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¹ Department of Biochemistry, Institute of Medical Science, University of Tokyo, Tokyo 108-8539, Japan; 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8539, Japan
² PRESTO, Japan Science and Technology Corporation (JST), Institute of Molecular and Cellular Biosciences, University of Tokyo, Tokyo, Japan
³ Fine Morphology Laboratory, Department of Basic Medical Science, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8539, Japan

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.

^* Correspondence: E-mail: takenawa{at}ims.u-tokyo.ac.jp

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