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Myosin S2 is not required for effects of myosin binding protein-C on motility.

作者信息

Shaffer Justin F, Razumova Maria V, Tu An-Yue, Regnier Michael, Harris Samantha P

机构信息

Department of Bioengineering, University of Washington, PO Box 355061, Seattle, WA 98195, United States.

出版信息

FEBS Lett. 2007 Apr 3;581(7):1501-4. doi: 10.1016/j.febslet.2007.03.007. Epub 2007 Mar 12.

Abstract

The unique myosin binding protein-c "motif" near the N-terminus of myosin binding protein-C (MyBP-C) binds myosin S2. Previous studies demonstrated that recombinant proteins containing the motif and flanking regions (e.g., C1C2) affect thin filament movement in motility assays using heavy meromyosin (S1 plus S2) as the molecular motor. To determine if S2 is required for these effects we investigated whether C1C2 affects motility in assays using only myosin S1 as the motor protein. Results demonstrate that effects of C1C2 are comparable in both systems and suggest that the MyBP-C motif affects motility through direct interactions with actin and/or myosin S1.

摘要

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