure formation Neuron 1999;22:313-325.
    • (1999) Neuron , vol.22 , pp. 313-325
    • Lanier, L.M.1
  • 159
    • 0037094369 scopus 로고    scopus 로고
    • Characterization and expression analyses of the mouse Wiskott-Aldrich syndrome protein (WASP) family member Wave 1/Scar
    • Benachenhou N, Massy I, Vacher J. Characterization and expression analyses of the mouse Wiskott-Aldrich syndrome protein (WASP) family member Wave 1/Scar. Gene 2002;290:131-140.
    • (2002) Gene , vol.290 , pp. 131-140
    • Benachenhou, N.1    Massy, I.2    Vacher, J.3
  • 160
    • 0035369127 scopus 로고    scopus 로고
    • Immunology. Agrin - A bridge between the nervous and immune systems
    • Trautmann A, Vivier E. Immunology. Agrin - a bridge between the nervous and immune systems. Science 2001;292:1667-1668.
    • (2001) Science , vol.292 , pp. 1667-1668
    • Trautmann, A.1    Vivier, E.2
  • 161
    • 0034924417 scopus 로고    scopus 로고
    • Kissing cousins: Immunological and neurological synapses
    • Shaw AS, Allen PM. Kissing cousins: immunological and neurological synapses. Nat Immunol 2001;2:575-576.
    • (2001) Nat Immunol , vol.2 , pp. 575-576
    • Shaw, A.S.1    Allen, P.M.2
  • 162
    • 0035999826 scopus 로고    scopus 로고
    • Neuropilin-1: Another neuronal molecule in the 'immunological synapse'
    • Wulfing C, Rupp F. Neuropilin-1: another neuronal molecule in the 'immunological synapse'. Nat Immunol 2002;3:418-419.
    • (2002) Nat Immunol , vol.3 , pp. 418-419
    • Wulfing, C.1    Rupp, F.2
  • 163
    • 0032403083 scopus 로고    scopus 로고
    • WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac
    • Miki H, Suetsugu S, Takenawa T. WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J 1998;17:6932-6941.
    • (1998) EMBO J , vol.17 , pp. 6932-6941
    • Miki, H.1    Suetsugu, S.2    Takenawa, T.3
  • 164
    • 0034619847 scopus 로고    scopus 로고
    • IRSpS3 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • Miki H, Yamaguchi H, Suetsugu S, Takenawa T. IRSpS3 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 2000;408:732-735.
    • (2000) Nature , vol.408 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 165
    • 0037102345 scopus 로고    scopus 로고
    • Cell motility: Braking WAVEs
    • Cory GO, Ridley AJ. Cell motility: braking WAVEs. Nature 2002;418:732-733.
    • (2002) Nature , vol.418 , pp. 732-733
    • Cory, G.O.1    Ridley, A.J.2
  • 166
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden S, Rohatgi R, Podtelejnikov AV, Mann M, Kirschner MW. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 2002;418:790-793.
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 167
    • 0037117840 scopus 로고    scopus 로고
    • Controlling the immune system through semaphorins
    • Bismuth G, Boumsell L. Controlling the immune system through semaphorins. Sci STKE 2002;2002:RE4.
    • (2002) Sci STKE , vol.2002
    • Bismuth, G.1    Boumsell, L.2
  • 168
    • 0030874979 scopus 로고    scopus 로고
    • The Eph family of receptors
    • Pasquale EB. The Eph family of receptors. Curr Opin Cell Biol 1997;9:608-615.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 608-615
    • Pasquale, E.B.1
  • 169
    • 0031922119 scopus 로고    scopus 로고
    • The ephrins and Eph receptors in neural development
    • Flanagan JG, Vanderhaeghen P. The ephrins and Eph receptors in neural development. Annu Rev Neurosci 1998;21:309-345.
    • (1998) Annu Rev Neurosci , vol.21 , pp. 309-345
    • Flanagan, J.G.1    Vanderhaeghen, P.2
  • 170
    • 0036045804 scopus 로고    scopus 로고
    • EphrinA1-induced cytoskeletal re-organization requires FAK and p130(cas)
    • Carter N, Nakamoto T, Hirai H, Hunter T. EphrinA1-induced cytoskeletal re-organization requires FAK and p130(cas). Nat Cell Biol 2002;4:565-573.
    • (2002) Nat Cell Biol , vol.4 , pp. 565-573
    • Carter, N.1    Nakamoto, T.2    Hirai, H.3    Hunter, T.4
  • 171
    • 0036644318 scopus 로고    scopus 로고
    • Expression and function of the Eph A receptors and their ligands ephrins A in the rat thymus
    • Munoz JJ, et al. Expression and function of the Eph A receptors and their ligands ephrins A in the rat thymus. J Immunol 2002;169:177-184.
    • (2002) J Immunol , vol.169 , pp. 177-184
    • Munoz, J.J.1
  • 172
    • 0033533613 scopus 로고    scopus 로고
    • alphaPIX nucleotide exchange factor is activated by interaction with phosphatidylinositol 3-kinase
    • Yoshii S, et al. alphaPIX nucleotide exchange factor is activated by interaction with phosphatidylinositol 3-kinase. Oncogene 1999;18:5680-5690.
    • (1999) Oncogene , vol.18 , pp. 5680-5690
    • Yoshii, S.1
  • 173
    • 0035369125 scopus 로고    scopus 로고
    • Physiological regulation of the immunological synapse by agrin
    • Khan AA, Bose C, Yam LS, Soloski MJ, Rupp F. Physiological regulation of the immunological synapse by agrin. Science 2001;292:1681-1686.
    • (2001) Science , vol.292 , pp. 1681-1686
    • Khan, A.A.1    Bose, C.2    Yam, L.S.3    Soloski, M.J.4    Rupp, F.5
  • 174
    • 0036096843 scopus 로고    scopus 로고
    • A neuronal receptor, neuropilin-1, is essential for the initiation of the primary immune response
    • Tordjman R, et al. A neuronal receptor, neuropilin-1, is essential for the initiation of the primary immune response. Nat Immunol 2002;3:477-482.
    • (2002) Nat Immunol , vol.3 , pp. 477-482
    • Tordjman, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.