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Identification of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains.
J BIOL CHEM
26291 - 26295.
Src homology 3 (SH3) domains have been shown to mediate selected interactions between signaling molecules and are essential for the activation of a number of receptor-driven pathways. The Wiskott-Aldrich syndrome protein was identified as a protein that associated selectively with the SH3 domains derived from c-Src, p85 alpha, phospholipase C gamma 1, and c-Fgr. Significantly reduced association was detected to the N-terminal SH3 domain and the tandem SH3 domains of p47(phox), and no binding was detected to the SH3 domain of n-Src, the C-terminal SH3 domain of p47(phox), or either of the SH3 domains of p67(phox). Three peptides corresponding to potential Wiskott-Aldrich syndrome protein SH3 domain binding moths were found to inhibit its association with c-Src, Fgr, and phospholipase C gamma 1 SH3 domains, but not the p85 alpha SH3 domain. These peptides have the sequences MRRQEPLPPPPPPSRG, TGRSGPLPPPPPGA, and KGRSGPLPPVPLGI and show homology with other SH3 domain binding motifs. It is possible that the intracellular association of Wiskott-Aldrich syndrome protein with other signaling proteins is mediated by its SH3 domain-binding regions, and this may play a role in its putative function as a regulatory molecule in immune cells.
|Title:||Identification of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains|
|Open access status:||An open access publication|
|Keywords:||PROLINE-RICH PEPTIDES, PHAGOCYTE NADPH OXIDASE, SH3 DOMAIN, TYROSINE KINASES, CRYSTAL-STRUCTURES, FOCAL ADHESION, BINDING MOTIF, HIGH-AFFINITY, GENE, SPECIFICITY|
|UCL classification:||UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences > Medicine (Division of)
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