N-WASP (Tyr-256) (WASL) Antibody – Rabbit Polyclonal

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. [provided by RefSeq]

Function: Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Ref.11

Subunit structure: Binds actin and the Arp2/3 complex. Interacts with CDC42. Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP. Interacts with SNX9. Interacts with the WW domains of PRPF40A/FBP11

By similarity. Interacts with NOSTRIN. Interacts with Shigella flexneri protein icsA. The interaction with icsA enhances the affinity of WASL for Arp2/3, thus assembling a tight complex which has maximal activity in actin assembly. Interacts with E.coli EspF-like protein encoded on prophage U. Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF-like protein encoded on prophage U. Ref.4 Ref.5 Ref.6 Ref.11

Subcellular location: Cytoplasm › cytoskeleton

By similarity. Nucleus

By similarity. Note: Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated

Sequence similarities: Contains 1 CRIB domain.Contains 1 WH1 domain.Contains 2 WH2 domains.