Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2012-04-20

AUTHORS

Mark Pfuhl, Mathias Gautel

ABSTRACT

The thick filament protein myosin-binding protein-C shows a highly modular architecture, with the C-terminal region responsible for tethering to the myosin and titin backbone of the thick filament. The N-terminal region shows the most significant differences between cardiac and skeletal muscle isogenes: an entire Ig-domain (C0) is added, together with highly regulated phosphorylation sites between Ig domains C1 and C2. These structural and functional differences at the N-terminus reflect important functions in cardiac muscle regulation in health and disease. Alternative interactions of this part of MyBP-C with the head–tail (S1–S2) junction of myosin or to actin filaments have been proposed, but with conflicting experimental evidence. The regulation of myosin or actin interaction by phosphorylation of the cardiac MyBP-C N-terminus may play an additional role in length-dependent contraction regulation. We discuss here the evidence for these proposed interactions, considering the required properties of MyBP-C, the way in which they may be regulated in muscle contraction and the way they might be related to heart disease. We also attempt to shed some light on experimental pitfalls and future strategies. More... »

PAGES

83-94

References to SciGraph publications

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  • 2011-12-16. Myosin binding protein C: implications for signal-transduction in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
  • 2012-03-14. Axial distribution of myosin binding protein-C is unaffected by mutations in human cardiac and skeletal muscle in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
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  • 2006-02-23. The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins in CELLULAR AND MOLECULAR LIFE SCIENCES
  • 2009-01-08. Restoration of potato virus X coat protein capacity for assembly with RNA after His-tag removal in ARCHIVES OF VIROLOGY
  • 1999-10. The interface between MyBP-C and myosin: site-directed mutagenesis of the CX myosin-binding domain of MyBP-C in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
  • 2011-11-17. cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
  • 1997-07. A survey of in situ sarcomere extension in mouse skeletal muscle in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
  • 2005-08. Atomic model of a myosin filament in the relaxed state in NATURE
  • 2011-05-10. Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C in BMC MOLECULAR AND CELL BIOLOGY
  • 2011-11-30. Cardiac myosin binding protein C phosphorylation in cardiac disease in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
  • 1986-12. The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
  • 2011-11-05. How do MYBPC3 mutations cause hypertrophic cardiomyopathy? in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
  • 2011-11-11. Adrenergic stress reveals septal hypertrophy and proteasome impairment in heterozygous Mybpc3-targeted knock-in mice in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s10974-012-9291-z

    DOI

    http://dx.doi.org/10.1007/s10974-012-9291-z

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1019621013

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/22527637


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