Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle

PK Luther, H Winkler, K Taylor, ME Zoghbi, R Craig, R Padron, JM Squire, J Liu

Research output: Contribution to journalArticle (Academic Journal)peer-review

99 Citations (Scopus)

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.
Translated title of the contributionDirect visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle
Original languageEnglish
Pages (from-to)11423 - 11428
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume108
DOIs
Publication statusPublished - Jul 2011

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