Reactome | Translocation of Vav1 to CD28

Translocation of Vav1 to CD28

Stable Identifier

R-HSA-389352

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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 (Hehner et al. ).

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 Hehner, SP, Hofmann, TG, Dienz, O, Droge, W, Schmitz, ML	J Biol Chem	2000
15886116	Vav-family proteins in T-cell signalling Tybulewicz, VL	Curr Opin Immunol	2005