Linked Life Data

15665867

Source:http://linkedlifedata.com/resource/pubmed/id/15665867

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-2-9
pubmed:abstractText
Myosin V is a calmodulin-binding motor protein. The dissociation of single calmodulin molecules from individual myosin V molecules at 1 microM Ca(2+) correlates with a reduction in sliding velocity in an in vitro motility assay. The dissociation of two calmodulin molecules at 5 microM Ca(2+) correlates with a detachment of actin filaments from myosin V. To mimic the regulation of myosin V motility by Ca(2+) in a cell, caged Ca(2+) coupled with a UV flash system was used to produce Ca(2+) transients. During the Ca(2+) transient, myosin V goes through the functional cycle of reduced sliding velocity, actin detachment and reattachment followed by the recovery of the sliding velocity. These results indicate that myosin V motility is regulated by Ca(2+) through a reduction in actin-binding affinity resulting from the dissociation of single calmodulin molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1545-9993
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
127-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Motility of myosin V regulated by the dissociation of single calmodulin.
pubmed:affiliation
Center for Interdisciplinary Research, Tohoku University, Sendai 980-8578, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't