Myosin binding protein-C: Enigmatic regulator of cardiac contraction

Cecily E. Oakley, Jean Chamoun, Louise J. Brown, Brett D. Hambly*

*Corresponding author for this work

    Research output: Contribution to journalShort surveypeer-review

    48 Citations (Scopus)

    Abstract

    Myosin binding protein C (MyBPC) is a sarcomeric protein whose role in sarcomere structure and regulation of contraction is currently under investigation. It is a member of the immunoglobulin superfamily and is found in the C-zone of the A-band of the sarcomere. The elongated structure of MyBPC is composed of a series of immunoglobulin and fibronectin domains, with the C-terminal domains binding to the myosin thick filament and the N-terminal domains interacting with the myosin subfragment-2 (S2) neck region and possibly the actin thin filament. The functions of MyBPC are to stabilise the sarcomere structure and to regulate contraction. When phosphorylated near its N-terminus, MyBPC no longer binds myosin-S2, causing an increase in the ordering of the myosin heads, ATPase activity, Fmax and Ca2+ sensitivity of contraction. Mutations in MyBPC have been found to cause familial hypertrophic cardiomyopathy (FHC) and changes in MyBPC phosphorylation have been linked to cardiac ischaemia-reperfusion injury.

    Original languageEnglish
    Pages (from-to)2161-2166
    Number of pages6
    JournalInternational Journal of Biochemistry and Cell Biology
    Volume39
    Issue number12
    DOIs
    Publication statusPublished - 2007

    Fingerprint

    Dive into the research topics of 'Myosin binding protein-C: Enigmatic regulator of cardiac contraction'. Together they form a unique fingerprint.

    Cite this