Linked Life Data

7818551

Source:http://linkedlifedata.com/resource/pubmed/id/7818551

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-2-9
pubmed:abstractText
Dystrophin is phosphorylated by several protein kinases. In this work, we have studied the effects of dystrophin phosphorylation on the binding to actin. Purified dystrophin was phosphorylated in vitro by the catalytic subunit of cAMP-dependent protein kinase (PKA), casein kinase II (CK-II), and protein kinase c (PKC). The results demonstrate that phosphorylation of dystrophin by PKA phosphorylation caused a three fold increase in dystrophin binding to actin. In contrast, phosphorylation by CK-II or PKC inhibited the binding to actin. These results indicate that phosphorylation of dystrophin modulates its interaction with the actin cytoskeleton. It is suggested that phosphorylation may be one mechanism for regulating protein turnover in muscle membrane-skeleton.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
206
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-63
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Phosphorylation of dystrophin:effects on actin binding.
pubmed:affiliation
Centro di Studio per la Biologia e la Fisiopatologia Muscolare-Dipartimento di Scienze Biomediche Sperimentali, Universita' di Padova, Italy.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't