Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
2005-11-1
pubmed:abstractText
RNA-binding motif protein 4 (RBM4) has been implicated in the regulation of precursor mRNA splicing. Using differential display analysis, we identified mRNAs that associate with RBM4-containing messenger RNPs in vivo. Among these mRNAs, alpha-tropomyosin (alpha-TM) is known to exhibit a muscle cell type-specific splicing pattern. The level of the skeletal muscle-specific alpha-TM mRNA isoform partially correlated with that of RBM4 in human tissues examined and could be modulated by ectopic overexpression or suppression of RBM4. These results indicated that RBM4 directly influences the expression of the skeletal muscle-specific alpha-TM isoform. Using minigenes, we demonstrated that RBM4 can activate the selection of skeletal muscle-specific exons, possibly via binding to intronic pyrimidine-rich elements. By contrast, the splicing regulator polypyrimidine tract binding protein (PTB) excluded these exons; moreover, RBM4 antagonized this PTB-mediated exon exclusion likely by competing with PTB for binding to a CU-rich element. This study suggests a possible mechanism underlying the regulated alternative splicing of alpha-TM by the antagonistic splicing regulators RBM4 and PTB.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-10495287, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-10829067, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11003644, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11081623, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11158314, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11313454, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11421360, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11473790, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11563548, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11779509, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11931771, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-11932019, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12086614, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12177296, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12244124, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12549978, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12574126, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12578833, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12626338, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12628928, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12649496, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-12837581, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-14517304, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-14633994, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-14729963, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-14761971, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-15010470, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-15933722, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-15956978, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-8070413, http://linkedlifedata.com/resource/pubmed/commentcorrection/16260624-8085156
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0270-7306
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10111-21
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:16260624-Alternative Splicing, pubmed-meshheading:16260624-Blotting, Northern, pubmed-meshheading:16260624-Cell Line, pubmed-meshheading:16260624-DNA Primers, pubmed-meshheading:16260624-Exons, pubmed-meshheading:16260624-Gene Expression Profiling, pubmed-meshheading:16260624-Humans, pubmed-meshheading:16260624-Introns, pubmed-meshheading:16260624-Models, Biological, pubmed-meshheading:16260624-Models, Genetic, pubmed-meshheading:16260624-Muscle, Skeletal, pubmed-meshheading:16260624-Plasmids, pubmed-meshheading:16260624-Polymerase Chain Reaction, pubmed-meshheading:16260624-Polypyrimidine Tract-Binding Protein, pubmed-meshheading:16260624-Protein Binding, pubmed-meshheading:16260624-Protein Isoforms, pubmed-meshheading:16260624-Pyrimidines, pubmed-meshheading:16260624-RNA, pubmed-meshheading:16260624-RNA, Messenger, pubmed-meshheading:16260624-RNA Interference, pubmed-meshheading:16260624-RNA-Binding Proteins, pubmed-meshheading:16260624-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:16260624-Tissue Distribution, pubmed-meshheading:16260624-Tropomyosin
pubmed:year
2005
pubmed:articleTitle
Exon selection in alpha-tropomyosin mRNA is regulated by the antagonistic action of RBM4 and PTB.
pubmed:affiliation
Institute of Biomedical Sciences, Academia Sinica, 128 Academy Road Section 2, Nankang, Taipei 11529, Taiwan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't