MYOSIN VI: Cellular Functions and Motor Properties
- 1 November 2004
- journal article
- review article
- Published by Annual Reviews in Annual Review of Cell and Developmental Biology
- Vol. 20 (1) , 649-676
- https://doi.org/10.1146/annurev.cellbio.20.012103.094243
Abstract
▪ Abstract Myosin motor proteins use the energy derived from ATP hydrolysis to move cargo along actin tracks. Myosin VI, unlike almost all other myosins, moves toward the minus end of actin filaments and functions in a variety of intracellular processes such as vesicular membrane traffic, cell migration, and mitosis. These diverse roles of myosin VI are mediated by interaction with a number of different binding partners present in multi-protein complexes. Myosin VI can work in vitro as a processive dimeric motor and as a nonprocessive monomeric motor, each with a large working stroke. The possibility that both monomeric and dimeric forms of myosin VI operate in the cell may represent an important regulatory mechanism for controlling the multiple steps in transport pathways where nonprocessive and processive motors are required.Keywords
This publication has 99 references indexed in Scilit:
- Sorting it outThe Journal of cell biology, 2003
- Myosin IXb is a single-headed minus-end-directed processive motorNature Cell Biology, 2002
- Class VI Myosin Moves Processively along Actin Filaments Backward with Large StepsBiochemical and Biophysical Research Communications, 2002
- Interactions of the Low Density Lipoprotein Receptor Gene Family with Cytosolic Adaptor and Scaffold Proteins Suggest Diverse Biological Functions in Cellular Communication and Signal TransductionJournal of Biological Chemistry, 2000
- SAP Family ProteinsBiochemical and Biophysical Research Communications, 2000
- Golgi Structure in Three Dimensions: Functional Insights from the Normal Rat Kidney CellThe Journal of cell biology, 1999
- Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complexEuropean Journal of Cell Biology, 1998
- A family of unconventional myosins from the nematode Caenorhabditis elegansJournal of Molecular Biology, 1997
- The mouse Snell's waltzer deafness gene encodes an unconventional myosin required for structural integrity of inner ear hair cellsNature Genetics, 1995
- Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin moleculesNature, 1983