The translational product of the Vav proto-oncogene is exclusively expressed in cells of hematopoietic origin and is critical for lymphocyte development and activation. However, the biochemical basis of Vavâ€™s function is unclear. Vav contains a single SH2 domain that is required for its association with the T cell receptor (TCR). Overexpression of Vav or SLP-76 in Jurkat cells leads to NFAT activation and IL-2 production. When co-expressed, Vav and SLP-76 synergize to induce a robust basal and TCR-mediated IL-2 response. Although SLP-76 does not contain a motif that would indicate it to be a member of the tyrosine, serine/threonine or lipid kinase families, it does contain several putative SH2/SH3-binding domains and has been shown to physically associate with the adapter protein GRB2 as well as PLC g1. The discovery of SLP-76 represents an important step in elucidating the mechanism of Vav transformation and TCR-mediated NFAT activation.
Synonyms: 76 kDa tyrosine phosphoprotein, CG8697, LCP 2, LCP 2, LCP2, LCP2_HUMAN, Lymphocyte Cytosolic Protein 2, Lymphocyte Cytosolic Protein 2, SH2 Domain Containing Leukocyte Protein 76 KD, SH2 domain containing leukocyte protein of 76kD, SH2 domain containing leukocyte protein of 76 kDa, SH2 domain-containing leukocyte protein of 76 kDa, SLP 76, SLP 76, SLP 76 tyrosine phosphoprotein, SLP-76 tyrosine phosphoprotein, SLP76, SLP76 tyrosine phosphoprotein.