Formation of a stable Src-AFAP-110 complex through either an amino- terminal or a carboxy-terminal SH2-binding motif

Molecular Carcinogenesis

Volumn 22, Issue 2, 1998, Pages 110-119

  Guappone, Anne C ^a   Weimer, Tracy ^a   Flynn, Daniel C ^a  

^a WEST VIRGINIA UNIVERSITY   (United States)

Author keywords

Actin; AFAP 110; SH2; Src; Tyrosine phosphorylation

Indexed keywords

ACTIN FILAMENT ASSOCIATED PROTEIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MUTANT PROTEIN; PHENYLALANINE; PROTEIN TYROSINE KINASE; STRUCTURAL PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL STRAIN COS1; COMPLEX FORMATION; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS;

ANIMALS; BINDING SITES; COS CELLS; MICROFILAMENT PROTEINS; MUTAGENESIS, SITE-DIRECTED; PHOSPHOPROTEINS; PHOSPHORYLATION; PRECIPITIN TESTS; PROTO-ONCOGENE PROTEINS PP60(C-SRC); SRC HOMOLOGY DOMAINS; TYROSINE;

EID: 0031806537     PISSN: 08991987     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1098-2744(199806)22:2<110::AID-MC6>3.0.CO;2-Q     Document Type: Article

References (30)

1. src with two tyrosine phosphorylated cellular proteins. Mol Cell Biol 9:3951-3958, 1989.
2. Kanner SB, Reynolds AB, Wang H-C, Parsons JT. The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110. EMBO J 10:1689-1698, 1991.
3. src substrate. Mol Cell Biol 13:7892-7900, 1993.
4. Guappone AC, Flynn DC. The integrity of the SH3 binding motif of AFAP-110 is required to facilitate tyrosine phosphorylation by, and stable complex formation with, Src. Mol Cell Biochem 175:243-252, 1997.
5. Songyang Z, Shoelson SE, Chaudburi M, et al. SH2 domains recognize specific phosphopeptide sequences. Cell 72:767-778, 1993.
6. Songyang Z, Carraway KL, Eck MJ, et al. Catalytic specificity of protein-tyrosine kinases is critical for selective signalling. Nature 373:536-539, 1995.
7. Mori S, Ronnstrand L, Yokote K, et al. Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; Involvement in the interaction with Src family tyrosine kinases. EMBO J 12:2257-2264, 1993.
8. Sakai R, Iwamatsu A, Hirano N, et al. 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, 1994.
9. Alonso G, Koegl M, Mazurenko N, Courtneidge SA. Sequence requirements for binding of Src family tyrosine kinases to activated growth factor receptors. J Biol Chem 270:9840-9848, 1995.
10. Fak. Mol Cell Biol 14:147-155, 1994.
11. src. Mol Cell Biol 14:1680-1688, 1994.
12. Taylor SJ, Shalloway D. Src and the control of cell division. Bioessays 18:9-11, 1996.
13. Fumagalli S, Totty NF, Hsuan JJ, Courtneidge SA. A target for Src in mitosis. Nature 368:871-874, 1994.
14. cas to SH2 and SH3 domains of Src kinase. J Biol Chem 271:8959-8965, 1996.
15. Lee H, Trimble JJ, Yoon DW, Regier D, Desrosiers RC, Jung JU. Genetic variation of herpesvirus saimiri subgroup A transforming protein and its association with cellular src. J Virol 71:3817-3825, 1997.
16. Wang HC, Parsons JT. Deletions and insertions within an amino-terminal domain of pp60v-src inactivate transformation and modulate membrane stability. J Virol 63:291-302, 1989.
17. Tian M, Martin GS. Reduced phosphotyrosine binding by the v-Src SH2 domain is compatible with wild-type transformation. Oncogene 12:727-734, 1996.
18. Kaplan KB, Swedlow JR, Morgan DO, Varmus HE. c-Src enhances the spreading of src-/-fibroblasts on fibronectin by a kinase-in-dependent mechanism. Genes Dev 9:1505-1517, 1995.
19. FAK, a structurally distinctive protein-tyrosine kinase associated with focal adhesions. Proc Natl Acad Sci USA 89:5192-5196, 1992.
20. Cary LA, Chang JF, Guan J-L. Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J Cell Sci 109:1787-1794, 1996.
21. Kanner SB, Reynolds AB, Vines RR, Parsons JT. Monoclonal antibodies to tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc Natl Acad Sci USA 87:3328-3332, 1990.
22. Liu M, Qin Y, Liu J, Tanswell AK, Post M. Mechanical strain induces pp60src activation and translocation to cytoskeleton in fetal rat lung cells. J Biol Chem 271:7066-7071, 1996.
23. v-src association with the cytoskeleton induces actin reorganization without affecting polymerization status. Eur J Cell Biol 52:47-59, 1990.
24. Gibson TJ, Hyvonen M, Birney E, Musacchio A, Saraste M. PH domain - The first anniversary. TIBS 19:349-353, 1994.
25. Chen C, Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7:2745-2752, 1987.
26. Guappone AC, Qian Y, Weimer T, Flynn DC. An in vivo system for analysis of stable complex formation between Src and AFAP-110. Methods in Cell Science, 18:55-65, 1996.
27. Flynn DC, Koay TC, Humphries CG, Guappone AC. AFAP-120: A variant form of the Src SH2/SH3 binding partner AFAP-110 is detected in brain and contains a novel internal sequence which binds to a 67 kDa protein. J Biol Chem 270: 3894-3899, 1995.
28. Moran MF, Koch CA, Anderson D, et al. Src homology region 2 domains direct protein-protein interactions in signal transduction. Proc Natl Acad Sci USA 87:8622-8626, 1990.
29. Patschinsky T, Hunter T, Esch FS, Cooper JA, Sefton BM. Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation. Proc Natl Acad Sci USA 79:973-977, 1982.
30. Gilmer T, Rodriguez M, Jordan S, et al. Peptide inhibitors of src SH3-SH2 phosphoprotein interactions. J Biol Chem 269:31711-31719, 1994.