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Actin nucleation: bacteria get in-Spired

Nature Cell Biology volume 10, pages 13–15 (2008)Cite this article

Spir proteins nucleate actin polymerization by assembling a linear actin oligomer along a cluster of four actin-binding WH2 domains, and this process is enhanced by formins of the Cappuccino family. The discovery of Spir-like proteins in bacteria indicates that pathogens have adopted this mechanism to manipulate the host actin cytoskeleton.

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Figure 1: Model of Spir and Cappuccino cooperation in actin nucleation/polymerization.
Figure 2: Comparison of WH2-based nucleators and formin structures.

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Authors and Affiliations

  1. Margot E. Quinlan is at the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, N314 Genentech Hall, 600 16th Street, San Francisco CA 94107,

    Margot E. Quinlan

  2. Bayerisches Genomforschungsnetzwerk (BayGene), Institut für funktionelle Genomik, Universität Regensburg, Franz-Josef-Strauß-Allee 11, Regensburg, 93053, Germany

    Eugen Kerkhoff

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  1. Margot E. Quinlan
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  2. Eugen Kerkhoff
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Quinlan, M., Kerkhoff, E. Actin nucleation: bacteria get in-Spired. Nat Cell Biol 10, 13–15 (2008). https://doi.org/10.1038/ncb0108-13

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