Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-9-22
pubmed:abstractText
Although several lines of evidence have indicated that the activity of SRC-3/AIB1/ACTR/pCIP/RAC3/TRAM1 could be regulated by phosphorylation, an important question remained as to how different signaling pathways can act through limiting concentrations of the same SRC-3 molecule to exert different physiological functions. Herein, we report the successful identification of six functional in vivo SRC-3 phosphorylation sites. Interestingly, all phosphorylation sites are required for coactivation of estrogen and androgen receptors, but not all sites are required for coactivation of NF-kappaB. Different combinations of site-specific phosphorylations of SRC-3 are required for induction of IL-6 gene expression by TNF-alpha as compared to oncogenic transformation of MEFs. Mechanisms of pathway selectivity involve protein-protein interactions of differentially phosphorylated SRC-3 with downstream transcriptional activators and coactivators. Our results uncovered an additional level of transcriptional regulation whereby specific modulations of SRC-3 phosphorylation allow this coactivator to function as a regulatable integrator for diverse signaling pathways in cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione, http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/NCOA3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Ncoa3 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 3, http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1097-2765
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Cell Press
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
937-49
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15383283-Acetyltransferases, pubmed-meshheading:15383283-Animals, pubmed-meshheading:15383283-Blotting, Western, pubmed-meshheading:15383283-Cell Line, pubmed-meshheading:15383283-Cell Line, Tumor, pubmed-meshheading:15383283-Fibroblasts, pubmed-meshheading:15383283-Genome, pubmed-meshheading:15383283-Glutathione, pubmed-meshheading:15383283-HeLa Cells, pubmed-meshheading:15383283-Histone Acetyltransferases, pubmed-meshheading:15383283-Humans, pubmed-meshheading:15383283-Mice, pubmed-meshheading:15383283-Nuclear Receptor Coactivator 3, pubmed-meshheading:15383283-Oncogene Proteins, pubmed-meshheading:15383283-Phosphorylation, pubmed-meshheading:15383283-Precipitin Tests, pubmed-meshheading:15383283-RNA, Small Interfering, pubmed-meshheading:15383283-Recombinant Fusion Proteins, pubmed-meshheading:15383283-Retroviridae, pubmed-meshheading:15383283-Signal Transduction, pubmed-meshheading:15383283-Trans-Activators, pubmed-meshheading:15383283-Transcription Factors
pubmed:year
2004
pubmed:articleTitle
Selective phosphorylations of the SRC-3/AIB1 coactivator integrate genomic reponses to multiple cellular signaling pathways.
pubmed:affiliation
Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.