| pubmed-article:21439943 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21439943 | lifeskim:mentions | umls-concept:C1325596 | lld:lifeskim |
| pubmed-article:21439943 | lifeskim:mentions | umls-concept:C2265627 | lld:lifeskim |
| pubmed-article:21439943 | lifeskim:mentions | umls-concept:C0243044 | lld:lifeskim |
| pubmed-article:21439943 | lifeskim:mentions | umls-concept:C1825534 | lld:lifeskim |
| pubmed-article:21439943 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:21439943 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:21439943 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:21439943 | pubmed:dateCreated | 2011-4-25 | lld:pubmed |
| pubmed-article:21439943 | pubmed:abstractText | Previously, we found that treatment of cells with the Hsp90 inhibitor geldanamycin (GA) leads to a substantial reduction in the number of processing bodies (P-bodies), and also alters the size and subcellular localization of stress granules. These findings imply that the chaperone activity of Hsp90 is involved in the formation of P-bodies and stress granules. To verify these observations, we examined whether another Hsp90 inhibitor radicicol (RA) affected P-bodies and stress granules. Treatment with RA reduced the level of the Hsp90 client protein Argonaute 2 and the number of P-bodies. Although stress granules still assembled in RA-treated cells upon heat shock, they were smaller and more dispersed in the cytoplasm than those in untreated cells. Furthermore eIF4E and eIF4E-transporter were dissociated selectively from stress granules in RA-treated cells. These observations were comparable to those obtained upon treatment with GA in our previous work. Thus, we conclude that abrogation of the chaperone activity of Hsp90 affects P-body formation and the integrity of stress granules. | lld:pubmed |
| pubmed-article:21439943 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21439943 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21439943 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21439943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21439943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21439943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21439943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21439943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21439943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21439943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21439943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21439943 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21439943 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:21439943 | pubmed:issn | 1090-2104 | lld:pubmed |
| pubmed-article:21439943 | pubmed:author | pubmed-author:MatsumotoKenK | lld:pubmed |
| pubmed-article:21439943 | pubmed:author | pubmed-author:MatsumotoShog... | lld:pubmed |
| pubmed-article:21439943 | pubmed:author | pubmed-author:AbeKeikoK | lld:pubmed |
| pubmed-article:21439943 | pubmed:author | pubmed-author:SuzukiYukariY | lld:pubmed |
| pubmed-article:21439943 | pubmed:author | pubmed-author:ZennoShuheiS | lld:pubmed |
| pubmed-article:21439943 | pubmed:author | pubmed-author:MinamiMichiko... | lld:pubmed |
| pubmed-article:21439943 | pubmed:author | pubmed-author:MinamiYasufum... | lld:pubmed |
| pubmed-article:21439943 | pubmed:author | pubmed-author:ShinozakiFumi... | lld:pubmed |
| pubmed-article:21439943 | pubmed:copyrightInfo | Copyright © 2011 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:21439943 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21439943 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:21439943 | pubmed:volume | 407 | lld:pubmed |
| pubmed-article:21439943 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21439943 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21439943 | pubmed:pagination | 720-4 | lld:pubmed |
| pubmed-article:21439943 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:21439943 | pubmed:meshHeading | pubmed-meshheading:21439943... | lld:pubmed |
| pubmed-article:21439943 | pubmed:meshHeading | pubmed-meshheading:21439943... | lld:pubmed |
| pubmed-article:21439943 | pubmed:meshHeading | pubmed-meshheading:21439943... | lld:pubmed |
| pubmed-article:21439943 | pubmed:meshHeading | pubmed-meshheading:21439943... | lld:pubmed |
| pubmed-article:21439943 | pubmed:meshHeading | pubmed-meshheading:21439943... | lld:pubmed |
| pubmed-article:21439943 | pubmed:meshHeading | pubmed-meshheading:21439943... | lld:pubmed |
| pubmed-article:21439943 | pubmed:meshHeading | pubmed-meshheading:21439943... | lld:pubmed |
| pubmed-article:21439943 | pubmed:meshHeading | pubmed-meshheading:21439943... | lld:pubmed |
| pubmed-article:21439943 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21439943 | pubmed:articleTitle | Hsp90 is involved in the formation of P-bodies and stress granules. | lld:pubmed |
| pubmed-article:21439943 | pubmed:affiliation | Molecular Entomology Laboratory, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. matsumok@riken.jp | lld:pubmed |
| pubmed-article:21439943 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21439943 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:3320 | entrezgene:pubmed | pubmed-article:21439943 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21439943 | lld:entrezgene |
