Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly

Dennis Zimmermann; Kaitlin E. Homa; Glen M. Hocky; Luther W. Pollard; Enrique M. De La Cruz; Gregory A. Voth; Kathleen M. Trybus; David R. Kovar

doi:10.1038/s41467-017-00445-3

Nature Communications (Sep 2017)

Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly

Dennis Zimmermann,
Kaitlin E. Homa,
Glen M. Hocky,
Luther W. Pollard,
Enrique M. De La Cruz,
Gregory A. Voth,
Kathleen M. Trybus,
David R. Kovar

Affiliations

Dennis Zimmermann: Department of Molecular Genetics and Cell Biology, The University of Chicago
Kaitlin E. Homa: Department of Molecular Genetics and Cell Biology, The University of Chicago
Glen M. Hocky: Department of Chemistry, The James Franck Institute and Institute for Biophysical Dynamics and Computation Institute, The University of Chicago
Luther W. Pollard: Department of Molecular Physiology and Biophysics, University of Vermont
Enrique M. De La Cruz: Department of Molecular Biophysics and Biochemistry, Yale University
Gregory A. Voth: Department of Chemistry, The James Franck Institute and Institute for Biophysical Dynamics and Computation Institute, The University of Chicago
Kathleen M. Trybus: Department of Molecular Physiology and Biophysics, University of Vermont
David R. Kovar: Department of Molecular Genetics and Cell Biology, The University of Chicago

DOI: https://doi.org/10.1038/s41467-017-00445-3
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 13

Abstract

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The fission yeast cytokinetic ring assembles by Search-Capture-Pull-Release from precursor nodes that include formin Cdc12 and myosin Myo2. The authors reconstitute Search-Capture-Pull in vitro and find that Myo2 pulling on Cdc12-associated actin filaments mechano-inhibits Cdc12-mediated assembly, which enables proper ring assembly in vivo.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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