Recruitment of VAV to p-SLP-76

Stable Identifier
Reaction [binding]
Homo sapiens
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VAV an activator of RAC-GTPases, is redistributed to plasma membrane and is phosphorylated following engagement of FCERI. Phosphorylated SLP-76 tyrosines Y113 and Y128 (112Y and 128Y in mouse) provide binding sites for the SH2 domains of VAV. The binding of VAV to these phosphotyrosine residues may link SLP-76 to the Jun amino-terminal kinase (JNK) pathway and the actin cytoskeleton (Kettner et al. 2003).
In addition to its known role as guanine nucleotide exchange factor (GEF), VAV also modulates cytokine production in mast cells. VAV1-deficient bone marrow-derived mast cells exhibited reduced degranulation and cytokine production and calcium release in addition of reduced activation of c-Jun NH2-terminal kinase 1 (JNK1), although tyrosine phosphorylation of FCERI, SYK and LAT was normal (Manetz et al. 2001, Arudchandran et al. 2000, Song et al. 1999).

Literature References
PubMed ID Title Journal Year
10395673 Tyrosine phosphorylation of Vav stimulates IL-6 production in mast cells by a Rac/c-Jun N-terminal kinase-dependent pathway

Scott, PM, Rivera, J, Song, JS, Haleem-Smith, H, Mill, JF, Tan, TH, Gomez, J, Arudchandran, R

J. Immunol. 1999
11340169 Vav1 regulates phospholipase cgamma activation and calcium responses in mast cells

Gonzalez-Espinosa, C, Rivera, J, Xirasagar, S, Manetz, TS, Tybulewicz, V, Arudchandran, R

Mol. Cell. Biol. 2001
8673706 Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation

Motto, DG, Weiss, A, Koretzky, GA, Wu, J

Immunity 1996
Orthologous Events
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