Linked Life Data

15834131

Source:http://linkedlifedata.com/resource/pubmed/id/15834131

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
2005-8-1
pubmed:abstractText
Myocyte enhancer factor 2 (MEF2) transcription factors play pivotal roles in striated muscle, neuron, and lymphocyte gene expression and are targets of stress- and calcium-mediated signaling. All MEF2 gene products have a common DNA binding and dimerization domain, but MEF2 transcripts are alternatively spliced among coding exons to produce splicing isoforms. In vertebrate MEF2A, -C, and -D, a splice versus no-splice option gives forms that include or exclude a short domain that we designate beta. We show that mRNAs containing beta are expressed predominantly in striated muscle and brain and that splicing to include beta is induced during myocyte differentiation. MEF2 beta+ isoforms are more robust than beta- forms in activating MEF2-responsive reporters despite similar expression levels. One-hybrid transcription assays using Gal4-MEF2 fusions show similar distinctions in the transactivation produced by beta+ versus beta- isoforms in all cell types tested, including myocytes. beta function is position-independent and exists in all MEF2 splicing variant contexts. The activity is not due to cis effects on MEF2 DNA binding or dimerization nor are established transcription factor or coactivator interactions involved. Each MEF2 beta domain contains multiple acidic residues, mutation of which abolishes function. Despite a location between the p38 MAPK docking domain and Thr phosphoacceptors of MEF2A and MEF2C, inclusion of beta does not influence responses of these factors to this signaling pathway. Thus, a conserved pattern of alternative splicing in vertebrate MEF2 genes generates an acidic activation domain in MEF2 proteins selectively in tissues where MEF2 target genes are highly expressed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
28749-60
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15834131-Alternative Splicing, pubmed-meshheading:15834131-Amino Acid Sequence, pubmed-meshheading:15834131-Animals, pubmed-meshheading:15834131-Brain, pubmed-meshheading:15834131-DNA-Binding Proteins, pubmed-meshheading:15834131-Humans, pubmed-meshheading:15834131-MADS Domain Proteins, pubmed-meshheading:15834131-Mice, pubmed-meshheading:15834131-Molecular Sequence Data, pubmed-meshheading:15834131-Muscle, Skeletal, pubmed-meshheading:15834131-Myogenic Regulatory Factors, pubmed-meshheading:15834131-RNA Precursors, pubmed-meshheading:15834131-RNA Splicing, pubmed-meshheading:15834131-Sequence Alignment, pubmed-meshheading:15834131-Sequence Homology, Amino Acid, pubmed-meshheading:15834131-Transcription Factors, pubmed-meshheading:15834131-Transcriptional Activation, pubmed-meshheading:15834131-Vertebrates
pubmed:year
2005
pubmed:articleTitle
Alternative pre-mRNA splicing governs expression of a conserved acidic transactivation domain in myocyte enhancer factor 2 factors of striated muscle and brain.
pubmed:affiliation
Diabetes Research Laboratory, Department of Medicine, Massachusetts General Hospital, Charlestown, Massachusetts 02129, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural