Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-7-24
pubmed:abstractText
PCAF is a histone acetyltransferase that associates with p300/CBP and competes with E1A for access to them. While exogenous expression of PCAF potentiates both MyoD-directed transcription and myogenic differentiation, PCAF inactivation by anti-PCAF antibody microinjection prevents differentiation. MyoD interacts directly with both p300/CBP and PCAF, forming a multimeric protein complex on the promoter elements. Viral transforming factors that interfere with muscle differentiation disrupt this complex without affecting the MyoD-DNA interaction, indicating functional significance of the complex formation. Exogenous expression of PCAF or p300 promotes p21 expression and terminal cell-cycle arrest. Both of these activities are dependent on the histone acetyltransferase activity of PCAF, but not on that of p300. These results indicate that recruitment of histone acetyltransferase activity of PCAF by MyoD, through p300/CBP, is crucial for activation of the myogenic program.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetyl-CoA C-Acyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral, Tumor, http://linkedlifedata.com/resource/pubmed/chemical/CREB-Binding Protein, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Crebbp protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/E1A-Associated p300 Protein, http://linkedlifedata.com/resource/pubmed/chemical/Ep300 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/MyoD Protein, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP-associated factor
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35-45
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9659901-Acetyl-CoA C-Acyltransferase, pubmed-meshheading:9659901-Acetyltransferases, pubmed-meshheading:9659901-Animals, pubmed-meshheading:9659901-Antigens, Viral, Tumor, pubmed-meshheading:9659901-CREB-Binding Protein, pubmed-meshheading:9659901-Cell Cycle Proteins, pubmed-meshheading:9659901-Cell Differentiation, pubmed-meshheading:9659901-Cells, Cultured, pubmed-meshheading:9659901-E1A-Associated p300 Protein, pubmed-meshheading:9659901-Gene Expression Regulation, Developmental, pubmed-meshheading:9659901-Gene Expression Regulation, Enzymologic, pubmed-meshheading:9659901-Histone Acetyltransferases, pubmed-meshheading:9659901-Mice, pubmed-meshheading:9659901-Multienzyme Complexes, pubmed-meshheading:9659901-Muscle, Skeletal, pubmed-meshheading:9659901-Muscle Fibers, Skeletal, pubmed-meshheading:9659901-MyoD Protein, pubmed-meshheading:9659901-Nuclear Proteins, pubmed-meshheading:9659901-RNA Polymerase II, pubmed-meshheading:9659901-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9659901-Trans-Activators, pubmed-meshheading:9659901-Transcription Factors, pubmed-meshheading:9659901-Transcriptional Activation, pubmed-meshheading:9659901-p300-CBP Transcription Factors
pubmed:year
1997
pubmed:articleTitle
Differential roles of p300 and PCAF acetyltransferases in muscle differentiation.
pubmed:affiliation
Laboratory of Gene Expression, Fondazione Andrea Cesalpino, Istituto I Clinica Medica, Policlinico Umberto I, University of Rome, La Sapienza, Italy.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't