ArticleBiochemistry2007
PKCepsilon increases phosphorylation of the cardiac myosin binding protein C at serine 302 both in vitro and in vivo.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Myocardium From Patients With ATTR Amyloidosis Produces Less Force Secondary to Increased Fibrosis.JACC. Basic to translational science · 2025Article
- Site-specific phosphorylation of myosin binding protein-C coordinates thin and thick filament activation in cardiac muscle.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Biophysical reviews · 2018Review
- Cardiac myosin binding protein-C SerScience advances · 2017Article
- Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Alterations in Multi-Scale Cardiac Architecture in Association With Phosphorylation of Myosin Binding Protein-C.Journal of the American Heart Association · 2016Article
- Phosphorylation of cardiac Myosin-binding protein-C is a critical mediator of diastolic function.Circulation. Heart failure · 2015Article
- Cardiac MyBP-C regulates the rate and force of contraction in mammalian myocardium.Circulation research · 2015Review
- Cardiac myosin binding protein-C as a central target of cardiac sarcomere signaling: a special mini review series.Pflugers Archiv : European journal of physiology · 2014Review
- Agonist activated PKCβII translocation and modulation of cardiac myocyte contractile function.Scientific reports · 2013Article
- Cardiac myosin binding protein-C: redefining its structure and function.Biophysical reviews · 2012Article
- cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance.Journal of muscle research and cell motility · 2012Review
- Article
- Myosin binding protein-C slow is a novel substrate for protein kinase A (PKA) and C (PKC) in skeletal muscle.Journal of proteome research · 2011Article
- The role of protein kinase C-mediated phosphorylation of sarcomeric proteins in the heart-detrimental or beneficial?Biophysical reviews · 2011Review
- Redox signaling and cardiac sarcomeres.The Journal of biological chemistry · 2011Review
- Receptor-independent cardiac protein kinase Calpha activation by calpain-mediated truncation of regulatory domains.Circulation research · 2010Article
- Stage-specific changes in myofilament protein phosphorylation following myocardial infarction in mice.Journal of molecular and cellular cardiology · 2010Article
- Phosphorylation and function of cardiac myosin binding protein-C in health and disease.Journal of molecular and cellular cardiology · 2010Review
- Protein kinase C alpha and epsilon phosphorylation of troponin and myosin binding protein C reduce Ca2+ sensitivity in human myocardium.Basic research in cardiology · 2010Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cardiac myosin binding protein C (cMyBPC) phosphorylation is essential for normal cardiac function. Although PKC was reported to phosphorylate cMyBPC in vitro, the relevant PKC isoforms and functions of PKC-mediated cMyBPC phosphorylation are unknown. We recently reported that a transgenic mouse model with cardiac-specific overexpression of PKCepsilon (PKCepsilon TG) displayed enhanced sarcomeric protein phosphorylation and dilated cardiomyopathy. In the present study, we have investigated cMyBPC phosphorylation in PKCepsilon TG mice. Western blotting and two-dimensional gel electrophoresis demonstrated a significant increase in cMyBPC serine (Ser) phosphorylation in 12-month-old TG mice compared to wild type (WT). In vitro PKCepsilon treatment of myofibrils increased the level of cMyBPC Ser phosphorylation in WT mice to that in TG mice, whereas treatment of TG myofibrils with PKCepsilon showed only a minimal increase in cMyBPC Ser phosphorylation. Three peptide motifs of cMyBPC were identified as the potential PKCepsilon consensus sites including a 100% matched motif at Ser302 and two nearly matched motifs at Ser811 and Ser1203. We treated synthetic peptides corresponding to the sequences of these three motifs with PKCepsilon and determined phosphorylation by mass spectrometry and ELISA assay. PKCepsilon induced phosphorylation at the Ser302 site but not at the Ser811 or Ser1203 sites. A S302A point mutation in the Ser302 peptide abolished the PKCepsilon-dependent phosphorylation. Taken together, our data show that the Ser302 on mouse cMyBPC is a likely PKCepsilon phosphorylation site both in vivo and in vitro and may contribute to the dilated cardiomyopathy associated with increased PKCepsilon activity.
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