메뉴 건너뛰기




Volumn 186, Issue , 2002, Pages 90-99

The regulation of actin remodeling during T-cell-APC conjugate formation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL CYCLE PROTEIN; LEUKOCYTE ANTIGEN; LIGAND; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; PROTEIN DERIVATIVE; RECEPTOR; T LYMPHOCYTE RECEPTOR; CELL ADHESION MOLECULE; LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN; WAS PROTEIN, HUMAN; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 0036696565     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-065X.2002.18609.x     Document Type: Review
Times cited : (84)

References (85)
  • 4
    • 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
  • 5
    • 0031838741 scopus 로고    scopus 로고
    • CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts
    • Serrador JM, et al. CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts. Blood 1998;91:4632-4644.
    • (1998) Blood , vol.91 , pp. 4632-4644
    • Serrador, J.M.1
  • 6
    • 0033019133 scopus 로고    scopus 로고
    • Cytoskeletal rearrangement during migration and activation of T lymphocytes
    • Serrador JM, Nieto M, Sanchez-Madrid F. Cytoskeletal rearrangement during migration and activation of T lymphocytes. Trends Cell Biol 1999;9:228-233.
    • (1999) Trends Cell Biol , vol.9 , pp. 228-233
    • Serrador, J.M.1    Nieto, M.2    Sanchez-Madrid, F.3
  • 7
    • 0035879352 scopus 로고    scopus 로고
    • Cutting edge: Integration of human T lymphocyte cytoskeleton by the cytolinker plectin
    • Brown MJ, Hallam JA, Liu Y, Yamada KM, Shaw S. Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin. J Immunol 2001; 167:641-645.
    • (2001) J Immunol , vol.167 , pp. 641-645
    • Brown, M.J.1    Hallam, J.A.2    Liu, Y.3    Yamada, K.M.4    Shaw, S.5
  • 8
    • 0031202175 scopus 로고    scopus 로고
    • Microtubule retraction into the uropod and its role in T cell polarization and motility
    • Ratner S, Sherrod WS, Lichlyter D. Microtubule retraction into the uropod and its role in T cell polarization and motility. J Immunol 1997;159:1063-1067.
    • (1997) J Immunol , vol.159 , pp. 1063-1067
    • Ratner, S.1    Sherrod, W.S.2    Lichlyter, D.3
  • 9
    • 0025885771 scopus 로고
    • T-cell effector functions: Mechanisms for delivery of cytotoxicity and help
    • Podack ER, Kupfer A. T-cell effector functions: mechanisms for delivery of cytotoxicity and help. Annu Rev Cell Biol 1991;7:479-504.
    • (1991) Annu Rev Cell Biol , vol.7 , pp. 479-504
    • Podack, E.R.1    Kupfer, A.2
  • 11
    • 0022653477 scopus 로고
    • Reorientation and fusion of cytotoxic T lymphocyte granules after interaction with target cells as determined by high resolution cinemicrography
    • Yannelli JR, Sullivan JA, Mandell GL, Engelhard VH. Reorientation and fusion of cytotoxic T lymphocyte granules after interaction with target cells as determined by high resolution cinemicrography. J Immunol 1986;136:377-382.
    • (1986) J Immunol , vol.136 , pp. 377-382
    • Yannelli, J.R.1    Sullivan, J.A.2    Mandell, G.L.3    Engelhard, V.H.4
  • 12
    • 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 microscopy studies of Th-B antigen-presenting cell interactions
    • Kupfer H, Monks C, 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 microscopy 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.2    Kupfer, A.3
  • 13
    • 0027457958 scopus 로고
    • Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro
    • Burkhardt JK, McIlvain JM Jr, Sheetz MP, Argon Y. Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro. J Cell Sci 1993;104:151-162.
    • (1993) J Cell Sci , vol.104 , pp. 151-162
    • Burkhardt, J.K.1    McIlvain J.M., Jr.2    Sheetz, M.P.3    Argon, Y.4
  • 14
    • 0034046180 scopus 로고    scopus 로고
    • T cell activation and the cytoskeleton
    • Acuto O, Cantrell D. T cell activation and the cytoskeleton. Annu Rev Immunol 2000;18:165-184.
    • (2000) Annu Rev Immunol , vol.18 , pp. 165-184
    • Acuto, O.1    Cantrell, D.2
  • 15
    • 0025541125 scopus 로고
    • The PMA-induced specific association of LFA-1 and talin in intact cloned T helper cells
    • Kupfer A, Burn P, Singer SJ. The PMA-induced specific association of LFA-1 and talin in intact cloned T helper cells. J Mol Cell Immunol 1990;4:317-325.
    • (1990) J Mol Cell Immunol , vol.4 , pp. 317-325
    • Kupfer, A.1    Burn, P.2    Singer, S.J.3
  • 16
    • 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
  • 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;39S:82-86.
    • (1998) Nature , vol.39 S , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 18
    • 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
  • 19
    • 0032559586 scopus 로고    scopus 로고
    • Cytoskeletal polarization of T cells is regulated by an immunoreceptor tyrosine-based activation motif-dependent mechanism
    • Lowin-Kropf B, Shapiro VS, Weiss A. Cytoskeletal polarization of T cells is regulated by an immunoreceptor tyrosine-based activation motif-dependent mechanism. J Cell Biol 1998;140:861-871.
    • (1998) J Cell Biol , vol.140 , pp. 861-871
    • Lowin-Kropf, B.1    Shapiro, V.S.2    Weiss, A.3
  • 20
    • 0033083257 scopus 로고    scopus 로고
    • TCR LFA-1, and CD28 play unique and complementary roles in signaling T cell cytoskeletal reorganization
    • Sedwick CE, Morgan MM, Jusino L, Cannon JL, Miller J, Burkhardt JK. TCR, LFA-1, and CD28 play unique and complementary roles in signaling T cell cytoskeletal reorganization. J Immunol 1999;162:1367-1375.
    • (1999) J Immunol , vol.162 , pp. 1367-1375
    • Sedwick, C.E.1    Morgan, M.M.2    Jusino, L.3    Cannon, J.L.4    Miller, J.5    Burkhardt, J.K.6
  • 21
    • 0034877142 scopus 로고    scopus 로고
    • Wasp recruitment to the T cell. APC contact site occurs independendy of cdc42 activation
    • Cannon JL, et al. Wasp recruitment to the T cell. APC contact site occurs independendy of cdc42 activation. Immunity 2001;15:249-259.
    • (2001) Immunity , vol.15 , pp. 249-259
    • Cannon, J.L.1
  • 22
    • 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
  • 23
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • Liu S, Calderwood DA, Ginsberg MH. Integrin cytoplasmic domain-binding proteins. J Cell Sci 2000;113:3563-3571.
    • (2000) J Cell Sci , vol.113 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 24
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • van Kooyk Y, Figdor CG. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr Opin Cell Biol 2000;12:542-547.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 542-547
    • Van Kooyk, Y.1    Figdor, C.G.2
  • 25
    • 0031018338 scopus 로고    scopus 로고
    • Dual role of the actin cytoskeleton in regulating cell adhesion mediated by the integrin lymphocyte function-associated molecule-1
    • Lub M, van Kooyk Y, van Vliet SJ, Figdor CG. Dual role of the actin cytoskeleton in regulating cell adhesion mediated by the integrin lymphocyte function-associated molecule-1. Mol Biol Cell 1997;8:341-351.
    • (1997) Mol Biol Cell , vol.8 , pp. 341-351
    • Lub, M.1    Van Kooyk, Y.2    Van Vliet, S.J.3    Figdor, C.G.4
  • 27
    • 0035652354 scopus 로고    scopus 로고
    • Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin
    • Delon J, Kaibuchi K, Germain RN. Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin. Immunity 2001;15:691-701.
    • (2001) Immunity , vol.15 , pp. 691-701
    • Delon, J.1    Kaibuchi, K.2    Germain, R.N.3
  • 28
    • 0033666324 scopus 로고    scopus 로고
    • Antigen presentation in extracellular matrix. Interactions of T cells with dendritic cells are dynamic, short lived, and sequential
    • Gunzer M, et al. Antigen presentation in extracellular matrix. Interactions of T cells with dendritic cells are dynamic, short lived, and sequential. Immunity 2000;13:323-332.
    • (2000) Immunity , vol.13 , pp. 323-332
    • Gunzer, M.1
  • 29
    • 0035059418 scopus 로고    scopus 로고
    • The immunological synapse
    • Bromley SK, et al. The immunological synapse. Annu Rev Immunol 2001;19:375-396.
    • (2001) Annu Rev Immunol , vol.19 , pp. 375-396
    • Bromley, S.K.1
  • 30
    • 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
  • 31
    • 0035889958 scopus 로고    scopus 로고
    • Superantigen-induced T cell: B cell conjugation is mediated by LFA-1 and requires signaling through Lck, but not ZAP-70
    • Morgan MM, Labno CM, Van Seventer GA, Denny MF, Straus DB, Burkhardt JK. Superantigen-induced T cell: B cell conjugation is mediated by LFA-1 and requires signaling through Lck, but not ZAP-70. J Immunol 2001;167:5708-5718.
    • (2001) J Immunol , vol.167 , pp. 5708-5718
    • Morgan, M.M.1    Labno, C.M.2    Van Seventer, G.A.3    Denny, M.F.4    Straus, D.B.5    Burkhardt, J.K.6
  • 32
    • 0033582440 scopus 로고    scopus 로고
    • The lck SH3 domain is required for activation of the mitogen-activated protein kinase pathway but not the initiation of T-cell antigen receptor signaling
    • Denny MF, Kaufman HC, Chan AC, Straus DB. The lck SH3 domain is required for activation of the mitogen-activated protein kinase pathway but not the initiation of T-cell antigen receptor signaling. J Biol Chem 1999;274:5146-5152.
    • (1999) J Biol Chem , vol.274 , pp. 5146-5152
    • Denny, M.F.1    Kaufman, H.C.2    Chan, A.C.3    Straus, D.B.4
  • 33
    • 0033756553 scopus 로고    scopus 로고
    • CD28 and the tyrosine kinase lck stimulate mitogen-activated protein kinase activity in T cells via inhibition of the small G protein rap1
    • Carey KD, et al. CD28 and the tyrosine kinase lck stimulate mitogen-activated protein kinase activity in T cells via inhibition of the small G protein rap1. Mol Cell Biol 2000;20:8409-8419.
    • (2000) Mol Cell Biol , vol.20 , pp. 8409-8419
    • Carey, K.D.1
  • 34
    • 0034004457 scopus 로고    scopus 로고
    • Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase
    • Katagiri K, Hattori M, Minato N, Irie S, Takatsu K, Kinashi T. Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase. Mol Cell Biol 2000;20:1956-1969.
    • (2000) Mol Cell Biol , vol.20 , pp. 1956-1969
    • Katagiri, K.1    Hattori, M.2    Minato, N.3    Irie, S.4    Takatsu, K.5    Kinashi, T.6
  • 35
    • 0035863801 scopus 로고    scopus 로고
    • A molecular framework for two-step T cell signaling: Lck Src homology 3 mutations discriminate distinctly regulated lipid raft reorganization events
    • Patel VP, Moran M, Low TA, Miceli MC. A molecular framework for two-step T cell signaling: Lck Src homology 3 mutations discriminate distinctly regulated lipid raft reorganization events. J Immunol 2001;166:754-764.
    • (2001) J Immunol , vol.166 , pp. 754-764
    • Patel, V.P.1    Moran, M.2    Low, T.A.3    Miceli, M.C.4
  • 36
    • 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
  • 37
    • 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
  • 38
    • 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
  • 39
    • 0032926260 scopus 로고    scopus 로고
    • Separation of integrin-dependent adhesion from morphological changes based on differential PLC specificities
    • Wooten DK, Teague TK, McIntyre BW. Separation of integrin-dependent adhesion from morphological changes based on differential PLC specificities. J Leukoc Biol 1999;65:127-136.
    • (1999) J Leukoc Biol , vol.65 , pp. 127-136
    • Wooten, D.K.1    Teague, T.K.2    McIntyre, B.W.3
  • 40
    • 0034288906 scopus 로고    scopus 로고
    • A novel functional interaction between Vav and PKCtheta is required for TCR-induced T cell activation
    • Villalba M, Coudronniere N, Deckert M, Teixeiro E, Mas P, Altman A. A novel functional interaction between Vav and PKCtheta is required for TCR-induced T cell activation. Immunity 2000;12:151-160.
    • (2000) Immunity , vol.12 , pp. 151-160
    • Villalba, M.1    Coudronniere, N.2    Deckert, M.3    Teixeiro, E.4    Mas, P.5    Altman, A.6
  • 41
    • 18844473151 scopus 로고    scopus 로고
    • PKC-theta is required for TCR-induced NF-kappaB activation in mature but not immature T lymphocytes
    • Sun Z, et al. PKC-theta is required for TCR-induced NF-kappaB activation in mature but not immature T lymphocytes. Nature 2000;404:402-407.
    • (2000) Nature , vol.404 , pp. 402-407
    • Sun, Z.1
  • 42
    • 0032813846 scopus 로고    scopus 로고
    • Small GTPases in lymphocyte biology: Rho proteins take center stage
    • Henning S, Cleverley S. Small GTPases in lymphocyte biology: Rho proteins take center stage. Immunol Res 1999;20:29-42.
    • (1999) Immunol Res , vol.20 , pp. 29-42
    • Henning, S.1    Cleverley, S.2
  • 43
    • 0033007293 scopus 로고    scopus 로고
    • Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity
    • Johnson DI. Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity. Microbiol Mol Biol Rev 1999;63:54-105.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 54-105
    • Johnson, D.I.1
  • 44
    • 0028871169 scopus 로고
    • Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast
    • Li R, Zheng Y, Drubin DG. Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast. J Cell Biol 1995;128:599-615.
    • (1995) J Cell Biol , vol.128 , pp. 599-615
    • Li, R.1    Zheng, Y.2    Drubin, D.G.3
  • 45
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes CD, Hall A. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J Cell Biol 1999;144:1235-1244.
    • (1999) J Cell Biol , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 47
    • 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
  • 48
    • 0028925711 scopus 로고
    • Rho-related proteins: Actin cytoskeleton and cell cycle
    • Ridley AJ. Rho-related proteins: actin cytoskeleton and cell cycle. Curr Opin Genet Dev 1995;5:24-30.
    • (1995) Curr Opin Genet Dev , vol.5 , pp. 24-30
    • Ridley, A.J.1
  • 49
    • 0027937223 scopus 로고
    • Isolation of a novel gene mutated in Wiscott-Aldrich Syndrome
    • Derry J, Ochs H, Francke U. Isolation of a novel gene mutated in Wiscott-Aldrich Syndrome. Cell 1994;78:635-644.
    • (1994) Cell , vol.78 , pp. 635-644
    • Derry, J.1    Ochs, H.2    Francke, U.3
  • 50
    • 0029680639 scopus 로고    scopus 로고
    • Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome
    • Aspenstrom P, Lindberg U, Hall A. Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome. Curr Biol 1996;6:70-75.
    • (1996) Curr Biol , vol.6 , pp. 70-75
    • Aspenstrom, P.1    Lindberg, U.2    Hall, A.3
  • 51
    • 0029078212 scopus 로고
    • Identification of WASP mutations in patients with Wiskott-Aldrich syndrome and isolated thrombocytopenia reveals allelic heterogeneity at the WAS locus
    • Kolluri R, et al. Identification of WASP mutations in patients with Wiskott-Aldrich syndrome and isolated thrombocytopenia reveals allelic heterogeneity at the WAS locus. Hum Mol Genet 1995;4:1119-1126.
    • (1995) Hum Mol Genet , vol.4 , pp. 1119-1126
    • Kolluri, R.1
  • 52
    • 0030006284 scopus 로고    scopus 로고
    • Wiscott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons M, et al. Wiscott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 1996;84:723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1
  • 53
    • 0031755919 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome
    • Ochs HD. The Wiskott-Aldrich syndrome. Semin Hematol 1998;35:332-345.
    • (1998) Semin Hematol , vol.35 , pp. 332-345
    • Ochs, H.D.1
  • 54
    • 0031831252 scopus 로고    scopus 로고
    • Chemotaxis of macrophages is abolished in the Wiskott-Aldrich syndrome
    • Zicha D, et al. Chemotaxis of macrophages is abolished in the Wiskott-Aldrich syndrome. Br J Haematol 1998;101:659-665.
    • (1998) Br J Haematol , vol.101 , pp. 659-665
    • Zicha, D.1
  • 56
    • 0022893107 scopus 로고
    • Morphological abnormalities in the lymphocytes of patients with the Wiscott-Aldrich syndrome
    • Kenney D, Cairns L, Remold-O'Donnell E, Peterson J, Rosen F, Parkman R. Morphological abnormalities in the lymphocytes of patients with the Wiscott-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.5    Parkman, R.6
  • 57
    • 0026731846 scopus 로고
    • T cell lines characterize events in the pathogenesis of the Wiscott-Aldrich syndrome
    • Molina I, Kenney D, Rosen F, Remold-O'Donnell E. T cell lines characterize events in the pathogenesis of the Wiscott-Aldrich syndrome. J Exp Med 1992;176:867-874.
    • (1992) J Exp Med , vol.176 , pp. 867-874
    • Molina, I.1    Kenney, D.2    Rosen, F.3    Remold-O'Donnell, E.4
  • 58
    • 0030816363 scopus 로고    scopus 로고
    • Defective actin reorganization and polymerization of Wiskott-Aldrich T cells in response to CD3-mediated stimulation
    • Gallego MD, Santamaria M, Pena J, Molina IJ. Defective actin reorganization and polymerization of Wiskott-Aldrich T cells in response to CD3-mediated stimulation. Blood 1997;90:3089-3097.
    • (1997) Blood , vol.90 , pp. 3089-3097
    • Gallego, M.D.1    Santamaria, M.2    Pena, J.3    Molina, I.J.4
  • 59
    • 0031802501 scopus 로고    scopus 로고
    • Defective actin polymerization in EBV-transformed B-cell lines from patients with the Wiskott-Aldrich syndrome
    • Facchetti F, et al. Defective actin polymerization in EBV-transformed B-cell lines from patients with the Wiskott-Aldrich syndrome. J Pathol 1998;185:99-107.
    • (1998) J Pathol , vol.185 , pp. 99-107
    • Facchetti, F.1
  • 60
    • 0032118427 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein-deficient mice reveal a role for WASP in T but not B cell activation
    • Snapper SB, et al. Wiskott-Aldrich syndrome protein-deficient mice reveal a role for WASP in T but not B cell activation. Immunity 1998;9:81-91.
    • (1998) Immunity , vol.9 , pp. 81-91
    • Snapper, S.B.1
  • 61
    • 0033230229 scopus 로고    scopus 로고
    • Antigen receptor-induced activation and cytoskeletal rearrangement are impaired in Wiskott-Aldrich syndrome protein-deficient lymphocytes
    • Zhang J, et al. Antigen receptor-induced activation and cytoskeletal rearrangement are impaired in Wiskott-Aldrich syndrome protein-deficient lymphocytes. J Exp Med 1999;190:1329-1342.
    • (1999) J Exp Med , vol.190 , pp. 1329-1342
    • Zhang, J.1
  • 62
    • 0033609388 scopus 로고    scopus 로고
    • Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein
    • Abdul-Manan N, et al. Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein. Nature 1999;399:379-383.
    • (1999) Nature , vol.399 , pp. 379-383
    • Abdul-Manan, N.1
  • 63
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Atp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R, et al. The interaction between N-WASP and the Atp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 1999;97:221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1
  • 64
    • 0033616763 scopus 로고    scopus 로고
    • Scar, a WASp-related protein, activates nucleation of actin filaments by the Atp2/3 complex
    • Machesky LM, et al. Scar, a WASp-related protein, activates nucleation of actin filaments by the Atp2/3 complex. Proc Natl Acad Sci USA 1999;96:3739-3744.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3739-3744
    • Machesky, L.M.1
  • 65
    • 0033594548 scopus 로고    scopus 로고
    • Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts
    • Mullins RD, Pollard TD. Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts. Curr Biol 1999;9:405-415.
    • (1999) Curr Biol , vol.9 , pp. 405-415
    • Mullins, R.D.1    Pollard, T.D.2
  • 66
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
    • Blanchoin L, Amann KJ, Higgs HN, Marchand JB, Kaiser DA, Pollard TD. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 2000;404:1007-1011.
    • (2000) Nature , vol.404 , pp. 1007-1011
    • Blanchoin, L.1    Amann, K.J.2    Higgs, H.N.3    Marchand, J.B.4    Kaiser, D.A.5    Pollard, T.D.6
  • 67
    • 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
  • 68
    • 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
  • 69
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda KE, Scott JA, Dyche Mullins R, Lim WA. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 2000;290:801-806.
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Dyche Mullins, R.3    Lim, W.A.4
  • 70
    • 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
  • 71
    • 0031446340 scopus 로고    scopus 로고
    • WIP a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells
    • Ramesh N, Anton IM, Hartwig JH, Geha RS. WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells. Proc Natl Acad Sci USA 1997;94:14671-14676.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14671-14676
    • Ramesh, N.1    Anton, I.M.2    Hartwig, J.H.3    Geha, R.S.4
  • 72
    • 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
  • 73
    • 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
  • 74
    • 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
  • 76
    • 0033780474 scopus 로고    scopus 로고
    • A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization
    • Moreau V, et al. A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization. Nat Cell Biol 2000;2:441-448.
    • (2000) Nat Cell Biol , vol.2 , pp. 441-448
    • Moreau, V.1
  • 77
    • 0033680925 scopus 로고    scopus 로고
    • Cbl-b is a negative regulator of receptor clustering and raft aggregation in T cells
    • Krawczyk C, et al. Cbl-b is a negative regulator of receptor clustering and raft aggregation in T cells. Immunity 2000;13:463-473.
    • (2000) Immunity , vol.13 , pp. 463-473
    • Krawczyk, C.1
  • 78
    • 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
  • 79
    • 0035182168 scopus 로고    scopus 로고
    • Surfing pathogens and the lessons learned for actin polymerization
    • Frischknecht F, Way M. Surfing pathogens and the lessons learned for actin polymerization. Trends Cell Biol 2001;11:30-38.
    • (2001) Trends Cell Biol , vol.11 , pp. 30-38
    • Frischknecht, F.1    Way, M.2
  • 80
    • 0035463288 scopus 로고    scopus 로고
    • Plagiarism and pathogenesis: Common themes in actin remodeling
    • May RC, Machesky LM. Plagiarism and pathogenesis: common themes in actin remodeling. Dev Cell 2001;1:317-318.
    • (2001) Dev Cell , vol.1 , pp. 317-318
    • May, R.C.1    Machesky, L.M.2
  • 81
    • 0036199184 scopus 로고    scopus 로고
    • Vav1 controls integrin clustering and MHC/peptide-specific cell adhesion to antigen-presenting cells
    • Krawczyk C, et al. Vav1 controls integrin clustering and MHC/peptide-specific cell adhesion to antigen-presenting cells. Immunity 2002;16:331-343.
    • (2002) Immunity , vol.16 , pp. 331-343
    • Krawczyk, C.1
  • 82
    • 0032211713 scopus 로고    scopus 로고
    • Regulation of PAK activation and the T cell cytoskeleton by the linker protein SLP-76
    • Bubeck-Wardenburg J, et al. Regulation of PAK activation and the T cell cytoskeleton by the linker protein SLP-76. Immunity 1998;9:607-616.
    • (1998) Immunity , vol.9 , pp. 607-616
    • Bubeck-Wardenburg, J.1
  • 83
    • 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
  • 84
    • 0034795423 scopus 로고    scopus 로고
    • N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility
    • Snapper SB, et al. N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility. Nat Cell Biol 2001;3:897-904.
    • (2001) Nat Cell Biol , vol.3 , pp. 897-904
    • Snapper, S.B.1
  • 85
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.