UMMS Affiliation
Department of Cell Biology
Date
7-12-2011
Document Type
Article
Medical Subject Headings
Actins; Animals; Biophysical Phenomena; Carrier Proteins; Electron Microscope Tomography; Freeze Substitution; Humans; Imaging, Three-Dimensional; Models, Molecular; Muscle, Skeletal; Myosins; Ranidae
Disciplines
Cell Biology
Abstract
Myosin-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.
Rights and Permissions
Citation: Proc Natl Acad Sci U S A. 2011 Jul 12;108(28):11423-8. Epub 2011 Jun 24. Link to article on publisher's site
Comments
Publisher PDF posted as allowed by the publisher's author rights policy at http://www.pnas.org/site/misc/authorfaq.shtml.