N-WASP Antibody - #AF7532

Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression (By similarity). Plays a role in dendrite spine morphogenesis (By similarity). Decreasing levels of DNMBP (using antisense RNA) alters apical junction morphology in cultured enterocytes, junctions curve instead of being nearly linear.

Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity.

Cytoplasm>Cytoskeleton. Nucleus. Cytoplasm.
Note: Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm (By similarity).

Binds actin and the Arp2/3 complex. Interacts with CDC42. Interacts with FCHSD1 (By similarity). Interacts with FCHSD2. Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP. Interacts with SNX9 (By similarity). Interacts with the WW domains of PRPF40A/FBP11 (By similarity). Interacts with PTK2/FAK1 (By similarity). Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity). Interacts with NOSTRIN. Binds to TNK2. Interacts with SNX33. Interacts with NONO (via second RRM domain); the interaction is direct. Component of a multiprotein complex with NONO and SFPQ; associates with the complex via direct interaction with NONO.

(Microbial infection) Interacts with E.coli effector protein EspF(U). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U).

(Microbial infection) 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.