| pubmed-article:18842582 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C0142661 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C0162796 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C1956003 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C1418833 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C1419980 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:18842582 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:18842582 | pubmed:issue | 51 | lld:pubmed |
| pubmed-article:18842582 | pubmed:dateCreated | 2008-12-16 | lld:pubmed |
| pubmed-article:18842582 | pubmed:abstractText | Pre-mRNA splicing entails reversible phosphorylation of spliceosomal proteins. Recent work has revealed essential roles for Ser/Thr phosphatases, such as protein phosphatase-1 (PP1), in splicing, but how these phosphatases are regulated is largely unknown. We show that nuclear inhibitor of PP1 (NIPP1), a major PP1 interactor in the vertebrate nucleus, recruits PP1 to Sap155 (spliceosome-associated protein 155), an essential component of U2 small nuclear ribonucleoprotein particles, and promotes Sap155 dephosphorylation. C-terminally truncated NIPP1 (NIPP1-DeltaC) formed a hyper-active holoenzyme with PP1, rendering PP1 minimally phosphorylated on an inhibitory site. Forced expression of NIPP1-WT and -DeltaC resulted in slight and severe decreases in Sap155 hyperphosphorylation, respectively, and the latter was accompanied with inhibition of splicing. PP1 overexpression produced similar effects, whereas small interfering RNA-mediated NIPP1 knockdown enhanced Sap155 hyperphosphorylation upon okadaic acid treatment. NIPP1 did not inhibit but rather stimulated Sap155 dephosphorylation by PP1 in vitro through facilitating Sap155/PP1 interaction. Further analysis revealed that NIPP1 specifically recognizes hyperphosphorylated Sap155 thorough its Forkhead-associated domain and dissociates from Sap155 after dephosphorylation by associated PP1. Thus NIPP1 works as a molecular sensor for PP1 to recognize phosphorylated Sap155. | lld:pubmed |
| pubmed-article:18842582 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18842582 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18842582 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18842582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18842582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18842582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18842582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18842582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18842582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18842582 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18842582 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:18842582 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:KosekiHaruhik... | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:SatoMasamiM | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:KawamuraTakes... | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:BollenMathieu... | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:BeullensMoniq... | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:IsonoKyoichiK | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:ShimaHiroshiH | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:KikuchiKunimi... | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:MitsuhashiShi... | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:TanumaNobuhir... | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:NomuraMiyukiM | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:KimSei-EunSE | lld:pubmed |
| pubmed-article:18842582 | pubmed:author | pubmed-author:TsubakiYaoY | lld:pubmed |
| pubmed-article:18842582 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18842582 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:18842582 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:18842582 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18842582 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18842582 | pubmed:pagination | 35805-14 | lld:pubmed |
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| pubmed-article:18842582 | pubmed:meshHeading | pubmed-meshheading:18842582... | lld:pubmed |
| pubmed-article:18842582 | pubmed:meshHeading | pubmed-meshheading:18842582... | lld:pubmed |
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| pubmed-article:18842582 | pubmed:meshHeading | pubmed-meshheading:18842582... | lld:pubmed |
| pubmed-article:18842582 | pubmed:meshHeading | pubmed-meshheading:18842582... | lld:pubmed |
| pubmed-article:18842582 | pubmed:meshHeading | pubmed-meshheading:18842582... | lld:pubmed |
| pubmed-article:18842582 | pubmed:meshHeading | pubmed-meshheading:18842582... | lld:pubmed |
| pubmed-article:18842582 | pubmed:meshHeading | pubmed-meshheading:18842582... | lld:pubmed |
| pubmed-article:18842582 | pubmed:meshHeading | pubmed-meshheading:18842582... | lld:pubmed |
| pubmed-article:18842582 | pubmed:meshHeading | pubmed-meshheading:18842582... | lld:pubmed |
| pubmed-article:18842582 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18842582 | pubmed:articleTitle | Nuclear inhibitor of protein phosphatase-1 (NIPP1) directs protein phosphatase-1 (PP1) to dephosphorylate the U2 small nuclear ribonucleoprotein particle (snRNP) component, spliceosome-associated protein 155 (Sap155). | lld:pubmed |
| pubmed-article:18842582 | pubmed:affiliation | Division of Cancer Chemotherapy, Miyagi Cancer Center Research Institute, Natori 981-1293, Japan. tanuma-no872@pref.miyagi.jp | lld:pubmed |
| pubmed-article:18842582 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18842582 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18842582 | lld:pubmed |
