title: Molecular modulation of actomyosin function by cardiac myosin-binding protein C.
abstract: Cardiac myosin-binding protein C is a key regulator of cardiac contractility and is capable of both activating the thin filament to initiate actomyosin motion generation and governing maximal sliding velocities. While MyBP-C's C terminus localizes the molecule within the sarcomere, the N terminus appears to confer regulatory function by binding to the myosin motor domain and/or actin. Literature pertaining to how MyBP-C binding to the myosin motor domain and or actin leads to MyBP-C's dual modulatory roles that can impact actomyosin interactions are discussed.
authors.affiliation: Department of Molecular Physiology & Biophysics, University of Vermont, 149 Beaumont Ave., HSRF Building Rm.-116, Burlington, VT, 05405, USA.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Previs
authors.forename: Arthur J
authors.initials: AJ
authors.lastname: Michalek
authors.forename: David M
authors.initials: DM
authors.lastname: Warshaw
mesh_terms: D000205:Actomyosin / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D009200:Myocardial Contraction; D012518:Sarcomeres / Q000378:metabolism* / Q000502:physiology; D000099163:Myosin Binding Protein C
chemical_list: D000205:Actomyosin; D002352:Carrier Proteins; D000099163:Myosin Binding Protein C