Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
2005-12-12
pubmed:abstractText
ATF4 plays a crucial role in the cellular response to stress and multiple stress responses pathways converge to the translational up-regulation of ATF4. ATF4 is a substrate of the SCF(betaTrCP) ubiquitin ligase that binds to betaTrCP through phosphorylation on a DSGXXXS motif. We show here that ATF4 stability is also modulated by the histone acetyltransferase p300, which induces ATF4 stabilization by inhibiting its ubiquitination. Despite p300 acetylates ATF4, we found that p300-mediated ATF4 stabilization is independent of p300 catalytic activity, using either the inactive form of p300 or the acetylation mutant ATF4-K311R. ATF4 deleted of its p300 binding domain is no more stabilized by p300 nor recruited into nuclear speckles. In consequence of ATF4 stabilization, both p300 and the catalytically inactive enzyme increase ATF4 transcriptional activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
41537-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16219772-Activating Transcription Factor 4, pubmed-meshheading:16219772-Amino Acid Motifs, pubmed-meshheading:16219772-Blotting, Western, pubmed-meshheading:16219772-CREB-Binding Protein, pubmed-meshheading:16219772-Catalysis, pubmed-meshheading:16219772-Cell Line, pubmed-meshheading:16219772-Cell Nucleus, pubmed-meshheading:16219772-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:16219772-Gene Silencing, pubmed-meshheading:16219772-Genetic Vectors, pubmed-meshheading:16219772-Glutathione Transferase, pubmed-meshheading:16219772-HeLa Cells, pubmed-meshheading:16219772-Histone Acetyltransferases, pubmed-meshheading:16219772-Humans, pubmed-meshheading:16219772-Immunoprecipitation, pubmed-meshheading:16219772-Microscopy, Fluorescence, pubmed-meshheading:16219772-Mutation, pubmed-meshheading:16219772-Phosphorylation, pubmed-meshheading:16219772-Plasmids, pubmed-meshheading:16219772-Protein Binding, pubmed-meshheading:16219772-Protein Structure, Tertiary, pubmed-meshheading:16219772-RNA, Small Interfering, pubmed-meshheading:16219772-Transcription, Genetic, pubmed-meshheading:16219772-Transfection, pubmed-meshheading:16219772-Ubiquitin, pubmed-meshheading:16219772-p300-CBP Transcription Factors
pubmed:year
2005
pubmed:articleTitle
p300 modulates ATF4 stability and transcriptional activity independently of its acetyltransferase domain.
pubmed:affiliation
Institut Cochin, Department of Maladies Infectieuses, INSERM U567, CNRS UMR8104, University Rene Descartes Paris V, Bat G. Roussy, 27 Rue du Faubourg Saint Jacques, 75014 Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't