Document Detail

Myosin VI: cellular functions and motor properties.
MedLine Citation:
PMID:  15647169     Owner:  NLM     Status:  MEDLINE    
Myosin VI has been localized in membrane ruffles at the leading edge of cells, at the trans-Golgi network compartment of the Golgi complex and in clathrin-coated pits or vesicles, indicating that it functions in a wide variety of intracellular processes. Myosin VI moves along actin filaments towards their minus end, which is the opposite direction to all of the other myosins so far studied (to our knowledge), and is therefore thought to have unique properties and functions. To investigate the cellular roles of myosin VI, we identified various myosin VI binding partners and are currently characterizing their interactions within the cell. As an alternative approach, we have expressed and purified full-length myosin VI and studied its in vitro properties. Previous studies assumed that myosin VI was a dimer, but our biochemical, biophysical and electron microscopic studies reveal that myosin VI can exist as a stable monomer. We observed, using an optical tweezers force transducer, that monomeric myosin VI is a non-processive motor which, despite a relatively short lever arm, generates a large working stroke of 18 nm. Whether monomer and/or dimer forms of myosin VI exist in cells and their possible functions will be discussed.
Rhys Roberts; Ida Lister; Stephan Schmitz; Matthew Walker; Claudia Veigel; John Trinick; Folma Buss; John Kendrick-Jones
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Philosophical transactions of the Royal Society of London. Series B, Biological sciences     Volume:  359     ISSN:  0962-8436     ISO Abbreviation:  Philos. Trans. R. Soc. Lond., B, Biol. Sci.     Publication Date:  2004 Dec 
Date Detail:
Created Date:  2005-01-13     Completed Date:  2005-03-29     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7503623     Medline TA:  Philos Trans R Soc Lond B Biol Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  1931-44     Citation Subset:  IM    
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
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MeSH Terms
Actins / metabolism
Calcium / metabolism
Calmodulin / metabolism
Cell Movement / physiology
Endocytosis / physiology
Models, Biological*
Molecular Motor Proteins / physiology*
Muscle Contraction / physiology*
Myosin Heavy Chains / chemistry*,  metabolism,  physiology*
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Grant Support
071162//Wellcome Trust
Reg. No./Substance:
0/Actins; 0/Calmodulin; 0/Molecular Motor Proteins; 0/Myosin Heavy Chains; 0/myosin VI; 7440-70-2/Calcium

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