SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors

Molecular and Cellular Biology

Volumn 19, Issue 2, 1999, Pages 1539-1546

  Larbolette, Oliver ^a   Wollscheid, Bernd ^a   Schweikert, Jutta ^a   Nielsen, Peter J ^a   Wienands, Jürgen ^a,b  

^a UNIVERSITY OF FREIBURG   (Germany)

^b MAX PLANCK INSTITUTE OF IMMUNOBIOLOGY AND EPIGENETICS   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ADAPTOR PROTEIN; AMINO ACID; LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN TYROSINE KINASE; TYROSINE;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONFOCAL LASER MICROSCOPY; CONTROLLED STUDY; CYTOSKELETON; IMMUNOBLOTTING; MOUSE; NONHUMAN; PHOSPHORYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

ANIMALIA;

EID: 0032952693     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.2.1539     Document Type: Article

References (47)

1. Baumann, G., D. Maier, F. Freuler, C. Tschopp, K. Baudisch, and J. Wienands. 1994. In vitro characterization of major ligands for Src homology 2 domains derived from tyrosine kinases, from the adaptor protein SHC and from GTPase-activating protein in Ramos B cells. Eur. J. Immunol. 42:1799-1807.
2. Borg, J.-P., and B. Margolis. 1998. Function of PTB domains. Curr. Top. Microbiol. Immunol. 228:23-38.
3. Bork, P., and M. Sudol. 1994. The WW domain: a signalling site in dystrophin. Trends Biochem. Sci. 19:531-533.
4. Caplan, S., S. Zeliger, L. Wang, and M. Baniyash. 1995. Cell-surface-expressed T-cell antigen-receptor ζ chain is associated with the cytoskeleton. Proc. Natl. Acad. Sci. USA 92:4768-4772.
5. Carpino, N., D. Wisniewski, A. Strife, D. Marshak, R. Kobayashi, B. Stillman, and B. Clarkson. 1997. p62dok: a constitutively tyrosine-phosphorylated GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell 88:197-204.
6. Cox, D., P. Chang, T. Kurosaki, and S. Greenberg. 1996. Syk tyrosine kinase is required for immunoreceptor tyrosine activation motif-dependent actin assembly. J. Biol. Chem. 271:16597-16602.
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 385:169-172.
8. DeFranco, A. L. 1997. The complexity of signaling pathways activated by the BCR. Curr. Opin. Immunol. 9:296-308.
9. deHostos, E. L., B. Bradtke, F. Lottspeich, and G. Gerisch. 1993. Coactosin, a 17 kDa F-actin binding protein from Dictyostelium discoideum. Cell Motil. Cytoskelet. 26:181-191.
10. Drubrin, D. G., J. Mulholland, Z. Zhu, and U. Botstein. 1990. Homology of a yeast actin-binding protein to signal transduction proteins and myosin-1. Nature 343:288-290.
11. Feng, S., J. K. Chen, H. Yu, J. A. Simon, and S. L. Schreiber. 1994. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266:1241-1247.
12. Fischer, K.-D., Y.-Y. Kong, K. Tedford, L. E. M. Marengère, I. Kozieradzki, T. Sasaki, M. Starr, G. Chan, S. Gardener, M. P. Nghiem, D. Bouchard, M. Barbacid, A. Bernstein, and J. M. Penninger. 1998. Vav is a regulator of the cytoskeletal reorganization mediated by the T-cell receptor. Curr. Biol. 8:554-562.
13. Freemann, N. L., T. Lila, K. Mintzer, Z. Chen, A. J. Pahk, R. Ren, D. G. Drubin, and J. Field. 1996. A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization. Mol. Cell. Biol. 16:548-556.
14. Gold, M. R., M. T. Crowley, G. A. Martin, F. McCormick, and A. L. De-Franco. 1993. Targets of B lymphocyte antigen receptor signal transduction include the p21ras GTPase-activating protein (GAP) and two GAP-associated proteins. J. Immunol. 150:377-386.
15. Holsinger, L. J., I. A. Graef, W. Swat, T. Chi, D. M. Bautista, L. Davidson, R. S. Lewis, F. W. Alt, and G. R. Crabtree. 1998. Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction. Curr. Biol. 8:563-572.
16. Kurosaki, T. 1997. Molecular mechanisms in B cell antigen receptor signaling. Curr. Opin. Immunol. 9:309-318.
17. Langdon, W. Y., J. W. Hartley, S. P. Klinken, S. K. Ruscetti, and H. C. D. Morse. 1989. v-cbl, an oncogene from a dual-recombinant murine retrovirus that induces early B-lineage lymphomas. Proc. Natl. Acad. Sci. USA 86: 1168-1172.
18. Lemmon, M. A., M. Falasca, K. M. Ferguson, and J. Schlessinger. 1997. Regulatory recruitment of signalling molecules to the cell membrane by pleckstrin-homology domains. Trends Cell Biol. 7:237-242.
19. Lowin-Kropf, B., V. Smith Shapiro, and A. Weiss. 1998. Cytoskeletal polarization of T cells is regulated by an immunoceptor tyrosine-based activation motif-dependent mechanism. J. Cell Biol. 140:861-971.
20. Marano, N., D. Holowka, and B. Baird. 1989. Bivalent binding of an anti-CD3 antibody to Jurkat cells induces association of the T cell receptor complex with cytoskeleton. J. Immunol. 143:931-938.
21. Mayer, B. J., and M. J. Eck. 1995. Minding your p's and q's. Curr. Biol. 4:364-367.
22. Mayer, B. J., and G. Gupta. 1998. Functions of SH2 and SH3 domains. Curr. Top. Microbiol. Immunol. 228:1-22.
23. Panchamoorthy, G., T. Fukazawa, S. Miyake, S. Soltoff, K. Reedquist, B. Druker, S. Shoelson, L. Cantley, and H. Band. 1996. p120cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphytidylinositol 3-kinase. J. Biol. Chem. 271:3187-3194.
24. Park, J. Y., and J. Jongstra-Bilen. 1997. Interactions between membrane IgM and the cytoskeleton involve the cytoplasmic domain of the immunoglobulin receptor. Eur. J. Immunol. 27:3001-3009.
25. Pawson, T. 1995. Protein modules and signalling networks. Nature 373:573-580.
26. Posas, F., and H. Saito. 1997. Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of PBS2p MAPKK. Science 276:1702-1705.
27. Reif, K., and D. A. Cantrell. 1998. Networking Rho family GTPases in lymphocytes. Immunity 8:395-401.
28. Ren, R., B. J. Mayer, P. Cicchetti, and D. Baltimore. 1993. Identification of a 10-amino acid proline-rich SH3 binding site. Science 259:1157-1161.
29. Reth, M., and J. Wienands. 1997. Initiation and processing of signals from the B cell antigen receptor. Annu. Rev. Immunol. 15:453-479.
30. Röhrig, U., G. Gerisch, L. Morozova, M. Schleicher, and A. Wegner. 1995. Coactosin interferes with the capping of actin filaments. FEBS Lett. 374: 284-286.
31. Rozdzial, M. M., B. Malissen, and T. H. Finkel. 1995. Tyrosine-phosphorylated T cell receptor ζ chain associates with the actin cytoskeleton upon activation of mature T lymphocytes. Immunity 3:623-633.
32. Sakai, R., A. Iwamatsu, N. Hirano, S. Ogawa, T. Tanaka, H. Mano, Y. Yazaki, and H. Hirai. 1994. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 13:3748-3756.
33. Shirao, T. 1995. The roles of microfilament-associated proteins, drebrins, in brain morphogenesis. J. Biochem. 117:231-236.
34. Songyang, Z., S. E. Shoelson, M. Chaudhuri, C. Gish, T. Pawson, W. G. Haser, F. King, T. Roberts, S. Ratnotsky, R. J. Lechleider, B. G. Neel, R. B. Birge, J. E. Fajardo, M. M. Chou, H. Hanafusa, B. Schaffhausen, and L. C. Cantley. 1993. SH2 domains recognize specific phosphopeptide sequences. Cell 72:767-778.
35. Sparks, A. B., N. G. Hoffmann, S. J. McConnell, D. M. Fowlkes, and B. K. Kay. 1996. Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins. Nat. Biotechnol. 14:741-744.
36. Staub, O., and D. Rotin. 1996. WW domains. Structure 4:495-499.
37. Tarakhovsky, A., M. Turner, S. Schaal, P. J. Mee, L. P. Duddy, K. Rajewsky, and V. L. Tybulewicz. 1995. Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav. Nature 374:467-470.
38. Tezuka, T., H. Umemori, N. Fusaki, T. Yagi, M. Takata, T. Kurosaki, and T. Yamamoto. 1996. Physical and functional association of the cbl proto-oncogene product with an Src-family protein tyrosine kinase, p53/56lyn, in the B cell antigen receptor-mediated signaling. J. Exp. Med. 183:675-680.
39. Tsunoda, S., J. Sierralta, Y. Sun, R. Bodner, E. Suzuki, A. Becker, M. Socolich, and C. S. Zuker. 1997. A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade. Nature 388:243-249.
40. Tuosto, L., F. Michel, and O. Acuto. 1996. p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells. J. Exp. Med. 184:1161-1166.
41. Wesp, A., L. Hicke, J. Palecek, R. Lombardi, T. Aust, A. L. Munn, and H. Riezman. 1997. End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell 8:2291-2306.
42. Wienands, J., O. Larbolette, and M. Reth. 1996. Evidence for a preformed transducer complex organized by the B cell antigen receptor. Proc. Natl. Acad. Sci. USA 93:7865-7870.
43. Wienands, J., J. Schweikert, B. Wollscheid, H. Jumaa, P. J. Nielsen, and M. Reth. 1998. SLP-65: a new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation. J. Exp. Med. 188:791-795.
44. 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.
45. Yamanashi, Y., and D. Baltimore. 1997. Identification of the Abl- and ras-GAP-assodated 62 kDa protein as a docking protein, Dok. Cell 88:205-211.
46. Yamanashi, Y., M. Okada, T. Semba, T. Yamori, H. Umemori, S. Tsunasawa, K. Toyoshima, D. Kitamura, T. Watanabe, and T. Yamamoto. 1993. Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling. Proc. Natl. Acad. Sci. USA 90:3631-3635.
47. Zhang, R., F. W. Alt, L. Davidson, S. H. Orkin, and W. Swat. 1995. Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene. Nature 374:470-473.