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The E525K mutation in M2\u03b2 is associated with dilated cardiomyopathy (DCM) and was found to stabilize the interacting heads motif (IHM) and autoinhibited super-relaxed (SRX) state in dimeric heavy meromyosin. However, in monomeric M2\u03b2 subfragment 1 (S1) we found that E525K enhances (threefold) the maximum steady-state actin-activated ATPase activity (kcat) and decreases (eightfold) the actin concentration at which ATPase is one-half maximal (KATPase). We also found a twofold to fourfold increase in the actin-activated power stroke and phosphate release rate constants at 30 \u03bcM actin, which overall enhanced the duty ratio threefold. Loaded motility assays revealed that the enhanced intrinsic motor activity translates to increased ensemble force in M2\u03b2 S1. Glutamate 525, located near the actin binding region in the so-called activation loop, is highly conserved and predicted to form a salt bridge with another conserved residue (lysine 484) in the relay helix. Enhanced sampling molecular dynamics simulations predict that the charge reversal mutation disrupts the E525-K484 salt bridge, inducing conformations with a more flexible relay helix and a wide phosphate release tunnel. Our results highlight a highly conserved allosteric pathway associated with actin activation of the power stroke and phosphate release and suggest an important feature of the autoinhibited IHM is to prevent this region of myosin from interacting with actin. The ability of the E525K mutation to stabilize the IHM likely overrides the enhanced intrinsic motor properties, which may be key to triggering DCM pathogenesis.<\/jats:p>","DOI":"10.1093\/pnasnexus\/pgae279","type":"journal-article","created":{"date-parts":[[2024,7,16]],"date-time":"2024-07-16T03:10:14Z","timestamp":1721099414000},"source":"Crossref","is-referenced-by-count":11,"title":["Dilated cardiomyopathy mutation in beta-cardiac myosin enhances actin activation of the power stroke and phosphate release"],"prefix":"10.1093","volume":"3","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5794-6927","authenticated-orcid":false,"given":"Skylar M L","family":"Bodt","sequence":"first","affiliation":[{"name":"Department of Cellular and Molecular Physiology, Pennsylvania State University College of Medicine , 500 University Dr, Hershey, PA 17033 , 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