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| Title | Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle. |
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| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 108, Issue 28, Page 11423-11428, Year 2011 |
| Publish date | Jul 12, 2011 |
 Authors | Pradeep K Luther / Hanspeter Winkler / Kenneth Taylor / Maria E Zoghbi / Roger Craig / Raúl Padrón / John M Squire / Jun Liu /  |
| PubMed 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. ...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. |
 External links | Proc Natl Acad Sci U S A / PubMed:21705660 / PubMed Central |
| Methods | EM (subtomogram averaging) |
| Resolution | 70.0 Å |
| Structure data |  EMDB-1909: |
| Source |
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