热休克蛋白90（HSP90）交联由N-WASP和肌动蛋白相关蛋白2/3复合物（Arp2/3 complex）诱导形成的分支状肌动蛋白丝。
HSP90 cross-links branched actin filaments induced by N-WASP and the Arp2/3 complex.
作者信息
Park Sun Joo, Suetsugu Shiro, Sagara Hiroshi, Takenawa Tadaomi
机构信息
Department of Biochemistry, Institute of Medical Science, University of Tokyo, Tokyo 108-8539, Japan; 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8539, Japan.
出版信息
Genes Cells. 2007 May;12(5):611-22. doi: 10.1111/j.1365-2443.2007.01081.x.
N-WASP induces filopodial actin cytoskeleton through activation of the Arp2/3 complex. Here, we show that heat shock protein 90 (HSP90) regulates the structure of actin filaments induced by N-WASP and the Arp2/3 complex. HSP90 binds to N-WASP and to F-actin and bundles actin filaments. Bundling activity of HSP90 does not affect actin filament nucleation induced by N-WASP and the Arp2/3 complex. HSP90 is co-localized with N-WASP at branching points of actin filaments produced by the Arp2/3 complex and thereby bundles branched filaments; this bundled actin structure is inhibited by blocking direct binding between HSP90 and N-WASP. Furthermore, HSP90 converts branched actin filaments on N-WASP-coated beads to filopodia-like star-shaped bundles. These findings indicate that HSP90 promotes the formation of N-WASP/Arp2/3 complex-induced unbranched filopodial actin structures.
N-WASP通过激活Arp2/3复合物诱导丝状伪足肌动蛋白细胞骨架的形成。在此，我们表明热休克蛋白90（HSP90）调节由N-WASP和Arp2/3复合物诱导的肌动蛋白丝结构。HSP90与N-WASP以及F-肌动蛋白结合，并使肌动蛋白丝成束。HSP90的成束活性不影响由N-WASP和Arp2/3复合物诱导的肌动蛋白丝成核。HSP90与N-WASP在由Arp2/3复合物产生的肌动蛋白丝分支点处共定位，从而使分支丝成束；这种成束的肌动蛋白结构可通过阻断HSP90与N-WASP之间的直接结合而受到抑制。此外，HSP90将N-WASP包被珠上的分支肌动蛋白丝转化为丝状伪足样星形束。这些发现表明，HSP90促进N-WASP/Arp2/3复合物诱导的无分支丝状伪足肌动蛋白结构的形成。
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