Craig Lab Publications

UMMS Affiliation

Department of Cell Biology

Publication Date


Document Type



Actins; Animals; Biophysical Phenomena; Carrier Proteins; Electron Microscope Tomography; Freeze Substitution; Humans; Imaging, Three-Dimensional; Models, Molecular; Muscle, Skeletal; Myosins; Ranidae


Cell Biology


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

Publisher PDF posted as allowed by the publisher's author rights policy at

DOI of Published Version



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

Journal/Book/Conference Title

Proceedings of the National Academy of Sciences of the United States of America

Related Resources

Link to Article in PubMed

PubMed ID


Included in

Cell Biology Commons