Translocation of N-WASP by nuclear localization and export signals into the nucleus modulates expression of HSP90.

摘要: N-WASP regulates the actin cytoskeleton through activation of Arp2/3 complex. localizes at cell periphery, where it controls polymerization downstream signal molecules such as adapter proteins, Cdc42, Src family kinases, and phosphoinositides. also in nucleus; however, role nucleus is unclear. Here, we show that localization controlled phosphorylation by kinases which phosphorylated exported from a nuclear export (NES) leptomycin B-dependent manner. had (NLS) its basic region NES close to site indicating accessibility conformational changes. Increased levels unphosphorylated suppressed expression HSP90 transcription heat shock element (HSE). bound factor (HSTF) enhanced HSTF association with HSE. In addition, was present protein complex associates HSE, suggesting participates suppression transcription. decreased activities cells but not experiments vitro pure Fyn. Because essential for these results suggest modulates kinase activity regulating expression.