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Drosophila Spire is an actin nucleation factor

Author

Listed:
  • Margot E. Quinlan

    (UCSF Medical School)

  • John E. Heuser

    (Washington University)

  • Eugen Kerkhoff

    (Universität Würzburg)

  • R. Dyche Mullins

    (UCSF Medical School)

Abstract

The actin cytoskeleton is essential for many cellular functions including shape determination, intracellular transport and locomotion. Previous work has identified two factors—the Arp2/3 complex and the formin family of proteins—that nucleate new actin filaments via different mechanisms. Here we show that the Drosophila protein Spire represents a third class of actin nucleation factor. In vitro, Spire nucleates new filaments at a rate that is similar to that of the formin family of proteins but slower than in the activated Arp2/3 complex, and it remains associated with the slow-growing pointed end of the new filament. Spire contains a cluster of four WASP homology 2 (WH2) domains, each of which binds an actin monomer. Maximal nucleation activity requires all four WH2 domains along with an additional actin-binding motif, conserved among Spire proteins. Spire itself is conserved among metazoans and, together with the formin Cappuccino, is required for axis specification in oocytes and embryos, suggesting that multiple actin nucleation factors collaborate to construct essential cytoskeletal structures.

Suggested Citation

  • Margot E. Quinlan & John E. Heuser & Eugen Kerkhoff & R. Dyche Mullins, 2005. "Drosophila Spire is an actin nucleation factor," Nature, Nature, vol. 433(7024), pages 382-388, January.
    • Handle: RePEc:nat:nature:v:433:y:2005:i:7024:d:10.1038_nature03241
    DOI: 10.1038/nature03241
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    Cited by:

    1. Noura Alzahofi & Tobias Welz & Christopher L. Robinson & Emma L. Page & Deborah A. Briggs & Amy K. Stainthorp & James Reekes & David A. Elbe & Felix Straub & Wouter W. Kallemeijn & Edward W. Tate & Ph, 2020. "Rab27a co-ordinates actin-dependent transport by controlling organelle-associated motors and track assembly proteins," Nature Communications, Nature, vol. 11(1), pages 1-21, December.

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