Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
2002-4-1
pubmed:abstractText
Dermo-1 is a multifunctional basic helix-loop-helix (bHLH) transcription factor that has been shown to be a potent negative regulator for gene transcription and apoptosis. To understand the molecular mechanisms that mediate the function of Dermo-1, we generated a series of Dermo-1 mutants and used a MyoD-mediated transcriptional activation model to characterize the roles of its N-terminal, bHLH, and C-terminal structural domains in transcriptional repression. Both the C-terminal and HLH domains of Dermo-1 were essential for its repression of MyoD-mediated transactivation. Dermo-1 repressed, in a dose-dependent fashion, the transactivation activity of myocyte enhancer factor 2 (MEF2), a protein known to cooperate with MyoD in activating E-box-dependent gene expression. Both the N- and C-terminal domains of Dermo-1, but not the bHLH domain, were required for the inhibition of MEF2, suggesting that Dermo-1 inhibits both MyoD- and MEF2-dependent transactivation but through different mechanisms. Dermo-1 interacted directly with MEF2 and selectively repressed the MEF2 transactivation domain. An overall increase of histone acetylation induced by trichostatin A treatment reduced Dermo-1 transcriptional repression activity, suggesting that histone deacetylation is involved in Dermo-1-mediated transcriptional repression. Together, these results suggest that MEF2 is an important target in Dermo-1-mediated transcriptional repression and provide initial evidence of the involvement of histone acetylation in Dermo-1 transcriptional repression.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/Hydroxamic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Luciferases, http://linkedlifedata.com/resource/pubmed/chemical/MyoD Protein, http://linkedlifedata.com/resource/pubmed/chemical/Myogenic Regulatory Factors, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Twist Transcription Factor, http://linkedlifedata.com/resource/pubmed/chemical/Twist2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/myocyte-specific enhancer-binding..., http://linkedlifedata.com/resource/pubmed/chemical/trichostatin A
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12310-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11809751-Acetylation, pubmed-meshheading:11809751-Amino Acid Sequence, pubmed-meshheading:11809751-Animals, pubmed-meshheading:11809751-Blotting, Western, pubmed-meshheading:11809751-Chromatin, pubmed-meshheading:11809751-DNA, Complementary, pubmed-meshheading:11809751-DNA-Binding Proteins, pubmed-meshheading:11809751-Dose-Response Relationship, Drug, pubmed-meshheading:11809751-Histone Deacetylases, pubmed-meshheading:11809751-Histones, pubmed-meshheading:11809751-Hydroxamic Acids, pubmed-meshheading:11809751-Luciferases, pubmed-meshheading:11809751-Mice, pubmed-meshheading:11809751-Models, Biological, pubmed-meshheading:11809751-Molecular Sequence Data, pubmed-meshheading:11809751-Mutation, pubmed-meshheading:11809751-MyoD Protein, pubmed-meshheading:11809751-Myogenic Regulatory Factors, pubmed-meshheading:11809751-Point Mutation, pubmed-meshheading:11809751-Precipitin Tests, pubmed-meshheading:11809751-Protein Binding, pubmed-meshheading:11809751-Protein Structure, Tertiary, pubmed-meshheading:11809751-Repressor Proteins, pubmed-meshheading:11809751-Sequence Homology, Amino Acid, pubmed-meshheading:11809751-Transcription, Genetic, pubmed-meshheading:11809751-Transcription Factors, pubmed-meshheading:11809751-Transcriptional Activation, pubmed-meshheading:11809751-Transfection, pubmed-meshheading:11809751-Twist Transcription Factor
pubmed:year
2002
pubmed:articleTitle
Dermo-1, a multifunctional basic helix-loop-helix protein, represses MyoD transactivation via the HLH domain, MEF2 interaction, and chromatin deacetylation.
pubmed:affiliation
Department of Internal Medicine and the Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.