Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 35, Issue 12, Pages 684-690Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2010.07.012
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Funding
- European Research Council (European Community) [FP7/2007-2013, 208319]
- European Union
- European Social Fund [TAMOP-4.2.1./B-09/ 1/KMR]
- Fogarty International Center
- National Heart, Lung and Blood Institute [1 R01TW007241]
- Hungarian Scientific Research Fund (OTKA) [K71915, NNF78783]
- European Research Council (ERC) [208319] Funding Source: European Research Council (ERC)
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Actomyosin powers muscle contraction and various cellular activities, including cell division, differentiation, intracellular transport and sensory functions. Despite their crucial roles, key aspects of force generation have remained elusive. To perform efficient force generation, the powerstroke must occur while myosin is bound to actin. Paradoxically, this process must be initiated when myosin is in a very low actin-affinity state. Recent results shed light on a kinetic pathway selection mechanism whereby the actin-induced activation of the swing of myosin's lever enables efficient mechanical functioning. Structural elements and biochemical principles involved in this mechanism are conserved among various NTPase-effector (e.g. kinesin-microtubule, G protein exchange factor and kinase-scaffold protein) systems that perform chemomechanical or signal transduction.
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