Linked Life Data

9461343

Source:http://linkedlifedata.com/resource/pubmed/id/9461343

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1998-3-18
pubmed:abstractText
Myf-5, a member of a family of muscle-specific transcription factors, is important for myogenic cell determination and differentiation. Here, we report that Myf-5 protein constitutes a substrate for phosphorylation in vitro by protein kinase CK2. We identified two potential phosphorylation sites at serine49 and serine133, both of which seem to be necessary for Myf-5 activity. Mutants which can no longer be phosphorylated fail to transactivate E-box-dependent reporter genes and act as trans-dominant repressors of wild-type Myf-5. Normal activity can be restored by replacing the serine residues with glutamate suggesting that a negative charge at these sites is obligatory for Myf-5 activity. Although serine133 is part of helix 2 which mediates dimerization, we find no evidence for impaired DNA-binding or heterodimerization of the Ser-Ala133 mutant. Some serine49 mutations exhibit reduced nuclear localization and/or protein stability. Our data suggest that CK2-mediated phosphorylation of Myf-5 is required for Myf-5 activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
378
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1445-56
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Two putative protein kinase CK2 phosphorylation sites are important for Myf-5 activity.
pubmed:affiliation
Department of Cell and Molecular Biology, University of Braunschweig, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't