| pubmed-article:15210956 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15210956 | lifeskim:mentions | umls-concept:C1515669 | lld:lifeskim |
| pubmed-article:15210956 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:15210956 | lifeskim:mentions | umls-concept:C1158884 | lld:lifeskim |
| pubmed-article:15210956 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:15210956 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:15210956 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:15210956 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:15210956 | pubmed:dateCreated | 2004-6-30 | lld:pubmed |
| pubmed-article:15210956 | pubmed:abstractText | In metazoans, multiple RNA-binding proteins, including the shuttling serine/arginine-rich (SR)-splicing factors, function as adapters for mRNA nuclear export by interacting with the export receptor TAP/nuclear export factor 1 (NXF1). Yet, it is unclear how interactions between adapters and TAP are regulated. Here, we demonstrate that the SR proteins 9G8 and ASF/SF2 exhibit higher affinity for TAP/NXF1 when hypophosphorylated. 9G8 is recruited to the pre-mRNA in a hyperphosphorylated form but becomes hypophosphorylated during splicing both in vivo and in vitro. TAP preferentially binds spliced mRNA-protein complexes compared with pre-mRNA-protein complexes. Thus, the phosphorylation state of the SR protein adapters may underlie the selectivity of TAP-mediated export of spliced mRNA. | lld:pubmed |
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| pubmed-article:15210956 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15210956 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15210956 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15210956 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15210956 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15210956 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15210956 | pubmed:author | pubmed-author:SteitzJoan... | lld:pubmed |
| pubmed-article:15210956 | pubmed:author | pubmed-author:HuangYingqunY | lld:pubmed |
| pubmed-article:15210956 | pubmed:author | pubmed-author:YarioTherese... | lld:pubmed |
| pubmed-article:15210956 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15210956 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:15210956 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:15210956 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15210956 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15210956 | pubmed:pagination | 9666-70 | lld:pubmed |
| pubmed-article:15210956 | pubmed:dateRevised | 2011-9-27 | lld:pubmed |
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| pubmed-article:15210956 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15210956 | pubmed:articleTitle | A molecular link between SR protein dephosphorylation and mRNA export. | lld:pubmed |
| pubmed-article:15210956 | pubmed:affiliation | Department of Obstetrics, Gynecology, and Reproductive Sciences, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA. | lld:pubmed |
| pubmed-article:15210956 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15210956 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15210956 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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