The Troponin C G159D Mutation Blunts Myofilament Desensitization Induced by Troponin I Ser23/24 Phosphorylation

• Published in: Circulation research Vol. 100; no. 10; pp. 1486 - 1493
• Main Authors: Biesiadecki, Brandon J, Kobayashi, Tomoyoshi, Walker, John S, Solaro, R John, de Tombe, Pieter P
• Format: Journal Article
• Language: English
• Published: Hagerstown, MD American Heart Association, Inc 25.05.2007; Lippincott
• Subjects: Actin Cytoskeleton - physiology; Biological and medical sciences; Calcium - metabolism; Cardiology. Vascular system; Cardiomyopathies - etiology; Cyclic AMP-Dependent Protein Kinases - physiology; Fundamental and applied biological sciences. Psychology; Heart; Humans; Medical sciences; Mutation; Myocarditis. Cardiomyopathies; Phosphorylation; Receptors, Adrenergic, beta - physiology; Serine; Troponin C - genetics; Troponin I - metabolism; Vertebrates: cardiovascular system; Human; tension cost; Phosphorylation; Desensitization; Rat; Cardiomyopathy; Rodentia; Cardiovascular disease; Striated muscle; Myocardial disease; Vertebrata; Troponin; cross-bridge cycling; Mammalia; Heart disease; skinned muscle; Circulatory system; Mutation

Striated muscle contraction is regulated by the binding of Ca to the N-terminal regulatory lobe of the cardiac troponin C (cTnC) subunit in the troponin complex. In the heart, β-adrenergic stimulation induces protein kinase A phosphorylation of cardiac troponin I (cTnI) at Ser23/24 to alter the inte...