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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2008-2-5
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-10205060,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-10637233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-11222765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-11514224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-11842200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-12242335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-12730603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-12750378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-12923263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-15126367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-15149593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-15375158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-16299471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-16314389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-16455650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-16825573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-16982678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-17245413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-17296726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-17349962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-1922078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-1931972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-7890744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-9020108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-9108479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-9230303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-9428803,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-9632780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-9843494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-9848652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045990-9874780
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1939-4586
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
546-52
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pubmed:dateRevised |
2011-4-25
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pubmed:meshHeading |
pubmed-meshheading:18045990-Animals,
pubmed-meshheading:18045990-Benzoquinones,
pubmed-meshheading:18045990-Binding Sites,
pubmed-meshheading:18045990-COS Cells,
pubmed-meshheading:18045990-Cell Line, Tumor,
pubmed-meshheading:18045990-Cercopithecus aethiops,
pubmed-meshheading:18045990-Endonucleases,
pubmed-meshheading:18045990-HSP90 Heat-Shock Proteins,
pubmed-meshheading:18045990-Humans,
pubmed-meshheading:18045990-Lactams, Macrocyclic,
pubmed-meshheading:18045990-Models, Biological,
pubmed-meshheading:18045990-Polyribosomes,
pubmed-meshheading:18045990-Proteasome Endopeptidase Complex,
pubmed-meshheading:18045990-Protein Binding,
pubmed-meshheading:18045990-Protein Interaction Mapping,
pubmed-meshheading:18045990-Protein Processing, Post-Translational,
pubmed-meshheading:18045990-Protein Structure, Tertiary,
pubmed-meshheading:18045990-RNA, Messenger,
pubmed-meshheading:18045990-RNA Stability,
pubmed-meshheading:18045990-Sequence Deletion
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pubmed:year |
2008
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pubmed:articleTitle |
The 90-kDa heat shock protein stabilizes the polysomal ribonuclease 1 mRNA endonuclease to degradation by the 26S proteasome.
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pubmed:affiliation |
Department of Molecular and Cellular Biochemistry, RNA Group and the Comprehensive Cancer Center, The Ohio State University, Columbus, OH 43210, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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