Lymphocyte cytosolic protein 2


Lymphocyte cytosolic protein 2, also known as LCP2 or SLP-76, is a gene that encodes a signal-transducing adaptor protein.

Structure

No full structure for SLP-76 has been solved. The PDB file 1H3H depicts the SH3 domain of GRAP2 in complex with an RSTK-containing peptide representing residues 226–235 of SLP-76.

Function

SLP-76 was originally identified as a substrate of the ZAP-70 protein tyrosine kinase following T cell receptor ligation in the leukemic T cell line Jurkat. The SLP-76 locus has been localized to human chromosome 5q33 and the gene structure has been partially characterized in mice. The human and murine cDNAs both encode 533 amino acid proteins that are 72% identical and composed of three modular domains. The NH2-terminus contains an acidic region that includes a PEST domain and several tyrosine residues that are phosphorylated following TCR ligation. SLP-76 also contains a central proline-rich domain and a COOH-terminal SH2 domain. A number of additional proteins have been identified that associate with SLP-76 both constitutively and inducibly following receptor ligation, supporting the notion that SLP-76 functions as an adaptor or scaffold protein. Studies using SLP-76-deficient T cell lines or mice have provided strong evidence that SLP-76 plays a positive role in promoting T cell development and activation as well as mast cell and platelet function. SLP-76 might serve as an integration point for signals by activating NK cell receptors. In NK cells, SLP-76 can be phosphorylated by SYK or ZAP70 following ligation of activating receptors.

Interactions

Lymphocyte cytosolic protein 2 has been shown to interact with: