Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 41, Issue 12, Pages 989-997Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2016.09.006
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Funding
- NHLBI NIH HHS [P01 HL110869] Funding Source: Medline
- NIDCD NIH HHS [R01 DC009100] Funding Source: Medline
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How myosin interacts with actin to generate force is a subject of considerable controversy. The major debate centers on understanding at what point in force generation the inorganic phosphate is released with respect to the lever arm swing, or powerstroke. Resolving the controversy is essential for understanding how force is produced as well as the mechanisms underlying disease-causing mutations in myosin. Recent structural insights into the powerstroke have come from a high-resolution structure of myosin in a previously unseen state and from an electron cryomicroscopy (cryo-EM) 3D reconstruction of the actin-myosin-MgADP complex. Here, we argue that seemingly contradictory data from time-resolved fluorescence resonance energy transfer (FRET) studies can be reconciled, and we put forward a model for myosin force generation on actin.
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