Modulation of striated muscle contraction by binding of myosin binding protein C to actin
UMass Chan Affiliations
Department of Cell BiologyDocument Type
Journal ArticlePublication Date
2011-11-01
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Myosin binding protein C (MyBP-C or C-protein) is a protein of the thick (myosin-containing) filaments of striated muscle thought to be involved in the modulation of cardiac contraction in response to beta-adrenergic stimulation. The mechanism of this modulation is unknown, but one possibility is through transient binding of the N-terminal end of MyBP-C to the thin (actin-containing) filaments. While such binding has been demonstrated in vitro, it was not known until recently whether such a link between thick and thin filaments also occurred in vivo. Here we review a recent paper in which electron microscopy (EM) is used to directly demonstrate MyBP-C links between myosin and actin filaments in the intact sarcomere, suggesting a possible physical mechanism for modulating filament sliding. Molecular details of MyBP-C binding to actin have recently been elucidated by EM of isolated filaments: the results suggest that MyBP-C might contribute to the modulation of contraction in part by competing with tropomyosin for binding sites on actin. New results on the structure and dynamics of the MyBP-C molecule provide additional insights into the function of this enigmatic molecule.Source
Bioarchitecture. 2011 Nov 1;1(6):277-283. Link to article on publisher's siteDOI
10.4161/bioa.1.6.19341Permanent Link to this Item
http://hdl.handle.net/20.500.14038/27666PubMed ID
22545180Related Resources
Link to Article in PubMedRights
This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
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10.4161/bioa.1.6.19341