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Volumn 60, Issue 1, 2014, Pages 72-79

The adapter proteins ADAP and Nck cooperate in T cell adhesion

Author keywords

ADAP; Adhesion; ICAM 1; LFA 1; Nck; T cells

Indexed keywords

ADAPTOR PROTEIN; ADHESION AND DEGRANULATION PROMOTING ADAPTER PROTEIN; CALCIUM PHOSPHATE; CD18 ANTIGEN; CD3 ANTIGEN; INTERCELLULAR ADHESION MOLECULE 1; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; NCK PROTEIN; NCK1 PROTEIN; NCK2 PROTEIN; OKT 3; PERVANADATE; PHENYLALANINE; PHYTOHEMAGGLUTININ; PHYTOHEMAGGLUTININ A; PROTEIN SH2; SMALL INTERFERING RNA; T LYMPHOCYTE RECEPTOR; TYROSINE; UNCLASSIFIED DRUG;

EID: 84899156568     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2014.03.017     Document Type: Article
Times cited : (10)

References (42)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 3
    • 52949130240 scopus 로고    scopus 로고
    • SKAP-55, SKAP-55-related and ADAP adaptors modulate integrin-mediated immune-cell adhesion
    • Wang H., Rudd C.E. SKAP-55, SKAP-55-related and ADAP adaptors modulate integrin-mediated immune-cell adhesion. Trends Cell Biol. 2008, 18:486-493.
    • (2008) Trends Cell Biol. , vol.18 , pp. 486-493
    • Wang, H.1    Rudd, C.E.2
  • 4
    • 0033485407 scopus 로고    scopus 로고
    • Cutting edge: SLP-76 cooperativity with FYB/FYN-T in the up-regulation of TCR-driven IL-2 transcription requires SLP-76 binding to FYB at Tyr595 and Tyr651
    • Geng L., Raab M., Rudd C.E. Cutting edge: SLP-76 cooperativity with FYB/FYN-T in the up-regulation of TCR-driven IL-2 transcription requires SLP-76 binding to FYB at Tyr595 and Tyr651. J. Immunol. 1999, 163:5753-5757.
    • (1999) J. Immunol. , vol.163 , pp. 5753-5757
    • Geng, L.1    Raab, M.2    Rudd, C.E.3
  • 5
    • 0033213937 scopus 로고    scopus 로고
    • Novel isoform of lymphoid adaptor FYN-T-binding protein (FYB-130) interacts with SLP-76 and up-regulates interleukin 2 production
    • Veale M., Raab M., Li Z., da Silva A.J., Kraeft S.K., Weremowicz S., Morton C.C., Rudd C.E. Novel isoform of lymphoid adaptor FYN-T-binding protein (FYB-130) interacts with SLP-76 and up-regulates interleukin 2 production. J. Biol. Chem. 1999, 274:28427-28435.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28427-28435
    • Veale, M.1    Raab, M.2    Li, Z.3    da Silva, A.J.4    Kraeft, S.K.5    Weremowicz, S.6    Morton, C.C.7    Rudd, C.E.8
  • 6
    • 0033597929 scopus 로고    scopus 로고
    • FYN-T-FYB-SLP-76 interactions define a T-cell receptor zeta/CD3-mediated tyrosine phosphorylation pathway that up-regulates interleukin 2 transcription in T-cells
    • Raab M., Kang H., da Silva A., Zhu X., Rudd C.E. FYN-T-FYB-SLP-76 interactions define a T-cell receptor zeta/CD3-mediated tyrosine phosphorylation pathway that up-regulates interleukin 2 transcription in T-cells. J. Biol. Chem. 1999, 274:21170-21179.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21170-21179
    • Raab, M.1    Kang, H.2    da Silva, A.3    Zhu, X.4    Rudd, C.E.5
  • 7
    • 0034681449 scopus 로고    scopus 로고
    • Functional association between SLAP-130 and SLP-76 in Jurkat T cells
    • Boerth N.J., Judd B.A., Koretzky G.A. Functional association between SLAP-130 and SLP-76 in Jurkat T cells. J. Biol. Chem. 2000, 275:5143-5152.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5143-5152
    • Boerth, N.J.1    Judd, B.A.2    Koretzky, G.A.3
  • 8
    • 0031092695 scopus 로고    scopus 로고
    • Biochemical analysis of p120/130: a protein-tyrosine kinase substrate restricted to T and myeloid cells
    • da Silva A.J., Rosenfield J.M., Mueller I., Bouton A., Hirai H., Rudd C.E. Biochemical analysis of p120/130: a protein-tyrosine kinase substrate restricted to T and myeloid cells. J. Immunol. 1997, 158:2007-2016.
    • (1997) J. Immunol. , vol.158 , pp. 2007-2016
    • da Silva, A.J.1    Rosenfield, J.M.2    Mueller, I.3    Bouton, A.4    Hirai, H.5    Rudd, C.E.6
  • 9
    • 0032475935 scopus 로고    scopus 로고
    • Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130
    • Marie-Cardine A., Hendricks-Taylor L.R., Boerth N.J., Zhao H., Schraven B., Koretzky G.A. Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130. J. Biol. Chem. 1998, 273:25789-25795.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25789-25795
    • Marie-Cardine, A.1    Hendricks-Taylor, L.R.2    Boerth, N.J.3    Zhao, H.4    Schraven, B.5    Koretzky, G.A.6
  • 11
    • 17444416707 scopus 로고    scopus 로고
    • The helically extended SH3 domain of the T cell adaptor protein ADAP is a novel lipid interaction domain
    • Heuer K., Arbuzova A., Strauss H., Kofler M., Freund C. The helically extended SH3 domain of the T cell adaptor protein ADAP is a novel lipid interaction domain. J. Mol. Biol. 2005, 348:1025-1035.
    • (2005) J. Mol. Biol. , vol.348 , pp. 1025-1035
    • Heuer, K.1    Arbuzova, A.2    Strauss, H.3    Kofler, M.4    Freund, C.5
  • 12
    • 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 M.G., Krause M., Hagendorff P., Monner D.A., Trimble W., Grinstein S., Wehland J., Sechi A.S. 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    Krause, M.2    Hagendorff, P.3    Monner, D.A.4    Trimble, W.5    Grinstein, S.6    Wehland, J.7    Sechi, A.S.8
  • 13
    • 0034599541 scopus 로고    scopus 로고
    • Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton
    • Krause M., Sechi A.S., Konradt M., Monner D., Gertler F.B., 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
  • 16
    • 0038383014 scopus 로고    scopus 로고
    • The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network
    • Bladt F., Aippersbach E., Gelkop S., Strasser G.A., Nash P., Tafuri A., Gertler F.B., Pawson T. The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network. Mol. Cell Biol. 2003, 23:4586-4597.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 4586-4597
    • Bladt, F.1    Aippersbach, E.2    Gelkop, S.3    Strasser, G.A.4    Nash, P.5    Tafuri, A.6    Gertler, F.B.7    Pawson, T.8
  • 17
    • 84877990371 scopus 로고    scopus 로고
    • Nck adapter proteins: functional versatility in T cells
    • Lettau M., Pieper J., Janssen O. Nck adapter proteins: functional versatility in T cells. Cell Commun. Signaling 2009, 7:1.
    • (2009) Cell Commun. Signaling , vol.7 , pp. 1
    • Lettau, M.1    Pieper, J.2    Janssen, O.3
  • 18
    • 0036015163 scopus 로고    scopus 로고
    • The Nck family of adapter proteins: regulators of actin cytoskeleton
    • Buday L., Wunderlich L., Tamas P. The Nck family of adapter proteins: regulators of actin cytoskeleton. Cell. Signalling 2002, 14:723-731.
    • (2002) Cell. Signalling , vol.14 , pp. 723-731
    • Buday, L.1    Wunderlich, L.2    Tamas, P.3
  • 19
    • 8444246689 scopus 로고    scopus 로고
    • Involvement of the Wiskott-Aldrich syndrome protein and other actin regulatory adaptors in T cell activation
    • Badour K., Zhang J., Siminovitch K.A. Involvement of the Wiskott-Aldrich syndrome protein and other actin regulatory adaptors in T cell activation. Semin. Immunol. 2004, 16:395-407.
    • (2004) Semin. Immunol. , vol.16 , pp. 395-407
    • Badour, K.1    Zhang, J.2    Siminovitch, K.A.3
  • 20
    • 0037304542 scopus 로고    scopus 로고
    • All roads lead to actin: the intimate relationship between TCR signaling and the cytoskeleton
    • Fuller C.L., Braciale V.L., Samelson L.E. All roads lead to actin: the intimate relationship between TCR signaling and the cytoskeleton. Immunol. Rev. 2003, 191:220-236.
    • (2003) Immunol. Rev. , vol.191 , pp. 220-236
    • Fuller, C.L.1    Braciale, V.L.2    Samelson, L.E.3
  • 22
    • 0032910208 scopus 로고    scopus 로고
    • Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes
    • Wunderlich L., Farago A., Downward J., Buday L. Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes. Eur. J. Immunol. 1999, 29:1068-1075.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 1068-1075
    • Wunderlich, L.1    Farago, A.2    Downward, J.3    Buday, L.4
  • 26
    • 0031017477 scopus 로고    scopus 로고
    • A casein kinase I activity is constitutively associated with Nck
    • Lussier G., Larose L. A casein kinase I activity is constitutively associated with Nck. J. Biol. Chem. 1997, 272:2688-2694.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2688-2694
    • Lussier, G.1    Larose, L.2
  • 28
    • 33746289906 scopus 로고    scopus 로고
    • Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL
    • Qian J., Chen W., Lettau M., Podda G., Zörnig M., Kabelitz D., Janssen O. Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL. Cell Signalling 2006, 18:1327-1337.
    • (2006) Cell Signalling , vol.18 , pp. 1327-1337
    • Qian, J.1    Chen, W.2    Lettau, M.3    Podda, G.4    Zörnig, M.5    Kabelitz, D.6    Janssen, O.7
  • 29
    • 0028789982 scopus 로고
    • Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins
    • Tanaka M., Gupta R., Mayer B.J. Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins. Mol. Cell Biol. 1995, 15:6829-6837.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 6829-6837
    • Tanaka, M.1    Gupta, R.2    Mayer, B.J.3
  • 31
    • 0027490809 scopus 로고
    • T cell receptor zeta/CD3-p59fyn(T)-associated p120/130 binds to the SH2 domain of p59fyn(T)
    • da Silva A.J., Janssen O., Rudd C.E. T cell receptor zeta/CD3-p59fyn(T)-associated p120/130 binds to the SH2 domain of p59fyn(T). J. Exp. Med. 1993, 178:2107-2113.
    • (1993) J. Exp. Med. , vol.178 , pp. 2107-2113
    • da Silva, A.J.1    Janssen, O.2    Rudd, C.E.3
  • 34
    • 0029126878 scopus 로고
    • Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains
    • Rivero-Lezcano O.M., Marcilla A., Sameshima J.H., Robbins K.C. 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
  • 35
    • 0037160142 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein
    • Cory G.O., Garg R., Cramer R., Ridley A.J. Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein. J. Biol. Chem. 2002, 277:45115-45121.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45115-45121
    • Cory, G.O.1    Garg, R.2    Cramer, R.3    Ridley, A.J.4
  • 36
    • 0035854732 scopus 로고    scopus 로고
    • Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
    • Rohatgi R., Nollau P., Ho H.Y., Kirschner M.W., Mayer B.J. Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway. J. Biol. Chem. 2001, 276:26448-26452.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26448-26452
    • Rohatgi, R.1    Nollau, P.2    Ho, H.Y.3    Kirschner, M.W.4    Mayer, B.J.5
  • 37
    • 79959396065 scopus 로고    scopus 로고
    • Functional cooperation between the proteins Nck and ADAP is fundamental for actin reorganization
    • Pauker M.H., Reicher B., Fried S., Perl O., Barda-Saad M. Functional cooperation between the proteins Nck and ADAP is fundamental for actin reorganization. Mol. Cell Biol. 2011, 31:2653-2666.
    • (2011) Mol. Cell Biol. , vol.31 , pp. 2653-2666
    • Pauker, M.H.1    Reicher, B.2    Fried, S.3    Perl, O.4    Barda-Saad, M.5
  • 38
    • 77951020111 scopus 로고    scopus 로고
    • Impaired NK-cell migration in WAS/XLT patients: role of Cdc42/WASp pathway in the control of chemokine-induced beta2 integrin high-affinity state
    • Stabile H., Carlino C., Mazza C., Giliani S., Morrone S., Notarangelo L.D., Notarangelo L.D., Santoni A., Gismondi A. Impaired NK-cell migration in WAS/XLT patients: role of Cdc42/WASp pathway in the control of chemokine-induced beta2 integrin high-affinity state. Blood 2010, 115:2818-2826.
    • (2010) Blood , vol.115 , pp. 2818-2826
    • Stabile, H.1    Carlino, C.2    Mazza, C.3    Giliani, S.4    Morrone, S.5    Notarangelo, L.D.6    Notarangelo, L.D.7    Santoni, A.8    Gismondi, A.9
  • 39
    • 34347337643 scopus 로고    scopus 로고
    • RIAM links the ADAP/SKAP-55 signaling module to Rap1, facilitating T-cell-receptor-mediated integrin activation
    • Menasche G., Kliche S., Chen E.J., Stradal T.E., Schraven B., Koretzky G. RIAM links the ADAP/SKAP-55 signaling module to Rap1, facilitating T-cell-receptor-mediated integrin activation. Mol. Cell Biol. 2007, 27:4070-4081.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 4070-4081
    • Menasche, G.1    Kliche, S.2    Chen, E.J.3    Stradal, T.E.4    Schraven, B.5    Koretzky, G.6
  • 41
    • 77954162555 scopus 로고    scopus 로고
    • Src homology 2-domain containing leukocyte-specific phosphoprotein of 76kDa is mandatory for TCR-mediated inside-out signaling, but dispensable for CXCR4-mediated LFA-1 activation, adhesion, and migration of T cells
    • Horn J., Wang X., Reichardt P., Stradal T.E., Warnecke N., Simeoni L., Gunzer M., Yablonski D., Schraven B., Kliche S. Src homology 2-domain containing leukocyte-specific phosphoprotein of 76kDa is mandatory for TCR-mediated inside-out signaling, but dispensable for CXCR4-mediated LFA-1 activation, adhesion, and migration of T cells. J. Immunol. 2009, 183:5756-5767.
    • (2009) J. Immunol. , vol.183 , pp. 5756-5767
    • Horn, J.1    Wang, X.2    Reichardt, P.3    Stradal, T.E.4    Warnecke, N.5    Simeoni, L.6    Gunzer, M.7    Yablonski, D.8    Schraven, B.9    Kliche, S.10


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