Ask about this productRelated genes to: WASL antibody
- Gene:
- NCKIPSD NIH gene
- Name:
- NCK interacting protein with SH3 domain
- Previous symbol:
- -
- Synonyms:
- AF3P21, SPIN90, ORF1, WISH, WASLBP, DIP1
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 2004-02-26
- Date modifiied:
- 2016-10-05
- Gene:
- WASL NIH gene
- Name:
- WASP like actin nucleation promoting factor
- Previous symbol:
- -
- Synonyms:
- N-WASP, NWASP, WASPB
- Chromosome:
- 7q31.32
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-14
- Date modifiied:
- 2019-02-15
Related products to: WASL antibody
Related articles to: WASL antibody
- DIP/WISH binds to mammalian diaphanous and N-WASP, and functions as a scaffold protein by binding to Nck protein (called SPIN90). In addition, DIP/WISH accelerates actin polymerization through integration with N-WASP and is involved in cytoskeletal dynamics. We previously reported that DIP controls the activities of Rho GTPases in a Src-dependent manner, and accordingly contributes to cell motility (Meng et al. 2004). Here, we made the mice lacking DIP/WISH and demonstrated that DIP/WISH is critical for cell motility and adhesion by using murine embryonic fibroblasts (MEF). Rho activity was higher in DIP/WISH-deficient MEF cells even before platelet-derived growth factor (PDGF) or adhesion stimulation. Cell motility and adhesion were impaired in DIP/WISH-deficient MEF cells, and the MEF cells moved little probably due to the deficiency of tail retractions although they had many small membrane ruffles. Consistent with high Rho activity, DIP/WISH-deficient MEF cells exhibited many stress fibers due to clustering pre-existing actin filament. Thus, DIP/WISH is a negative regulator of Rho and modulates cell adhesion by controlling the integration of adhesion molecules. - Source: PubMed
Fukumi-Tominaga TomokoMori YoshikoMatsuura AtsukoKaneko KeikoMatsui MakotoOgata MasatoTominaga Makoto - One of the pathological characteristics of Alzheimer's disease (AD) is the formation of dystrophic neurites accompanied by aberrant neuronal sprouting. Although a number of studies have focussed on the formation of amyloid plaques and neurofibrillary tangles, the mechanism of neuronal sprouting in AD is not fully understood. The protein levels of neural Wiskott-Aldrich syndrome protein (N-WASP), WASP interacting SH3 protein (WISH) and WASP family verprolin-homologous protein (WAVE) were significantly increased in AD brains. In addition, N-WASP, WISH and WAVE were co-localized with filamentous actin in abnormal dendrite-like processes sprouting from staurosporine-treated human SH-SY5Y cells. These results suggest that N-WASP, WISH and WAVE may participate in the neurodegenerative aberrant sprouting in AD neurons. - Source: PubMed
Kitamura YoshihisaTsuchiya DaijuTakata KazuyukiShibagaki KeiichiTaniguchi TakashiSmith Mark APerry GeorgeMiki HiroakiTakenawa TadaomiShimohama Shun - We identified a novel adaptor protein that contains a Src homology (SH)3 domain, SH3 binding proline-rich sequences, and a leucine zipper-like motif and termed this protein WASP interacting SH3 protein (WISH). WISH is expressed predominantly in neural tissues and testis. It bound Ash/Grb2 through its proline-rich regions and neural Wiskott-Aldrich syndrome protein (N-WASP) through its SH3 domain. WISH strongly enhanced N-WASP-induced Arp2/3 complex activation independent of Cdc42 in vitro, resulting in rapid actin polymerization. Furthermore, coexpression of WISH and N-WASP induced marked formation of microspikes in Cos7 cells, even in the absence of stimuli. An N-WASP mutant (H208D) that cannot bind Cdc42 still induced microspike formation when coexpressed with WISH. We also examined the contribution of WISH to a rapid actin polymerization induced by brain extract in vitro. Arp2/3 complex was essential for brain extract-induced rapid actin polymerization. Addition of WISH to extracts increased actin polymerization as Cdc42 did. However, WISH unexpectedly could activate actin polymerization even in N-WASP-depleted extracts. These findings suggest that WISH activates Arp2/3 complex through N-WASP-dependent and -independent pathways without Cdc42, resulting in the rapid actin polymerization required for microspike formation. - Source: PubMed
Fukuoka MSuetsugu SMiki HFukami KEndo TTakenawa T