Myosin II contributes to cell-scale actin network treadmilling through network disassembly

Cyrus A. Wilson, Mark A. Tsuchida, Greg M. Allen, Erin L. Barnhart, Kathryn T. Applegate, Patricia T. Yam, Lin Ji, Kinneret Keren, Gaudenz Danuser and Julie A. Theriot ()
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Cyrus A. Wilson: Stanford University School of Medicine, Stanford, California 94305, USA
Mark A. Tsuchida: Stanford University School of Medicine, Stanford, California 94305, USA
Greg M. Allen: Stanford University School of Medicine, Stanford, California 94305, USA
Erin L. Barnhart: Stanford University School of Medicine, Stanford, California 94305, USA
Kathryn T. Applegate: The Scripps Research Institute, La Jolla, California 92037, USA
Patricia T. Yam: Stanford University School of Medicine, Stanford, California 94305, USA
Lin Ji: The Scripps Research Institute, La Jolla, California 92037, USA
Kinneret Keren: Stanford University School of Medicine, Stanford, California 94305, USA
Gaudenz Danuser: The Scripps Research Institute, La Jolla, California 92037, USA
Julie A. Theriot: Stanford University School of Medicine, Stanford, California 94305, USA

Nature, 2010, vol. 465, issue 7296, 373-377

Abstract: Myosin II in cell motility In animals, most cells when on the move migrate using a crawling motion, in which the front of the cell is propelled forward by the force provided by polymerization of actin filaments. Cell biologists have generally assumed that the rear of the crawling cell is then pushed forward by a contractile force generated by non-muscle myosin II. Observations of fish keratocytes in motion now show that no actual contraction is required for rear retraction. Rather, the myosin II has a direct role in facilitating actin network treadmilling via actin disassembly.

Date: 2010
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DOI: 10.1038/nature08994

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