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The post-rigor structure of myosin VI and implications for the recovery stroke.

Ménétrey J, Llinas P, Cicolari J, Squires G, Liu X, Li A, Sweeney HL, Houdusse A
EMBO J 27 244-52 (2008)
Cited: 26 times
EuropePMC logo PMID: 18046460

Abstract

Myosin VI has an unexpectedly large swing of its lever arm (powerstroke) that optimizes its unique reverse direction movement. The basis for this is an unprecedented rearrangement of the subdomain to which the lever arm is attached, referred to as the converter. It is unclear at what point(s) in the myosin VI ATPase cycle rearrangements in the converter occur, and how this would effect lever arm position. We solved the structure of myosin VI with an ATP analogue (ADP.BeF3) bound in its nucleotide-binding pocket. The structure reveals that no rearrangement in the converter occur upon ATP binding. Based on previously solved myosin structures, our structure suggests that no reversal of the powerstroke occurs during detachment of myosin VI from actin. The structure also reveals novel features of the myosin VI motor that may be important in maintaining the converter conformation during detachment from actin, and other features that may promote rapid rearrangements in the structure following actin detachment that enable hydrolysis of ATP.

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Reviews citing this publication (3)

  1. SH3 domains: modules of protein-protein interactions. Kurochkina N, Guha U. Biophys Rev 5 29-39 (2013)
  2. Poorly understood aspects of striated muscle contraction. Månsson A, Rassier D, Tsiavaliaris G. Biomed Res Int 2015 245154 (2015)
  3. Keeping the focus on biophysics and actin filaments in Nagoya: A report of the 2016 "now in actin" symposium. Fujiwara I, Narita A. Cytoskeleton (Hoboken) 74 450-464 (2017)

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  6. Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity. Gurel PS, Kim LY, Ruijgrok PV, Omabegho T, Bryant Z, Alushin GM. Elife 6 e31125 (2017)
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  8. The myosin start-of-power stroke state and how actin binding drives the power stroke. Preller M, Holmes KC. Cytoskeleton (Hoboken) 70 651-660 (2013)
  9. Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines. Cochran JC. Biophys Rev 7 269-299 (2015)
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  11. A novel splice site mutation of myosin VI in mice leads to stereociliary fusion caused by disruption of actin networks in the apical region of inner ear hair cells. Seki Y, Miyasaka Y, Suzuki S, Wada K, Yasuda SP, Matsuoka K, Ohshiba Y, Endo K, Ishii R, Shitara H, Kitajiri SI, Nakagata N, Takebayashi H, Kikkawa Y. PLoS One 12 e0183477 (2017)
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  14. The structure of the actin-smooth muscle myosin motor domain complex in the rigor state. Banerjee C, Hu Z, Huang Z, Warrington JA, Taylor DW, Trybus KM, Lowey S, Taylor KA. J Struct Biol 200 325-333 (2017)
  15. Simultaneous observation of the lever arm and head explains myosin VI dual function. Ikezaki K, Komori T, Sugawa M, Arai Y, Nishikawa S, Iwane AH, Yanagida T. Small 8 3035-3040 (2012)
  16. Reverse conformational changes of the light chain-binding domain of myosin V and VI processive motor heads during and after hydrolysis of ATP by small-angle X-ray solution scattering. Sugimoto Y, Sato O, Watanabe S, Ikebe R, Ikebe M, Wakabayashi K. J Mol Biol 392 420-435 (2009)
  17. Spontaneous detachment of the leading head contributes to myosin VI backward steps. Ikezaki K, Komori T, Yanagida T. PLoS One 8 e58912 (2013)


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