Linked Life Data

17286578

Source:http://linkedlifedata.com/resource/pubmed/id/17286578

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-2-14
pubmed:abstractText
Adipocyte differentiation is an ordered multistep process requiring the sequential activation of several groups of adipogenic transcription factors, including CCAAT/enhancer-binding protein-alpha and peroxisome proliferator-activated receptor-gamma, and coactivators. Here we show that replication factor C 140, which was known to act as a coactivator for CCAAT/enhancer-binding protein-alpha in our previous study, was phosphorylated on the proliferating cell nuclear antigen-bindng domain during the adipocyte differentiation process. Calmodulin-dependent protein kinase II was responsible for phosphorylating replication factor C 140 in the process of adipocyte differentiation. Ser518 of replication factor C 140 was identified as a major target of calmodulin-dependent protein kinase II phosphorylation in vitro. Calmodulin-dependent protein kinase II inhibitor attenuated phosphorylation of replication factor C 140 by differentiation inducers and blocked replication factor C 140-derived transcriptional activation. Taken together, these findings demonstrate that calmodulin-dependent protein kinase II signaling leads the cooperative transactivation of CCAAT/enhancer-binding protein-alpha and replication factor C 140 through an increase in replication factor C 140 phosphorylation, and subsequently enhances the transcriptional activation of target genes involved in adipocyte differentiation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1742-464X
pubmed:author
pubmed:issnType
Print
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1235-45
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:17286578-3T3-L1 Cells, pubmed-meshheading:17286578-Adipocytes, pubmed-meshheading:17286578-Animals, pubmed-meshheading:17286578-CCAAT-Enhancer-Binding Protein-alpha, pubmed-meshheading:17286578-Calcium-Calmodulin-Dependent Protein Kinase Type 2, pubmed-meshheading:17286578-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:17286578-Cell Differentiation, pubmed-meshheading:17286578-Genes, Reporter, pubmed-meshheading:17286578-Luciferases, pubmed-meshheading:17286578-Mice, pubmed-meshheading:17286578-Phosphorylation, pubmed-meshheading:17286578-Precipitin Tests, pubmed-meshheading:17286578-Protein Structure, Tertiary, pubmed-meshheading:17286578-Protein Subunits, pubmed-meshheading:17286578-RNA, Small Interfering, pubmed-meshheading:17286578-Replication Protein C, pubmed-meshheading:17286578-Transfection
pubmed:year
2007
pubmed:articleTitle
Phosphorylation of the large subunit of replication factor C is associated with adipocyte differentiation.
pubmed:affiliation
Department of Molecular Biology, Pusan National University, Jang-Jeon Dong, Keum-Jeong Gu, Busan 607-935, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't