Linked Life Data

9660810

Source:http://linkedlifedata.com/resource/pubmed/id/9660810

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1998-8-13
pubmed:abstractText
Interactions between the dephosphorylated regulatory light chains (RLCs) of smooth muscle myosin are involved in maintaining the enzymatically "off" state. Expressed chimeric smooth muscle heavy meromyosins containing skeletal muscle myosin heavy chain (HC) sequences were used to assess the relative importance of the light chain-binding domain (or "neck") to regulation. Surprisingly, regulation remained intact with a skeletal RLC-binding site. A chimera with the entire alpha-helical neck composed of skeletal HC sequence showed 2-fold regulation of motility and nearly 5-fold regulation of actin-activated ATPase activity. Complete activation of the dephosphorylated state (i.e. complete loss of regulation) occurred when skeletal HC sequence extended from the head/rod junction to the SH1-SH2 helix. Smooth muscle-specific sequences near the motor domain may therefore position the regulatory domain in a way that optimizes RLC-rod-head interactions, thus enabling a completely off state when the RLC is dephosphorylated. Conversely, a chimera that joins the motor domain from unconventional myosin V to the smooth muscle myosin neck and rod showed only 2-fold regulation. The presence of the smooth muscle light chain-binding region and rod is therefore not sufficient to confer complete phosphorylation-dependent regulation upon all motor domains of the myosin family.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18423-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
The light chain-binding domain of the smooth muscle myosin heavy chain is not the only determinant of regulation.
pubmed:affiliation
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254-9110, USA. trybus@salus.med.uvm.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.