Translocation of Vav1 to CD28

Stable Identifier
Reaction [binding]
Homo sapiens
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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.
Literature References
PubMed ID Title Journal Year
18295596 CD28 and Grb-2, relative to Gads or Grap, preferentially co-operate with Vav1 in the activation of NFAT/AP-1 transcription

Schneider, H, Rudd, CE

Biochem Biophys Res Commun 2008
10849438 Tyrosine-phosphorylated Vav1 as a point of integration for T-cell receptor- and CD28-mediated activation of JNK, p38, and interleukin-2 transcription

Hofmann, TG, Hehner, SP, Dienz, O, Schmitz, ML, Droge, W

J Biol Chem 2000
15886116 Vav-family proteins in T-cell signalling

Tybulewicz, VL

Curr Opin Immunol 2005
Orthologous Events
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