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A gelsolin-like Ca2+-dependent actin-binding domain in villin

Nature volume 315, pages 248–250 (1985)Cite this article

Abstract

Villin is an actin-binding protein of relative molecular mass (Mr) 95,000 found in the core bundle of microfilaments in brush border microvilli from intestine1–3. In physiological calcium concentrations (<1 µM), villin crosslinks actin filaments into bundles. However, in free calcium concentrations (>1 µM), villin severs actin filaments into short pieces3–5. To understand how villin can sever and bundle actin filaments, we are studying the molecular basis of villin–actin binding interactions by identifying important actin-binding domains in villin. Here, we report the purification and preliminary characterization of a 44,000-Mr fragment of villin which contains a calcium-dependent actin-severing activity. In addition, the partial amino-acid sequence from the amino terminus of this fragment reveals homology with a 16-residue region near the amino terminus6 of gelsolin, an actin-severing protein found in many cells7–9 and sera10–12. The sequence homology suggests a common structural basis for the calcium-regulated actin-severing properties shared by villin and gelsolin.

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Author notes

  1. Paul Matsudaira

    Present address: Whitehead Institute for Biomedical Research and Department of Biology, MIT, Nine Cambridge Center, Cambridge, Massachusetts, 02142, USA

Authors and Affiliations

  1. Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Paul Matsudaira, Ross Jakes & John E. Walker

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  1. Paul Matsudaira
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  2. Ross Jakes
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Matsudaira, P., Jakes, R. & Walker, J. A gelsolin-like Ca2+-dependent actin-binding domain in villin. Nature 315, 248–250 (1985). https://doi.org/10.1038/315248a0

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