메뉴 건너뛰기




Volumn 31, Issue 13, 2011, Pages 2653-2666

Functional cooperation between the proteins Nck and ADAP is fundamental for actin reorganization

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL PROTEIN; CELL PROTEIN ADAP; CELL PROTEIN SLP76; NCK PROTEIN; PROTEIN KINASE ZAP 70; PROTEIN TYROSINE PHOSPHATASE SHP; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 79959396065     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01358-10     Document Type: Article
Times cited : (45)

References (52)
  • 1
    • 0347915637 scopus 로고    scopus 로고
    • Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein (WASp) tyrosine phosphorylation is required for coupling T cell antigen receptor engagement to WASp effector function and T cell activation
    • Badour, K., et al. 2004. Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein (WASp) tyrosine phosphorylation is required for coupling T cell antigen receptor engagement to WASp effector function and T cell activation. J. Exp. Med. 199:99-112.
    • (2004) J. Exp. Med. , vol.199 , pp. 99-112
    • Badour, K.1
  • 2
    • 0037241232 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse
    • Badour, K., et al. 2003. The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse. Immunity 18:141-154.
    • (2003) Immunity , vol.18 , pp. 141-154
    • Badour, K.1
  • 3
    • 8444246689 scopus 로고    scopus 로고
    • Involvement of the Wiskott-Aldrich syndrome protein and other actin regulatory adaptors in T cell activation
    • Badour, K., J. Zhang, and K. A. Siminovitch. 2004. Involvement of the Wiskott-Aldrich syndrome protein and other actin regulatory adaptors in T cell ctivation. Semin. Immunol. 16:395-407.
    • (2004) Semin. Immunol. , vol.16 , pp. 395-407
    • Badour, K.1    Zhang, J.2    Siminovitch, K.A.3
  • 4
    • 12344272845 scopus 로고    scopus 로고
    • Dynamic molecular interactions linking the T cell antigen receptor to the actin cytoskeleton
    • Barda-Saad, M., et al. 2005. Dynamic molecular interactions linking the T cell antigen receptor to the actin cytoskeleton. Nat. Immunol. 6:80-89.
    • (2005) Nat. Immunol. , vol.6 , pp. 80-89
    • Barda-Saad, M.1
  • 5
    • 77954887980 scopus 로고    scopus 로고
    • Cooperative interactions at the SLP-76 complex are critical for actin polymerization
    • Barda-Saad, M., et al. 2010. Cooperative interactions at the SLP-76 complex are critical for actin polymerization. EMBO J. 29:2315-2328.
    • (2010) EMBO J , vol.29 , pp. 2315-2328
    • Barda-Saad, M.1
  • 6
    • 33746962713 scopus 로고    scopus 로고
    • T-cell antigen receptor-induced signaling complexes: internalization via a cholesterol-dependent endocytic pathway
    • Barr, V. A., et al. 2006. T-cell antigen receptor-induced signaling complexes: internalization via a cholesterol-dependent endocytic pathway. Traffic :1143-1162.
    • (2006) Traffic , vol.7 , pp. 1143-1162
    • Barr, V.A.1
  • 7
    • 33644506455 scopus 로고    scopus 로고
    • Recruitment and activation of PLCgamma1 in T cells: a new insight into old domains
    • Braiman, A., M. Barda-Saad, C. L. Sommers, and L. E. Samelson. 2006. Recruitment and activation of PLCgamma1 in T cells: a new insight into old omains. EMBO J. 25:774-784.
    • (2006) EMBO J , vol.25 , pp. 774-784
    • Braiman, A.1    Barda-Saad, M.2    Sommers, C.L.3    Samelson, L.E.4
  • 8
    • 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. 1998. Regulation of PAK activation and the T cell cytoskeleton by the linker protein SLP-76. Immunity 9:607-616.
    • (1998) Immunity , vol.9 , pp. 607-616
    • Bubeck Wardenburg, J.1
  • 9
    • 0037144842 scopus 로고    scopus 로고
    • T cell receptor ligation induces the formation of dynamically regulated signaling assemblies
    • Bunnell, S. C., et al. 2002. T cell receptor ligation induces the formation of dynamically regulated signaling assemblies. J. Cell Biol. 158:1263-1275.
    • (2002) J. Cell Biol. , vol.158 , pp. 1263-1275
    • Bunnell, S.C.1
  • 11
    • 0034877142 scopus 로고    scopus 로고
    • Wasp recruitment to the T cell:APC contact site occurs independently of Cdc42 activation
    • Cannon, J. L., et al. 2001. Wasp recruitment to the T cell:APC contact site occurs independently of Cdc42 activation. Immunity 15:249-259.
    • (2001) Immunity , vol.15 , pp. 249-259
    • Cannon, J.L.1
  • 12
    • 32844474692 scopus 로고    scopus 로고
    • Role of ERM (ezrin-radixin-moesin) proteins in T lymphocyte polarization, immune synapse formation and in T cell receptor-mediated signaling
    • Charrin, S., and A. Alcover. 2006. Role of ERM (ezrin-radixin-moesin) proteins in T lymphocyte polarization, immune synapse formation and in T cell receptor-mediated signaling. Front. Biosci. 11:1987-1997.
    • (2006) Front. Biosci. , vol.11 , pp. 1987-1997
    • Charrin, S.1    Alcover, A.2
  • 13
    • 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., R. Garg, R. Cramer, and A. J. Ridley. 2002. Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich syndrome protein. J. Biol. Chem. 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
  • 14
    • 35548953842 scopus 로고    scopus 로고
    • Splicingand cleavage-independent requirement of RNA polymerase II CTD for mRNA release from the transcription site
    • Custodio, N., M. Vivo, M. Antoniou, and M. Carmo-Fonseca. 2007. Splicingand cleavage-independent requirement of RNA polymerase II CTD for mRNA release from the transcription site. J. Cell Biol. 179:199-207.
    • (2007) J. Cell Biol. , vol.179 , pp. 199-207
    • Custodio, N.1    Vivo, M.2    Antoniou, M.3    Carmo-Fonseca, M.4
  • 15
    • 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, A. J., et al. 1997. 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. U. S. A. 94:7493-7498.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7493-7498
    • da Silva, A.J.1
  • 16
    • 19944431032 scopus 로고    scopus 로고
    • Kinase-independent functions for Itk in TCR-induced regulation of Vav and the actin cytoskeleton
    • Dombroski, D., et al. 2005. Kinase-independent functions for Itk in TCR-induced regulation of Vav and the actin cytoskeleton. J. Immunol. 174:1385-392.
    • (2005) J. Immunol. , vol.174 , pp. 1385-1392
    • Dombroski, D.1
  • 17
    • 0033679212 scopus 로고    scopus 로고
    • A second amplifier function for the allergy-associated Fc(epsilon)RI-beta subunit
    • Donnadieu, E., M. H. Jouvin, and J. P. Kinet. 2000. A second amplifier function for the allergy-associated Fc(epsilon)RI-beta subunit. Immunity 2:515-523.
    • (2000) Immunity , vol.12 , pp. 515-523
    • Donnadieu, E.1    Jouvin, M.H.2    Kinet, J.P.3
  • 18
    • 0035949507 scopus 로고    scopus 로고
    • Adaptor FYB (Fyn-binding protein) regulates integrin-mediated adhesion and mediator release: differential involvement of the FYB SH3 domain
    • Geng, L., S. Pfister, S. K. Kraeft, and C. E. Rudd. 2001. Adaptor FYB (Fyn-binding protein) regulates integrin-mediated adhesion and mediator release: differential involvement of the FYB SH3 domain. Proc. Natl. Acad. Sci. U. S. A. 98:11527-11532.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11527-11532
    • Geng, L.1    Pfister, S.2    Kraeft, S.K.3    Rudd, C.E.4
  • 19
    • 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., M. Raab, and C. E. Rudd. 1999. 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. 163: 5753-5757.
    • (1999) J. Immunol. , vol.163 , pp. 5753-5757
    • Geng, L.1    Raab, M.2    Rudd, C.E.3
  • 20
    • 33847311403 scopus 로고    scopus 로고
    • Formins regulate the actin-related protein 2/3 complex-independent polarization of the centrosome to the immunological synapse
    • Gomez, T. S., et al. 2007. Formins regulate the actin-related protein 2/3 complex-independent polarization of the centrosome to the immunological ynapse. Immunity 26:177-190.
    • (2007) Immunity , vol.26 , pp. 177-190
    • Gomez, T.S.1
  • 21
    • 33744981370 scopus 로고    scopus 로고
    • HS1 functions as an essential actin-regulatory adaptor protein at the immune synapse
    • Gomez, T. S., et al. 2006. HS1 functions as an essential actin-regulatory adaptor protein at the immune synapse. Immunity 24:741-752.
    • (2006) Immunity , vol.24 , pp. 741-752
    • Gomez, T.S.1
  • 22
    • 0035929128 scopus 로고    scopus 로고
    • Positive regulation of T cell activation and integrin adhesion by the adapter Fyb/Slap
    • Griffiths, E. K., et al. 2001. Positive regulation of T cell activation and integrin adhesion by the adapter Fyb/Slap. Science 293:2260-2263.
    • (2001) Science , vol.293 , pp. 2260-2263
    • Griffiths, E.K.1
  • 23
    • 0036604987 scopus 로고    scopus 로고
    • Communication between the TCR and integrins: role of the molecular adapter ADAP/Fyb/Slap
    • Griffiths, E. K., and J. M. Penninger. 2002. Communication between the TCR and integrins: role of the molecular adapter ADAP/Fyb/Slap. Curr. Opin. mmunol. 14:317-322.
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 317-322
    • Griffiths, E.K.1    Penninger, J.M.2
  • 24
    • 21244492894 scopus 로고    scopus 로고
    • Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells
    • Huang, Y., et al. 2005. Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells. J. Biol. Chem. 280:23576-23583.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23576-23583
    • Huang, Y.1
  • 25
    • 0037318720 scopus 로고    scopus 로고
    • Adaptors as central mediators of signal transduction in immune cells
    • Jordan, M. S., A. L. Singer, and G. A. Koretzky. 2003. Adaptors as central mediators of signal transduction in immune cells. Nat. Immunol. 4:110-116.
    • (2003) Nat. Immunol. , vol.4 , pp. 110-116
    • Jordan, M.S.1    Singer, A.L.2    Koretzky, G.A.3
  • 26
    • 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., et al. 2000. Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton. J. Cell Biol. 149:181-194.
    • (2000) J. Cell Biol. , vol.149 , pp. 181-194
    • Krause, M.1
  • 27
    • 1642373183 scopus 로고    scopus 로고
    • Identification of pro-interleukin 16 as a novel target of MAP kinases in activated T lymphocytes
    • Laurence, A., E. Astoul, S. Hanrahan, N. Totty, and D. Cantrell. 2004. Identification of pro-interleukin 16 as a novel target of MAP kinases in ctivated T lymphocytes. Eur. J. Immunol. 34:587-597.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 587-597
    • Laurence, A.1    Astoul, E.2    Hanrahan, S.3    Totty, N.4    Cantrell, D.5
  • 28
    • 77950263357 scopus 로고    scopus 로고
    • The adapter protein Nck: role of individual SH3 and SH2 binding modules for protein interactions in T lymphocytes
    • Lettau, M., et al. 2010. The adapter protein Nck: role of individual SH3 and SH2 binding modules for protein interactions in T lymphocytes. Protein ci. 19:658-669.
    • (2010) Protein Sci , vol.19 , pp. 658-669
    • Lettau, M.1
  • 29
    • 84877990371 scopus 로고    scopus 로고
    • Nck adapter proteins: functional versatility in T cells
    • Lettau, M., J. Pieper, and O. Janssen. 2009. Nck adapter proteins: functional versatility in T cells. Cell Commun. Signal. 7:1.
    • (2009) Cell Commun. Signal. , vol.7 , pp. 1
    • Lettau, M.1    Pieper, J.2    Janssen, O.3
  • 30
    • 27844541329 scopus 로고    scopus 로고
    • Differential recruitment of pre-mRNA splicing factors to alternatively spliced transcripts in vivo
    • Mabon, S. A., and T. Misteli. 2005. Differential recruitment of pre-mRNA splicing factors to alternatively spliced transcripts in vivo. PLoS Biol. 3:e374.
    • (2005) PLoS Biol , vol.3
    • Mabon, S.A.1    Misteli, T.2
  • 31
    • 0035811573 scopus 로고    scopus 로고
    • Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor
    • Miyoshi-Akiyama, T., L. M. Aleman, J. M. Smith, C. E. Adler, and B. J. Mayer. 2001. Regulation of Cbl phosphorylation by the Abl tyrosine kinase nd the Nck SH2/SH3 adaptor. Oncogene 20:4058-4069.
    • (2001) Oncogene , vol.20 , pp. 4058-4069
    • Miyoshi-Akiyama, T.1    Aleman, L.M.2    Smith, J.M.3    Adler, C.E.4    Mayer, B.J.5
  • 32
    • 0030959305 scopus 로고    scopus 로고
    • Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases
    • Musci, M. A., et al. 1997. Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine inases. J. Biol. Chem. 272:11674-11677.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11674-11677
    • Musci, M.A.1
  • 33
    • 30044446991 scopus 로고    scopus 로고
    • The WAVE2 complex regulates actin cytoskeletal reorganization and CRAC-mediated calcium entry during T cell activation
    • Nolz, J. C., et al. 2006. The WAVE2 complex regulates actin cytoskeletal reorganization and CRAC-mediated calcium entry during T cell activation. urr. Biol. 16:24-34.
    • (2006) Curr. Biol. , vol.16 , pp. 24-34
    • Nolz, J.C.1
  • 34
    • 34548259213 scopus 로고    scopus 로고
    • WAVE2 regulates high-affinity integrin binding by recruiting vinculin and talin to the immunological synapse
    • Nolz, J. C., et al. 2007. WAVE2 regulates high-affinity integrin binding by recruiting vinculin and talin to the immunological synapse. Mol. Cell. Biol. 7:5986-6000.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5986-6000
    • Nolz, J.C.1
  • 35
    • 0037902494 scopus 로고    scopus 로고
    • The TCR ADAPts to integrin-mediated cell adhesion
    • Peterson, E. J. 2003. The TCR ADAPts to integrin-mediated cell adhesion. Immunol. Rev. 192:113-121.
    • (2003) Immunol. Rev. , vol.192 , pp. 113-121
    • Peterson, E.J.1
  • 36
    • 0035929222 scopus 로고    scopus 로고
    • Coupling of the TCR to integrin activation by Slap-130/Fyb
    • Peterson, E. J., et al. 2001. Coupling of the TCR to integrin activation by Slap-130/Fyb. Science 293:2263-2265.
    • (2001) Science , vol.293 , pp. 2263-2265
    • Peterson, E.J.1
  • 37
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins
    • Samelson, L. E. 2002. Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu. Rev. Immunol. 20:371-394.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 38
    • 0035976905 scopus 로고    scopus 로고
    • Hematopoietic progenitor kinase 1 associates physically and functionally with the adaptor proteins B cell linker protein and SLP-76 in lymphocytes
    • Sauer, K., et al. 2001. Hematopoietic progenitor kinase 1 associates physically and functionally with the adaptor proteins B cell linker protein and SLP-6 in lymphocytes. J. Biol. Chem. 276:45207-45216.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45207-45216
    • Sauer, K.1
  • 39
    • 33847259789 scopus 로고    scopus 로고
    • Formin the way
    • Schwartzberg, P. L. 2007. Formin the way. Immunity 26:139-141.
    • (2007) Immunity , vol.26 , pp. 139-141
    • Schwartzberg, P.L.1
  • 40
    • 0036862530 scopus 로고    scopus 로고
    • Changes in actin dynamics at the T-cell/APC interface: implications for T-cell anergy?
    • Sechi, A. S., J. Buer, J. Wehland, and M. Probst-Kepper. 2002. Changes in actin dynamics at the T-cell/APC interface: implications for T-cell anergy? mmunol. Rev. 189:98-110.
    • (2002) Immunol. Rev. , vol.189 , pp. 98-110
    • Sechi, A.S.1    Buer, J.2    Wehland, J.3    Probst-Kepper, M.4
  • 41
    • 67651009429 scopus 로고    scopus 로고
    • The importance of Src homology 2 domain-containing leukocyte phosphoprotein of 76 kilodaltons sterile-alpha motif domain in thymic selection and T-cell activatio
    • Shen, S., et al. 2009. The importance of Src homology 2 domain-containing leukocyte phosphoprotein of 76 kilodaltons sterile-alpha motif domain in hymic selection and T-cell activation. Blood 114:74-84.
    • (2009) Blood , vol.114 , pp. 74-84
    • Shen, S.1
  • 42
    • 38049112582 scopus 로고    scopus 로고
    • Mononeme: a new secretory organelle in Plasmodium falciparum merozoites identified by localization of rhomboid-1 protease
    • Singh, S., M. Plassmeyer, D. Gaur, and L. H. Miller. 2007. Mononeme: a new secretory organelle in Plasmodium falciparum merozoites identified by localization of rhomboid-1 protease. Proc. Natl. Acad. Sci. U. S. A. 104: 20043-20048.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 20043-20048
    • Singh, S.1    Plassmeyer, M.2    Gaur, D.3    Miller, L.H.4
  • 43
    • 33846031421 scopus 로고    scopus 로고
    • The actin cloud induced by LFA-1-mediated outside-in signals lowers the threshold for T-cell activation
    • Suzuki, J., S. Yamasaki, J. Wu, G. A. Koretzky, and T. Saito. 2007. The actin cloud induced by LFA-1-mediated outside-in signals lowers the threshold for T-cell activation. Blood 109:168-175.
    • (2007) Blood , vol.109 , pp. 168-175
    • Suzuki, J.1    Yamasaki, S.2    Wu, J.3    Koretzky, G.A.4    Saito, T.5
  • 44
    • 33645643086 scopus 로고    scopus 로고
    • Protein-tyrosine kinase and GTPase signals cooperate to phosphorylate and activate Wiskott-Aldrich syndrome protein (WASP)/neuronal WASP
    • Torres, E., and M. K. Rosen. 2006. Protein-tyrosine kinase and GTPase signals cooperate to phosphorylate and activate Wiskott-Aldrich syndrome protein (WASP)/neuronal WASP. J. Biol. Chem. 281:3513-3520.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3513-3520
    • Torres, E.1    Rosen, M.K.2
  • 45
    • 7244221321 scopus 로고    scopus 로고
    • ADAP-SLP-76 binding differentially regulates supramolecular activation cluster (SMAC) formation relative to T cell-APC conjugation
    • Wang, H., et al. 2004. ADAP-SLP-76 binding differentially regulates supramolecular activation cluster (SMAC) formation relative to T cell-APC onjugation. J. Exp. Med. 200:1063-1074.
    • (2004) J. Exp. Med. , vol.200 , pp. 1063-1074
    • Wang, H.1
  • 46
    • 68149153184 scopus 로고    scopus 로고
    • SLP-76-ADAP adaptor module regulates LFA-1 mediated costimulation and T cell motility
    • Wang, H., B. Wei, G. Bismuth, and C. E. Rudd. 2009. SLP-76-ADAP adaptor module regulates LFA-1 mediated costimulation and T cell motility. roc. Natl. Acad. Sci. U. S. A. 106:12436-12441.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 12436-12441
    • Wang, H.1    Wei, B.2    Bismuth, G.3    Rudd, C.E.4
  • 47
    • 75649117395 scopus 로고    scopus 로고
    • The right team at the right time to go for a home run: tyrosine kinase activation by the TCR
    • Weiss, A. 2010. The right team at the right time to go for a home run: tyrosine kinase activation by the TCR. Nat. Immunol. 11:101-104.
    • (2010) Nat. Immunol. , vol.11 , pp. 101-104
    • Weiss, A.1
  • 48
    • 8444247821 scopus 로고    scopus 로고
    • The SLP-76 family of adapter proteins
    • Wu, J. N., and G. A. Koretzky. 2004. The SLP-76 family of adapter proteins. Semin. Immunol. 16:379-393.
    • (2004) Semin. Immunol. , vol.16 , pp. 379-393
    • Wu, J.N.1    Koretzky, G.A.2
  • 49
    • 0032910208 scopus 로고    scopus 로고
    • Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes
    • Wunderlich, L., A. Farago, J. Downward, and L. Buday. 1999. Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes. ur. J. Immunol. 29:1068-1075.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 1068-1075
    • Wunderlich, L.1    Farago, A.2    Downward, J.3    Buday, L.4
  • 50
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D. A., J. D. Violin, A. C. Newton, and R. Y. Tsien. 2002. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of ive cells. Science 296:913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 51
    • 0041845112 scopus 로고    scopus 로고
    • SLP-76 coordinates Nck-dependent Wiskott-Aldrich syndrome protein recruitment with Vav-1/Cdc42-dependent Wiskott-Aldrich syndrome protein activation at the T cell-APC contact site J
    • Zeng, R., et al. 2003. SLP-76 coordinates Nck-dependent Wiskott-Aldrich syndrome protein recruitment with Vav-1/Cdc42-dependent Wiskott-Aldrich syndrome protein activation at the T cell-APC contact site J. Immunol. 171:1360-1368.
    • (2003) Immunol , vol.171 , pp. 1360-1368
    • Zeng, R.1
  • 52
    • 30044438580 scopus 로고    scopus 로고
    • Role for the Abi/wave protein complex in T cell receptor-mediated proliferation and cytoskeletal remodeling
    • Zipfel, P. A., et al. 2006. Role for the Abi/wave protein complex in T cell receptor-mediated proliferation and cytoskeletal remodeling. Curr. Biol. 6:35-46.
    • (2006) Curr. Biol. , vol.16 , pp. 35-46
    • Zipfel, P.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.