Source:http://www.reactome.org/biopax/48887BiochemicalReaction2313
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Authored: Garapati, P V, 2008-12-16 11:12:19,
Edited: Garapati, P V, 2008-12-16 11:12:19,
Reviewed: Bluestone, JA, Esensten, J, 2009-06-01 18:47:33,
Vav1 protein is a cytoplasmic guanine nucleotide exchange factor (GEF) for Rho-family GTPases. CD28 co-stimulation resulted in a prolonged and sustained phosphorylation and membrane localization of Vav1 in comparison to T-cell receptor activation alone. Vav1 contains a unique arrangement of signaling motifs a calponin homology domain, an acidic domain, a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain (CR), and a SH2 domain flanked by two proline-binding SH3 domains. Vav-1 may be recruited to the membrane through its PH domain by binding PI(3,4,5)P3 produced by CD28-bound PI3K and also by binding to CD28:Grb2 complexes by the dimerized SH3 domains in both the molecules.
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Translocation of Vav1 to CD28
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