Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle
AuthorsLuther, Pradeep K.
Zoghbi, Maria E.
Craig, Roger W.
Squire, John M.
UMass Chan AffiliationsDepartment of Cell Biology
Electron Microscope Tomography
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AbstractMyosin-binding protein C (MyBP-C) is a thick filament protein playing an essential role in muscle contraction, and MyBP-C mutations cause heart and skeletal muscle disease in millions worldwide. Despite its discovery 40 y ago, the mechanism of MyBP-C function remains unknown. In vitro studies suggest that MyBP-C could regulate contraction in a unique way--by bridging thick and thin filaments--but there has been no evidence for this in vivo. Here we use electron tomography of exceptionally well preserved muscle to demonstrate that MyBP-C does indeed bind to actin in intact muscle. This binding implies a physical mechanism for communicating the relative sliding between thick and thin filaments that does not involve myosin and which could modulate the contractile process.
SourceProc Natl Acad Sci U S A. 2011 Jul 12;108(28):11423-8. Epub 2011 Jun 24. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/27670
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