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Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP

Author

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  • Hiroaki Miki

    (Institute of Medical Science, University of Tokyo)

  • Takuya Sasaki

    (Osaka University Medical School)

  • Yoshimi Takai

    (Osaka University Medical School)

  • Tadaomi Takenawa

    (Institute of Medical Science, University of Tokyo)

Abstract

Cdc42 is a small GTPase of the Rho family which regulates the formation of actin filaments to generate filopodia1,2. Although there are several proteins such as PAK3, ACK4 and WASP (Wiskott–Aldrich syndrome protein)5 that bind Cdc42 directly, none of these can account for the filopodium formation induced by Cdc42. Here we demonstrate that before it can induce filopodium formation, Cdc42 must bind a WASP-related protein, N-WASP, that is richest in neural tissues6 but is expressed ubiquitously. N-WASP induces extremely long actin microspikes only when co-expressed with active Cdc42, whereas WASP, which is expressed in haematopoietic cells, does not, despite the structural similarities between WASP and N-WASP. In a cell-free system, addition of active Cdc42 significantly stimulates the actin-depolymerizing activity of N-WASP, creating free barbed ends from which actin polymerization can then take place. This activation seems to be caused by exposure of N-WASP's actin-depolymerizing region induced by Cdc42 binding.

Suggested Citation

  • Hiroaki Miki & Takuya Sasaki & Yoshimi Takai & Tadaomi Takenawa, 1998. "Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP," Nature, Nature, vol. 391(6662), pages 93-96, January.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6662:d:10.1038_34208
    DOI: 10.1038/34208
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    Cited by:

    1. Norbert S. Hill & Matthew D. Welch, 2022. "A glycine-rich PE_PGRS protein governs mycobacterial actin-based motility," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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