ArticleJournal of molecular and cellular cardiology2013
Functional dissection of myosin binding protein C phosphorylation.
Article in Journal of molecular and cellular cardiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 21 citations in OpenAlex.
- Alterations in cardiac contractile and regulatory proteins contribute to age-related cardiac dysfunction in male rats.Physiological reports · 2024Article
- Retrospective Study of Intercalated Disk Defects Associated with Dilated Cardiomyopathy, Atrial Thrombosis, and Heart Failure in BALB/c Mice Deficient in IL4 Receptor α.Comparative medicine · 2020Article
- Phosphomimetic cardiac myosin-binding protein C partially rescues a cardiomyopathy phenotype in murine engineered heart tissue.Scientific reports · 2019Article
- Role of type 2A phosphatase regulatory subunit B56α in regulating cardiac responses to β-adrenergic stimulation in vivo.Cardiovascular research · 2019Article
- HIV-1 Nef-induced cardiotoxicity through dysregulation of autophagy.Scientific reports · 2017Article
- Sickle cell anemia mice develop a unique cardiomyopathy with restrictive physiology.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A post-MI power struggle: adaptations in cardiac power occur at the sarcomere level alongside MyBP-C and RLC phosphorylation.American journal of physiology. Heart and circulatory physiology · 2016Article
- Alterations in Multi-Scale Cardiac Architecture in Association With Phosphorylation of Myosin Binding Protein-C.Journal of the American Heart Association · 2016Article
- Should we treat heart failure with phosphatase inhibitors? Better to start at the end.Journal of molecular and cellular cardiology · 2015Article
- Cardiac MyBP-C regulates the rate and force of contraction in mammalian myocardium.Circulation research · 2015Review
- The contribution of cardiac myosin binding protein-c Ser282 phosphorylation to the rate of force generation and in vivo cardiac contractility.The Journal of physiology · 2014Article
- Myofilament dysfunction as an emerging mechanism of volume overload heart failure.Pflugers Archiv : European journal of physiology · 2014Review
- Phosphorylation of cMyBP-C affects contractile mechanisms in a site-specific manner.Biophysical journal · 2014Article
- Cardiac myosin-binding protein-C is a critical mediator of diastolic function.Pflugers Archiv : European journal of physiology · 2014Review
- Cardiac myosin binding protein-C: a novel sarcomeric target for gene therapy.Pflugers Archiv : European journal of physiology · 2014Article
- Post-translational control of cardiac hemodynamics through myosin binding protein C.Pflugers Archiv : European journal of physiology · 2014Review
- Cardiac myosin binding protein C phosphorylation affects cross-bridge cycle's elementary steps in a site-specific manner.PloS one · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Cardiac myosin binding protein C (cMyBP-C) phosphorylation is differentially regulated in the normal heart and during disease development. Our objective was to examine in detail three phosphorylatable sites (Ser-273, Ser-282, and Ser-302) present in the protein's cardiac-specific sequences, as these residues are differentially and reversibly phosphorylated during normal and abnormal cardiac function. Three transgenic lines were generated: DAA, which expressed cMyBP-C containing Asp-273, Ala-282, and Ala-302, in which a charged amino acid was placed at residue 273 and the remaining two sites rendered nonphosphorylatable by substituting alanines for the two serines; AAD containing Ala-273, Ala-282, and Asp-302, in which aspartate was placed at residue 302 and the remaining two sites rendered nonphosphorylatable; and SDS containing Ser-273, Asp-282, and Ser-302. These mice were compared to mice constructed previously along similar lines: wild type, in which normal cMyBP-C is transgenically expressed, AllP-, in which alanines were substituted and ADA mice as well. DAA and AAD mice showed pathology that was more severe than cMyBP-C nulls. DAA and AAD animals exhibited left ventricular chamber dilation, interstitial fibrosis, irregular cardiac rhythm and sudden cardiac death. Our results define the effects of the sites' post-translational modifications on cMyBP-C functionality and together, give a comprehensive picture of the potential consequences of site-specific phosphorylation. Ser-282 is a key residue in controlling S2 interaction with the thick and thin filaments. The new DAA and AAD constructs show that phosphorylation at one site in the absence of the ability to phosphorylate the other sites, depending upon the particular residues involved, can lead to severe cardiac remodeling and dysfunction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.