| pubmed-article:18045990 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18045990 | lifeskim:mentions | umls-concept:C0035696 | lld:lifeskim |
| pubmed-article:18045990 | lifeskim:mentions | umls-concept:C0286330 | lld:lifeskim |
| pubmed-article:18045990 | lifeskim:mentions | umls-concept:C0014230 | lld:lifeskim |
| pubmed-article:18045990 | lifeskim:mentions | umls-concept:C0018850 | lld:lifeskim |
| pubmed-article:18045990 | lifeskim:mentions | umls-concept:C0035542 | lld:lifeskim |
| pubmed-article:18045990 | lifeskim:mentions | umls-concept:C0184512 | lld:lifeskim |
| pubmed-article:18045990 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:18045990 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:18045990 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18045990 | pubmed:dateCreated | 2008-2-5 | lld:pubmed |
| pubmed-article:18045990 | pubmed:abstractText | The polysomal ribonuclease 1 (PMR1) mRNA endonuclease forms a selective complex with its translating substrate mRNAs where it is activated to initiate mRNA decay. Previous work showed tyrosine phosphorylation is required for PMR1 targeting to this polysome-bound complex, and it identified c-Src as the responsible kinase. c-Src phosphorylation occurs in a distinct complex, and the current study shows that 90-kDa heat shock protein (Hsp90) is also recovered with PMR1 and c-Src. Hsp90 binding to PMR1 is inhibited by geldanamycin, and geldanamycin stabilizes substrate mRNA to PMR1-mediated decay. PMR1 is inherently unstable and geldanamycin causes PMR1 to rapidly disappear in a process that is catalyzed by the 26S proteasome. We present a model where Hsp90 interacts transiently to stabilize PMR1 in a manner similar to its interaction with c-Src, thus facilitating the tyrosine phosphorylation and targeting of PMR1 to polysomes. | lld:pubmed |
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| pubmed-article:18045990 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18045990 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18045990 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18045990 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18045990 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18045990 | pubmed:issn | 1939-4586 | lld:pubmed |
| pubmed-article:18045990 | pubmed:author | pubmed-author:PengYongY | lld:pubmed |
| pubmed-article:18045990 | pubmed:author | pubmed-author:SchoenbergDan... | lld:pubmed |
| pubmed-article:18045990 | pubmed:author | pubmed-author:LiuXiaoqiangX | lld:pubmed |
| pubmed-article:18045990 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18045990 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:18045990 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18045990 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18045990 | pubmed:pagination | 546-52 | lld:pubmed |
| pubmed-article:18045990 | pubmed:dateRevised | 2011-4-25 | lld:pubmed |
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| pubmed-article:18045990 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18045990 | pubmed:articleTitle | The 90-kDa heat shock protein stabilizes the polysomal ribonuclease 1 mRNA endonuclease to degradation by the 26S proteasome. | lld:pubmed |
| pubmed-article:18045990 | pubmed:affiliation | Department of Molecular and Cellular Biochemistry, RNA Group and the Comprehensive Cancer Center, The Ohio State University, Columbus, OH 43210, USA. | lld:pubmed |
| pubmed-article:18045990 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18045990 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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