Linked Life Data

15196563

Source:http://linkedlifedata.com/resource/pubmed/id/15196563

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-6-15
pubmed:abstractText
Myosin VI is a member of a superfamily of actin-based motors with at least 18 different sub-types or classes. Myosins are best known as proteins that use ATP-hydrolysis-mediated conformational changes to move along actin filaments. Because of this property, some myosins, including myosins I, V, and VI, are thought to be transporters of vesicle or protein cargoes. Myosin VI has been implicated in many seemingly different processes through functional studies in flies, worms and mammals. In several cases, its role is not easily explained by transport along actin. In addition, some of the biochemical and biophysical properties of myosin VI suggest other mechanisms of action. In this review, we summarize recent data that suggest diverse functions for myosin VI and offer an explanation for how myosin VI may function similarly in all of them. We hypothesize that the main function of myosin VI is to bind tightly to actin, stabilizing actin cytoskeletal structures and linking actin structures to membranes and protein complexes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0955-0674
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
189-94
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Myosin VI: a structural role in actin organization important for protein and organelle localization and trafficking.
pubmed:affiliation
Department of Biology, Washington University, One Brookings Drive, Saint Louis, MO 63130, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review