Literature DB >> 20094053

Myosin VI: an innovative motor that challenged the swinging lever arm hypothesis.

James A Spudich1, Sivaraj Sivaramakrishnan.   

Abstract

The swinging crossbridge hypothesis states that energy from ATP hydrolysis is transduced to mechanical movement of the myosin head while bound to actin. The light chain-binding region of myosin is thought to act as a lever arm that amplifies movements near the catalytic site. This model has been challenged by findings that myosin VI takes larger steps along actin filaments than early interpretations of its structure seem to allow. We now know that myosin VI does indeed operate by an unusual approximately 180 degrees lever arm swing and achieves its large step size using special structural features in its tail domain.

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Year:  2010        PMID: 20094053      PMCID: PMC2859320          DOI: 10.1038/nrm2833

Source DB:  PubMed          Journal:  Nat Rev Mol Cell Biol        ISSN: 1471-0072            Impact factor:   94.444


  103 in total

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Authors:  T Yanagida; M Nakase; K Nishiyama; F Oosawa
Journal:  Nature       Date:  1984 Jan 5-11       Impact factor: 49.962

6.  Myosin VI steps via a hand-over-hand mechanism with its lever arm undergoing fluctuations when attached to actin.

Authors:  Ahmet Yildiz; Hyokeun Park; Dan Safer; Zhaohui Yang; Li-Qiong Chen; Paul R Selvin; H Lee Sweeney
Journal:  J Biol Chem       Date:  2004-07-14       Impact factor: 5.157

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Journal:  Nature       Date:  1987 Aug 6-12       Impact factor: 49.962

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Journal:  Nature       Date:  1985 Jul 25-31       Impact factor: 49.962

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Authors:  M S Mooseker; T R Coleman
Journal:  J Cell Biol       Date:  1989-06       Impact factor: 10.539

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Journal:  J Cell Biol       Date:  1975-12       Impact factor: 10.539

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  44 in total

Review 1.  Principles of unconventional myosin function and targeting.

Authors:  M Amanda Hartman; Dina Finan; Sivaraj Sivaramakrishnan; James A Spudich
Journal:  Annu Rev Cell Dev Biol       Date:  2011-05-31       Impact factor: 13.827

2.  UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region.

Authors:  Hang Shi; Günter Blobel
Journal:  Proc Natl Acad Sci U S A       Date:  2010-11-29       Impact factor: 11.205

Review 3.  The myosin superfamily at a glance.

Authors:  M Amanda Hartman; James A Spudich
Journal:  J Cell Sci       Date:  2012-04-01       Impact factor: 5.285

Review 4.  Modeling stochastic kinetics of molecular machines at multiple levels: from molecules to modules.

Authors:  Debashish Chowdhury
Journal:  Biophys J       Date:  2013-06-04       Impact factor: 4.033

5.  Extension of a three-helix bundle domain of myosin VI and key role of calmodulins.

Authors:  Yanxin Liu; Jen Hsin; HyeongJun Kim; Paul R Selvin; Klaus Schulten
Journal:  Biophys J       Date:  2011-06-22       Impact factor: 4.033

6.  Detailed tuning of structure and intramolecular communication are dispensable for processive motion of myosin VI.

Authors:  Mary Williard Elting; Zev Bryant; Jung-Chi Liao; James A Spudich
Journal:  Biophys J       Date:  2011-01-19       Impact factor: 4.033

Review 7.  Moving into the cell: single-molecule studies of molecular motors in complex environments.

Authors:  Claudia Veigel; Christoph F Schmidt
Journal:  Nat Rev Mol Cell Biol       Date:  2011-02-16       Impact factor: 94.444

8.  Structure of androcam supports specialized interactions with myosin VI.

Authors:  Mehul K Joshi; Sean Moran; Kathleen M Beckingham; Kevin R MacKenzie
Journal:  Proc Natl Acad Sci U S A       Date:  2012-07-31       Impact factor: 11.205

9.  Engineering Circular Gliding of Actin Filaments Along Myosin-Patterned DNA Nanotube Rings To Study Long-Term Actin-Myosin Behaviors.

Authors:  Rizal F Hariadi; Abhinav J Appukutty; Sivaraj Sivaramakrishnan
Journal:  ACS Nano       Date:  2016-09-12       Impact factor: 15.881

10.  Mechanosensation: A Catch Bond That Only Hooks One Way.

Authors:  Vinay Swaminathan; Gregory M Alushin; Clare M Waterman
Journal:  Curr Biol       Date:  2017-11-06       Impact factor: 10.834

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