How Myosin Generates Force on Actin Filaments

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• 作者：Anne Houdusse¹ ; ² ; ^{anne.houdusse@curie.fr" class="auth_mail" title="E-mail the corresponding author} ; H. Lee Sweeney³ ; ^{Lsweeney@ufl.edu" class="auth_mail" title="E-mail the corresponding author}
• 关键词：molecular motors ; allostery ; force generation ; chemo-mechanical transduction
• 刊名：Trends in Biochemical Sciences
• 出版年：2016
• 出版时间：December 2016
• 年：2016
• 卷：41
• 期：12
• 页码：989-997
• 全文大小：2001 K

文摘

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.