Cardiac myosin binding protein C and its phosphorylation regulate multiple steps in the cross-bridge cycle of muscle contraction.

No abstract is available for this paper.

• Publication year

  2012

• Venue

  Biochemistry

• Publication date

  2012-04-06

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1021/bi300085xPMID 22458937PMCID PMC5598764
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Unique single molecule binding of cardiac myosin binding protein-C to actin and phosphorylation-dependent inhibition of actomyosin motility requires 17 amino acids of the motif domain.

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• Electron microscopy and 3D reconstruction of F-actin decorated with cardiac myosin-binding protein C (cMyBP-C).

  2011cited by this paper
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• Cardiac Myosin Activation: A Potential Therapeutic Approach for Systolic Heart Failure

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• Protein kinase A changes calcium sensitivity but not crossbridge kinetics in human cardiac myofibrils.

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• The N-terminal domains of myosin binding protein C can bind polymorphically to F-actin.

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• Myosin Binding Protein C Interaction with Actin

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• Phosphorylation and function of cardiac myosin binding protein-C in health and disease.

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• The Myosin-binding Protein C Motif Binds to F-actin in a Phosphorylation-sensitive Manner*

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• Kinetic and equilibrium analysis of the myosin ATPase.

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• Protein Kinase A-Mediated Phosphorylation of cMyBP-C Increases Proximity of Myosin Heads to Actin in Resting Myocardium

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• Cardiac myosin binding protein-C modulates actomyosin binding and kinetics in the in vitro motility assay.

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• Multiplex Kinase Signaling Modifies Cardiac Function at the Level of Sarcomeric Proteins*

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• Acceleration of Crossbridge Kinetics by Protein Kinase A Phosphorylation of Cardiac Myosin Binding Protein C Modulates Cardiac Function

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• Control of In Vivo Contraction/Relaxation Kinetics by Myosin Binding Protein C: Protein Kinase A Phosphorylation–Dependent and –Independent Regulation

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• Ablation of Cardiac Myosin-Binding Protein-C Accelerates Stretch Activation in Murine Skinned Myocardium

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• Activation of Myocardial Contraction by the N-Terminal Domains of Myosin Binding Protein-C

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• Effects of the N-terminal Domains of Myosin Binding Protein-C in an in Vitro Motility Assay

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• Ablation of myosin-binding protein-C accelerates force development in mouse myocardium.

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• Role of Cardiac Myosin Binding Protein C in Sustaining Left Ventricular Systolic Stiffening

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• Hypertrophic Cardiomyopathy in Cardiac Myosin Binding Protein-C Knockout Mice

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• A role for C‐protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes

  2000cited by this paper
• Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2.

  2000cited by this paper
• Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain.

  1998cited by this paper
• Steric-model for activation of muscle thin filaments.

  1997cited by this paper
• A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy.

  1996cited by this paper
• The Regulatory Light Chains of Myosin Modulate Cross-bridge Cycling in Skeletal Muscle (*)

  1996cited by this paper
• The Role of the Four Ca Binding Sites of Troponin C in the Regulation of Skeletal Muscle Contraction (*)

  1996cited by this paper
• Strain-dependent cross-bridge cycle for muscle.

  1995cited by this paper
• The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif

  1993cited by this paper
• Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament.

  1993cited by this paper
• C‐protein limits shortening velocity of rabbit skeletal muscle fibres at low levels of Ca2+ activation.

  1991cited by this paper
• Alterations in Ca2+ sensitive tension due to partial extraction of C- protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers

  1991cited by this paper
• Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin‐filament activation.

  1986cited by this paper
• Structure of C protein purified from cardiac muscle

  1985cited by this paper
• The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin.

  1985cited by this paper
• Kinetics of acto-S1 interaction as a guide to a model for the crossbridge cycle

  1984cited by this paper
• Effects of cholinergic and adrenergic agonists on phosphorylation of a 165,000-dalton myofibrillar protein in intact cardiac muscle.

  1982cited by this paper
• Sarcomere length‐tension relations of frog skinned muscle fibres at lengths above the optimum.

  1980cited by this paper
• The interaction of C-protein with heavy meromyosin and subfragment-2.

  1978cited by this paper
• The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1.

  1978cited by this paper
• Axial arrangement of crossbridges in thick filaments of vertebrate skeletal muscle.

  1976cited by this paper
• Energetics and mechanism of actomyosin adenosine triphosphatase.

  1976cited by this paper
• Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin

  1975cited by this paper
• Calcium regulation of muscle contraction.

  1975cited by this paper
• The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.

  1971cited by this paper
• Native tropomyosin: effect on the interaction of actin with heavy meromyosin and subfragment-1.

  1970cited by this paper
• Kinetic and Equilibrium Analysis of the Myosin Atpase

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