The Vav binding site (Y315) in ZAP-70 is critical for antigen receptor- mediated signal transduction

Journal of Experimental Medicine

Volumn 185, Issue 10, 1997, Pages 1877-1882

  Wu, Jun ^a   Zhao, Qihong ^b   Kurosaki, Tomohiro ^c   Weiss, Arthur ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c KANSAI MEDICAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

LYMPHOCYTE ANTIGEN RECEPTOR;

ANTIGEN ANTIBODY REACTION; B LYMPHOCYTE; BINDING SITE; PRIORITY JOURNAL; PROTO ONCOGENE; RECEPTOR BINDING; REVIEW; SIGNAL TRANSDUCTION; T LYMPHOCYTE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; B-LYMPHOCYTES; BINDING SITES; CELL CYCLE PROTEINS; CELL LINE; GLUTATHIONE TRANSFERASE; HUMANS; KINETICS; LUCIFERASES; MAMMALS; MUTAGENESIS, SITE-DIRECTED; PEPTIDE BIOSYNTHESIS; PEPTIDES; PHOSPHOPROTEINS; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-VAV; RECEPTORS, ANTIGEN, B-CELL; RECEPTORS, ANTIGEN, T-CELL; RECOMBINANT FUSION PROTEINS; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAINS; T-LYMPHOCYTES; TRANSFECTION; ZAP-70 PROTEIN-TYROSINE KINASE;

EID: 0030914118     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.185.10.1877     Document Type: Review

References (26)

1. Weiss, A., and D.R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell. 76:263-274.
2. Wange, R.L., and L.E. Samelson. 1996. Complex complexes: signaling at the TCR. Immunity. 5:197-205.
3. Bustelo, X.R., and M. Barbacid. 1992. Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells. Science (Wash. DC). 256:1196-1199.
4. Margolis, B., P. Hu, S. Katzav, J.M. Oliver, A. Ullrich, A. Weiss, and J. Schlessinger. 1992. Tyrosine phosphorylation of vav: 3 proto-oncogene combining SH2 and SH3 domains with motifs found in transcriptional factors. Nature (Lond.). 356:71-74.
5. Adams, J.M., H. Houston, J. Allen, T. Lints, and R. Harvey. 1992. The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization. Oncogene. 7:611-618.
6. Boguski, M.S., A. Bairoch, T.K. Attwood, and G.S. Michaels. 1992. Proto-vav and gene expression. Nature (Lond.). 358:113.
7. Crespo, P., K.E. Schuebel, A.A. Ostrom, J.S. Gutkind, and X.R. Bustelo. 1997. Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature (Lond.). 385:169-172.
8. Han, J., B. Das, W. Wei, L.V. Aelst, R.D. Mosteller, R. Khosravi-Far, J.K. Westwick, C.J. Der, and D. Broek. 1997. Lck regulates Vav activation of members of the Rho family of GTPases. Mol. Cell. Biol. 17:1346-1353.
9. + thymocytes. Nature (Lond.). 374:474-477.
10. Tarakhovsky, A., M. Turner, S. Schaal, P.J. Mee, L.P. Duddy, K. Rajewsky, and V.L.J. Tybulewicz. 1995. Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav. Nature (Lond.). 374:467-470.
11. Zhang, R., F.W. Alt, L. Davidson, S.H. Orkin, and W. Swat. 1995. Defective signaling through the T and B cell antigen receptors in lymphoid cells lacking the vav proto-oncogene. Nature (Lond.). 374:470-473.
12. vav activity. Mol. Cell. Biol. 15:4337-4346.
13. Wu, J., D.G. Motto, G.A. Koretzky, and A. Weiss. 1996. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Immunity. 4:593-602.
14. Katzav, S., M. Sutherland, G. Packham, T. Yi, and A. Weiss. 1994. The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-vav. J. Biol. Chem. 269:32579-32585.
15. Deckert, M., S. Tartare-Deckert, C. Couture, T. Mustelin, and A. Altman. 1996. Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product. Immunity. 5:591-604.
16. Songyang, Z., S.E. Shoelson, J. McGlade, P. Olivier, T. Pawson, X.R. Bustelo, M. Barbacid, H. Sabe, H. Hanafusa, T. Yi, et al. 1994. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol. Cell. Biol. 14:2777-2785.
17. Zhao, Q., and A. Weiss. 1996. Enhancement of lymphocyte responsiveness by a gain-of-function mutation of ZAP-70. Mol. Cell. Biol. 16:6765-6774.
18. Iwashima, M., B.A. Irving, N.S.C. van Oers, A.C. Chan, and A. Weiss. 1994. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science (Wash. DC). 263: 1136-1139.
19. Takata, M., H. Sabe, A. Hata, T. Inazu, Y. Homma, T. Nukada, H. Yamamura, and T. Kurosaki. 1994. Tyrosine kinases Lyn and Syk regulate B cell receptor-coupled Ca2+ mobilization through distinct pathways. EMBO (Eur. Mol. Biol. Organ.) J. 13:1341-1349.
20. Kong, G., J. Bu, T. Kurosaki, A.S. Shaw, and A.C. Chan. 1995. Reconstitution of Syk function by the ZAP-70 protein tyrosine kinase. Immunity. 2:485-492.
21. Straus, D.B., A.C. Chan, B. Patai, and A. Weiss. 1996. SH2 domain function is essential for the role of the Lck tyrosine kinase in T cell receptor signal transduction. J. Biol. Chem. 271:9976-9981.
22. Duplay, P., M. Thome, F. Herve, and O. Acuto. 1994. p56lck interacts via its src homology 2 domain with the ZAP-70 kinase. J. Exp. Med. 179:1163-1172.
23. Chan, A.C., M. Dalton, R. Johnson, G. Kong, T. Wang, R. Thoma, and T. Kurosaki. 1995. Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function. EMBO (Eur. Mol. Biol. Organ.) J. 14:2499-2508.
24. Watts, J.D., M. Affolter, D.L. Krebs, R.L. Wange, L.E. Samelson, and R. Aebersold. 1994. Identification by electrospray ionization mass spectrometry of the sites of tyrosine phosphorylation induced in activated Jurkat T cells on the protein tyrosine kinase ZAP-70. J. Biol. Chem. 269:29520-29529.
25. Furlong, M.T., A.M. Mahrenholz, K.-H. Kim, C.L. Ashendel, M.L. Harrison, and R.L. Geahlen. 1997. Identification of the major sites of autophosphorylation of the murine protein-tyrosine kinase syk. Biochim. Biophys. Acta. 1355:177-190.
26. Takata, M., and T. Kurosaki. 1996. A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-γ2. J. Exp. Med. 184:31-40.