Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-3-11
pubmed:abstractText
We recently reported that APOE promoter activity is stimulated by cAMP, this effect being mediated by factor AP-2 [Garcia et al. (1996) J. Neurosci. 16, 7550-7556]. Here, we study whether cAMP-induced phosphorylation modulates the activity of AP-2. Recombinant AP-2 was phosphorylated in vitro by protein kinase A (PKA) at Ser239. Mutation of Ser239 to Ala abolished in vitro phosphorylation of AP-2 by PKA, but not the DNA binding activity of AP-2. Cotransfection studies showed that PKA stimulated the effect of AP-2 on the APOE promoter, but not that of the S239A mutant. Therefore, cAMP may modulate AP-2 activity by PKA-induced phosphorylation of this factor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes, http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serine, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-2, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/kemptide
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
444
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-31
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10037142-Amino Acid Substitution, pubmed-meshheading:10037142-Apolipoproteins E, pubmed-meshheading:10037142-Binding Sites, pubmed-meshheading:10037142-Cyclic AMP, pubmed-meshheading:10037142-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:10037142-DNA-Binding Proteins, pubmed-meshheading:10037142-Humans, pubmed-meshheading:10037142-Oligonucleotide Probes, pubmed-meshheading:10037142-Oligopeptides, pubmed-meshheading:10037142-Peptide Fragments, pubmed-meshheading:10037142-Phosphorylation, pubmed-meshheading:10037142-Promoter Regions, Genetic, pubmed-meshheading:10037142-Recombinant Fusion Proteins, pubmed-meshheading:10037142-Sequence Deletion, pubmed-meshheading:10037142-Serine, pubmed-meshheading:10037142-Transcription Factor AP-2, pubmed-meshheading:10037142-Transcription Factors, pubmed-meshheading:10037142-Transcriptional Activation, pubmed-meshheading:10037142-Transfection, pubmed-meshheading:10037142-Tumor Cells, Cultured, pubmed-meshheading:10037142-Ultraviolet Rays
pubmed:year
1999
pubmed:articleTitle
Transcription factor AP-2 activity is modulated by protein kinase A-mediated phosphorylation.
pubmed:affiliation
Centro de Biología Molecular Severo Ochoa, CSIC-Universidad Autónoma de Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't