Vinexin Forms a Signaling Complex with Sos and Modulates Epidermal Growth Factor-induced c-Jun N-terminal Kinase/Stress-activated Protein Kinase Activities

Vinexin, a novel protein that plays a key role in cell spreading and cytoskeletal organization, contains three SH3 domains and binds to vinculin through its first and second SH3 domains. We show here that the third SH3 domain binds to Sos, a guanine nucleotide exchange factor for Ras and Rac, both i...

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Veröffentlicht in:	The Journal of biological chemistry 1999-12, Vol.274 (50), p.35933-35937
Hauptverfasser:	Akamatsu, M, Aota, S, Suwa, A, Ueda, K, Amachi, T, Yamada, K M, Akiyama, S K, Kioka, N
Format:	Artikel
Sprache:	eng
Schlagworte:	3T3 Cells Animals c-Jun N-terminal kinase Chromatography, Affinity Epidermal Growth Factor - pharmacology JNK Mitogen-Activated Protein Kinases Kinetics Mice Mitogen-Activated Protein Kinases - metabolism Muscle Proteins - chemistry Muscle Proteins - isolation & purification Muscle Proteins - metabolism Phosphorylation Platelet-Derived Growth Factor - pharmacology Point Mutation Recombinant Fusion Proteins - metabolism Signal Transduction Son of Sevenless Proteins - chemistry Son of Sevenless Proteins - isolation & purification Son of Sevenless Proteins - metabolism Sos protein src Homology Domains stress-activated protein kinase Transfection vinexin
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