形式 |
The Wiskott-Aldrich syndrome (WAS) family of proteins share similar domain structure, and are involved in transduction of signals from receptors on the cell surface to the actin cytoskeleton. The presence of a number of different motifs suggests that they are regulated by a number of different stimuli, and interact with multiple proteins. Recent studies have demonstrated that these proteins, directly or indirectly, associate with the small GTPase, Cdc42, known to regulate formation of actin filaments, and the cytoskeletal organizing complex, Arp2/3. The WASL gene product is a homolog of WAS protein, however, unlike the latter, it is ubiquitously expressed and shows highest expression in neural tissues. It has been shown to bind Cdc42 directly, and induce formation of long actin microspikes.
|
復(fù)溶 |
Regulation of actin polymerization and adhesion-dependent cell edge protrusion by the Abl-related gene (Arg) tyrosine kinase and N-WASp. Miller MM, et al. Biochemistry, 2010 Mar 16. PMID 20146487.The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility. Weisswange I, et al. Nature, 2009 Mar 5. PMID 19262673.The Toca-1-N-WASP complex links filopodial formation to endocytosis. Bu W, et al. J Biol Chem, 2009 Apr 24. PMID 19213734.Overexpression of N-WASP in the brain of human epilepsy. Xiao F, et al. Brain Res, 2008 Oct 3. PMID 18708039.Inhibition of cytokinesis by wiskostatin does not rely on N-WASP/Arp2/3 complex pathway. Bompard G, et al. BMC Cell Biol, 2008 Jul 30. PMID 18667055.
|