PerspectiveCell Biology

Heart Brakes

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Science  07 Sep 2012:
Vol. 337, Issue 6099, pp. 1182-1183
DOI: 10.1126/science.1227943

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Many of us are keenly aware of muscle diseases because they frequently impact our lives. Heart failure, for example, is a leading cause of death, and its hereditary link has focused research efforts on sequencing the genes encoding muscle proteins (1). Several muscle proteins are implicated in heart disease, most notably the abundant motor protein myosin, and the relatively scarce structural protein myosin binding protein C (MyBP-C). Myosin generates the force for heart muscle contraction, but a heart will pump without MyBP-C, and its role in contraction and disease was unknown. In addition, mutations in MyBP-C cause late onset of heart failure, obscuring the link between protein malfunction and disease mechanism (2). These challenges have defied a bottom-up approach to characterize isolated MyBP-C's function in vitro, but the heart is too complex for top-down whole-muscle characterization (3). New research by Previs et al. (4) on page 1215 in this issue takes the middle road, using a concise experimental system that preserves relevant tissue structure while allowing the observation of single-particle dynamics to pinpoint MyBP-C's role in muscle contraction.