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PMID: 15647169 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Myosin VI: cellular functions and motor properties.

Roberts R, Lister I, Schmitz S, Walker M, Veigel C, Trinick J, Buss F, Kendrick-Jones J

Abstract

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.

MeSH Terms
Actins/metabolism Animals Calcium/metabolism Calmodulin/metabolism Cell Movement/physiology Endocytosis/physiology Models, Biological Molecular Motor Proteins/physiology Muscle Contraction/physiology Myosin Heavy Chains/chemistry,metabolism,physiology Phosphorylation Protein Binding Protein Conformation Protein Structure, Tertiary
Chemicals
Actins Calmodulin Molecular Motor Proteins myosin VI Myosin Heavy Chains Calcium
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Roberts Rhys
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Lister Ida
Schmitz Stephan
Walker Matthew
Veigel Claudia
Trinick John
Buss Folma
Kendrick-Jones John
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Article Info
Journal
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
Abbr.
Philos Trans R Soc Lond B Biol Sci
ISSN
0962-8436
Published
2004-12-29
Pages
1931-44
Language
English
Region
England
NLM ID
7503623
PMCID
PMC1693462
Subset
IM
Grants
Wellcome Trust · 071162 · United Kingdom
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