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Volumn 40, Issue 9, 2010, Pages 2437-2449

Sustained LFA-1 cluster formation in the immune synapse requires the combined activities of L-plastin and calmodulin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; CALMODULIN; ENTEROTOXIN; ENTEROTOXIN B, STAPHYLOCOCCAL; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; MEMBRANE PROTEIN; N (6 AMINOHEXYL) 5 CHLORO 1 NAPHTHALENESULFONAMIDE; PLASTIN; PROTEIN BINDING; SMALL INTERFERING RNA; SULFONAMIDE;

EID: 77956486432     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201040345     Document Type: Article
Times cited : (62)

References (38)
  • 1
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • DOI 10.1038/25764
    • Monks, C. R., Freiberg, B. A., Kupfer, H., Sciaky, N. and Kupfer, A., Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 1998. 395: 82-86. (Pubitemid 28420234)
    • (1998) Nature , vol.395 , Issue.6697 , pp. 82-86
    • Monks, C.R.F.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 2
    • 0034232037 scopus 로고    scopus 로고
    • The immunological synapse and the actin cytoskeleton: Molecular hardware for T cell signaling
    • Dustin, M. L. and Cooper, J. A., 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
  • 3
    • 2342566929 scopus 로고    scopus 로고
    • What is the importance of the immunological synapse?
    • Davis, D. M. and Dustin, M. L., What is the importance of the immunological synapse? Trends Immunol. 2004. 25: 323-327.
    • (2004) Trends Immunol. , vol.25 , pp. 323-327
    • Davis, D.M.1    Dustin, M.L.2
  • 4
    • 34447331260 scopus 로고    scopus 로고
    • The molecular makeup and function of regulatory and effector synapses
    • Reichardt, P., Dornbach, B. and Gunzer, M., The molecular makeup and function of regulatory and effector synapses. Immunol. Rev. 2007. 218: 165-177.
    • (2007) Immunol. Rev. , vol.218 , pp. 165-177
    • Reichardt, P.1    Dornbach, B.2    Gunzer, M.3
  • 5
    • 2342500829 scopus 로고    scopus 로고
    • New views of the immunological synapse: Variations in assembly and function
    • Jacobelli, J., Andres, P. G., Boisvert, J. and Krummel, M. F., New views of the immunological synapse: variations in assembly and function. Curr. Opin. Immunol. 2004. 16: 345-352.
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 345-352
    • Jacobelli, J.1    Andres, P.G.2    Boisvert, J.3    Krummel, M.F.4
  • 6
    • 51349131307 scopus 로고    scopus 로고
    • The balance between T cell receptor signaling and degradation at the center of the immunological synapse is determined by antigen quality
    • Cemerski, S., Das, J., Giurisato, E., Markiewicz, M. A., Allen, P. M., Chakraborty, A. K. and Shaw, A. S., The balance between T cell receptor signaling and degradation at the center of the immunological synapse is determined by antigen quality. Immunity 2008. 29: 414-422.
    • (2008) Immunity , vol.29 , pp. 414-422
    • Cemerski, S.1    Das, J.2    Giurisato, E.3    Markiewicz, M.A.4    Allen, P.M.5    Chakraborty, A.K.6    Shaw, A.S.7
  • 7
    • 34249029253 scopus 로고    scopus 로고
    • Immunological synapses: Breaking up may be good to do
    • Krummel, M. F., Immunological synapses: breaking up may be good to do. Cell 2007. 129: 653-655.
    • (2007) Cell , vol.129 , pp. 653-655
    • Krummel, M.F.1
  • 9
    • 0037244777 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in T lymphocyte activation and migration
    • Samstag, Y., Eibert, S. M., Klemke, M. and Wabnitz, G. H., Actin cytoskeletal dynamics in T lymphocyte activation and migration. J. Leukoc. Biol. 2003. 73: 30-48.
    • (2003) J. Leukoc. Biol. , vol.73 , pp. 30-48
    • Samstag, Y.1    Eibert, S.M.2    Klemke, M.3    Wabnitz, G.H.4
  • 10
    • 0036696565 scopus 로고    scopus 로고
    • The regulation of actin remodeling during T-cell-APC conjugate formation
    • Cannon, J. L. and Burkhardt, J. K., The regulation of actin remodeling during T-cell-APC conjugate formation. Immunol. Rev. 2002. 186: 90-99.
    • (2002) Immunol. Rev. , vol.186 , pp. 90-99
    • Cannon, J.L.1    Burkhardt, J.K.2
  • 12
    • 0027511422 scopus 로고
    • Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells
    • Lin, C. S., Park, T., Chen, Z. P. and Leavitt, J., Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells. J. Biol. Chem. 1993. 268: 2781-2792.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2781-2792
    • Lin, C.S.1    Park, T.2    Chen, Z.P.3    Leavitt, J.4
  • 13
    • 0025091625 scopus 로고
    • Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins
    • DOI 10.1083/jcb.111.3.1069
    • de Arruda, M. V., Watson, S., Lin, C. S., Leavitt, J. and Matsudaira, P., Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins. J. Cell Biol. 1990. 111: 1069-1079. (Pubitemid 20263788)
    • (1990) Journal of Cell Biology , vol.111 , Issue.3 , pp. 1069-1079
    • De Arruda, M.V.1    Watson, S.2    Lin, C.-S.3    Leavitt, J.4    Matsudaira, P.5
  • 14
    • 0035947761 scopus 로고    scopus 로고
    • An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function
    • DOI 10.1083/jcb.153.5.947
    • Volkmann, N., DeRosier, D., Matsudaira, P. and Hanein, D., An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function. J. Cell Biol. 2001. 153: 947-956. (Pubitemid 34289235)
    • (2001) Journal of Cell Biology , vol.153 , Issue.5 , pp. 947-956
    • Volkmann, N.1    Derosier, D.2    Matsudaira, P.3    Hanein, D.4
  • 15
    • 0030727339 scopus 로고    scopus 로고
    • Evidence for a conformational change in actin induced by fimbrin (N375) binding
    • Hanein, D., Matsudaira, P. and DeRosier, D. J., Evidence for a conformational change in actin induced by fimbrin (N375) binding. J. Cell Biol. 1997. 139: 387-396.
    • (1997) J. Cell Biol. , vol.139 , pp. 387-396
    • Hanein, D.1    Matsudaira, P.2    DeRosier, D.J.3
  • 17
    • 34147144013 scopus 로고    scopus 로고
    • Costimulation induced phosphorylation of L-plastin facilitates surface transport of the T cell activation molecules CD69 and CD25
    • Wabnitz, G. H., Kocher, T., Lohneis, P., Stober, C., Konstandin, M. H., Funk, B., Sester, U. et al., Costimulation induced phosphorylation of L-plastin facilitates surface transport of the T cell activation molecules CD69 and CD25. Eur. J. Immunol. 2007. 37: 649-662.
    • (2007) Eur. J. Immunol. , vol.37 , pp. 649-662
    • Wabnitz, G.H.1    Kocher, T.2    Lohneis, P.3    Stober, C.4    Konstandin, M.H.5    Funk, B.6    Sester, U.7
  • 18
    • 0029666259 scopus 로고    scopus 로고
    • FcgammaRII-mediated adhesion and phagocytosis induce L-plastin phosphorylation in human neutrophils
    • Jones, S. L. and Brown, E. J., FcgammaRII-mediated adhesion and phagocytosis induce L-plastin phosphorylation in human neutrophils. J. Biol. Chem. 1996. 271: 14623-14630.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14623-14630
    • Jones, S.L.1    Brown, E.J.2
  • 19
    • 0033588228 scopus 로고    scopus 로고
    • Immune complex-induced integrin activation and L-plastin phosphorylation require protein kinase a
    • Wang, J. and Brown, E. J., Immune complex-induced integrin activation and L-plastin phosphorylation require protein kinase A. J. Biol. Chem. 1999. 274: 24349-24356.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24349-24356
    • Wang, J.1    Brown, E.J.2
  • 20
    • 33744536569 scopus 로고    scopus 로고
    • Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells
    • Janji, B., Giganti, A., De Corte, V., Catillon, M., Bruyneel, E., Lentz, D., Plastino, J. et al., Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells. J. Cell Sci. 2006. 119: 1947-1960.
    • (2006) J. Cell Sci. , vol.119 , pp. 1947-1960
    • Janji, B.1    Giganti, A.2    De Corte, V.3    Catillon, M.4    Bruyneel, E.5    Lentz, D.6    Plastino, J.7
  • 21
    • 0032483008 scopus 로고    scopus 로고
    • A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function
    • Jones, S. L., Wang, J., Turck, C. W. and Brown, E. J., A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function. Proc. Natl. Acad. Sci. USA 1998. 95: 9331-9336.
    • Proc. Natl. Acad. Sci. USA 1998 , vol.95 , pp. 9331-9336
    • Jones, S.L.1    Wang, J.2    Turck, C.W.3    Brown, E.J.4
  • 22
    • 0026468443 scopus 로고
    • Human T cell L-plastin bundles actin filaments in a calcium-dependent manner
    • Namba, Y., Ito, M., Zu, Y., Shigesada, K. and Maruyama, K., Human T cell L-plastin bundles actin filaments in a calcium-dependent manner. J. Biochem. 1992. 112: 503-507.
    • (1992) J. Biochem. , vol.112 , pp. 503-507
    • Namba, Y.1    Ito, M.2    Zu, Y.3    Shigesada, K.4    Maruyama, K.5
  • 23
    • 34447339202 scopus 로고    scopus 로고
    • Naive B cells generate regulatory T cells in the presence of a mature immunologic synapse
    • Reichardt, P., Dornbach, B., Rong, S., Beissert, S., Gueler, F., Loser, K. and Gunzer, M., Naive B cells generate regulatory T cells in the presence of a mature immunologic synapse. Blood 2007. 110: 1519-1529.
    • (2007) Blood , vol.110 , pp. 1519-1529
    • Reichardt, P.1    Dornbach, B.2    Rong, S.3    Beissert, S.4    Gueler, F.5    Loser, K.6    Gunzer, M.7
  • 24
    • 34249013684 scopus 로고    scopus 로고
    • Opposing effects of PKCtheta and WASp on symmetry breaking and relocation of the immunological synapse
    • Sims, T. N., Soos, T. J., Xenias, H. S., Dubin-Thaler, B., Hofman, J. M., Waite, J. C., Cameron, T. O. et al., Opposing effects of PKCtheta and WASp on symmetry breaking and relocation of the immunological synapse. Cell 2007. 129: 773-785.
    • (2007) Cell , vol.129 , pp. 773-785
    • Sims, T.N.1    Soos, T.J.2    Xenias, H.S.3    Dubin-Thaler, B.4    Hofman, J.M.5    Waite, J.C.6    Cameron, T.O.7
  • 26
    • 77951203795 scopus 로고    scopus 로고
    • Quantitative measurement of F-actin accumulation at the NK cell immunological synapse
    • Banerjee, P. P. and Orange, J. S., Quantitative measurement of F-actin accumulation at the NK cell immunological synapse. J. Immunol. Methods 2010. 355: 1-13.
    • (2010) J. Immunol. Methods , vol.355 , pp. 1-13
    • Banerjee, P.P.1    Orange, J.S.2
  • 28
    • 0028331780 scopus 로고    scopus 로고
    • Bromophenacyl bromide binding to the actin-bundling protein l-plastin inhibits inositol trisphosphate-independent increase in Ca2+ in human neutrophils
    • Rosales, C., Jones, S. L., McCourt, D. and Brown, E. J., Bromophenacyl bromide binding to the actin-bundling protein l-plastin inhibits inositol trisphosphate-independent increase in Ca2+ in human neutrophils. Proc. Natl. Acad. Sci. USA 1994. 91: 3534-3538.
    • Proc. Natl. Acad. Sci. USA 1994 , vol.91 , pp. 3534-3538
    • Rosales, C.1    Jones, S.L.2    McCourt, D.3    Brown, E.J.4
  • 29
    • 77951630203 scopus 로고    scopus 로고
    • The actin-bundling protein L-plastin dissociates CCR7 proximal signaling from CCR7-induced motility
    • Morley, S. C., Wang, C., Lo, W. L., Lio, C. W., Zinselmeyer, B. H., Miller, M. J., Brown, E. J. and Allen, P. M., The actin-bundling protein L-plastin dissociates CCR7 proximal signaling from CCR7-induced motility. J. Immunol. 2010. 184: 3628-3638.
    • (2010) J. Immunol. , vol.184 , pp. 3628-3638
    • Morley, S.C.1    Wang, C.2    Lo, W.L.3    Lio, C.W.4    Zinselmeyer, B.H.5    Miller, M.J.6    Brown, E.J.7    Allen, P.M.8
  • 30
    • 33749533257 scopus 로고    scopus 로고
    • Regulation of cytoskeletal dynamics at the immune synapse: New stars join the actin troupe
    • Billadeau, D. D. and Burkhardt, J. K., Regulation of cytoskeletal dynamics at the immune synapse: new stars join the actin troupe. Traffic 2006. 7: 1451-1460.
    • (2006) Traffic , vol.7 , pp. 1451-1460
    • Billadeau, D.D.1    Burkhardt, J.K.2
  • 32
    • 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, S. J. and Figdor, C. G., 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
  • 33
    • 38049136514 scopus 로고    scopus 로고
    • Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells
    • Kaizuka, Y., Douglass, A. D., Varma, R., Dustin, M. L. and Vale, R. D., Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells. Proc. Natl. Acad. Sci. USA 2007. 104: 20296-20301.
    • Proc. Natl. Acad. Sci. USA 2007 , vol.104 , pp. 20296-20301
    • Kaizuka, Y.1    Douglass, A.D.2    Varma, R.3    Dustin, M.L.4    Vale, R.D.5
  • 34
    • 0041384357 scopus 로고    scopus 로고
    • LFA-1-induced T cell migration on ICAM-1 involves regulation of MLCK-mediated attachment and ROCK-dependent detachment
    • Smith, A., Bracke, M., Leitinger, B., Porter, J. C. and Hogg, N., LFA-1-induced T cell migration on ICAM-1 involves regulation of MLCK-mediated attachment and ROCK-dependent detachment. J Cell Sci. 2003. 116: 3123-3133.
    • (2003) J Cell Sci. , vol.116 , pp. 3123-3133
    • Smith, A.1    Bracke, M.2    Leitinger, B.3    Porter, J.C.4    Hogg, N.5
  • 35
    • 0022549779 scopus 로고
    • Calmodulin binding domains: Characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase
    • Lukas, T. J., Burgess, W. H., Prendergast, F. G., Lau, W. and Watterson, D. M., Calmodulin binding domains: characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase. Biochemistry 1986. 25: 1458-1464.
    • (1986) Biochemistry , vol.25 , pp. 1458-1464
    • Lukas, T.J.1    Burgess, W.H.2    Prendergast, F.G.3    Lau, W.4    Watterson, D.M.5
  • 36
    • 0026468443 scopus 로고
    • Human T cell L-plastin bundles actin filaments in a calcium-dependent manner
    • Namba, Y., Ito, M., Zu, Y., Shigesada, K. and Maruyama, K., Human T cell L-plastin bundles actin filaments in a calcium-dependent manner. J. Biochem. 1992. 112: 503-507.
    • (1992) J. Biochem. , vol.112 , pp. 503-507
    • Namba, Y.1    Ito, M.2    Zu, Y.3    Shigesada, K.4    Maruyama, K.5
  • 37
    • 0023689934 scopus 로고
    • Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts
    • Lin, C. S., Aebersold, R. H., Kent, S. B., Varma, M. and Leavitt, J., Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts. Mol. Cell. Biol. 1988. 8: 4659-4668.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4659-4668
    • Lin, C.S.1    Aebersold, R.H.2    Kent, S.B.3    Varma, M.4    Leavitt, J.5
  • 38
    • 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, S. C. and 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


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