pubmed-article:17000773 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17000773 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:17000773 | lifeskim:mentions | umls-concept:C0015295 | lld:lifeskim |
pubmed-article:17000773 | lifeskim:mentions | umls-concept:C1415642 | lld:lifeskim |
pubmed-article:17000773 | lifeskim:mentions | umls-concept:C1419998 | lld:lifeskim |
pubmed-article:17000773 | lifeskim:mentions | umls-concept:C1822774 | lld:lifeskim |
pubmed-article:17000773 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:17000773 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:17000773 | lifeskim:mentions | umls-concept:C0002317 | lld:lifeskim |
pubmed-article:17000773 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:17000773 | pubmed:dateCreated | 2006-11-19 | lld:pubmed |
pubmed-article:17000773 | pubmed:abstractText | The inclusion of exons 2 and 3 of alpha-tropomyosin is governed through tissue-specific alternative splicing. These exons are mutually exclusive, with exon 2 included in smooth muscle cells and exon 3 included in nearly all other cell types. Several cis-acting sequences contribute to this splicing decision: the branchpoints and pyrimidine tracts upstream of both exons, UGC-repeat elements flanking exon 3, and a series of purine-rich enhancers in exon 2. Previous work showed that proteins rich in serine-arginine (SR) dipeptides act through the exon 2 enhancers, but the specific proteins responsible for such activation remained unknown. Here we show that a 35-kDa member of the SR protein family, 9G8, can activate the splicing of alpha-tropomyosin exon 2. Using RNA affinity chromatography and cross-linking competition assays, we also demonstrate that the heterogeneous nuclear ribonucleoproteins (hnRNPs) H and F bind to and compete for the same elements. Overexpression of hnRNPs H and F blocked 9G8-mediated splicing both in vivo and in vitro, and small interfering RNA-directed depletion of H and F led to an increase in exon 2 splicing. These data suggest that the activation of exon 2 is dependent on the antagonistic activities of 9G8 and hnRNPs H and F. | lld:pubmed |
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pubmed-article:17000773 | pubmed:language | eng | lld:pubmed |
pubmed-article:17000773 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17000773 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17000773 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |