| pubmed-article:7499384 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7499384 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:7499384 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
| pubmed-article:7499384 | lifeskim:mentions | umls-concept:C0243044 | lld:lifeskim |
| pubmed-article:7499384 | lifeskim:mentions | umls-concept:C1519253 | lld:lifeskim |
| pubmed-article:7499384 | lifeskim:mentions | umls-concept:C1825534 | lld:lifeskim |
| pubmed-article:7499384 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7499384 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:7499384 | lifeskim:mentions | umls-concept:C0920376 | lld:lifeskim |
| pubmed-article:7499384 | pubmed:issue | 48 | lld:pubmed |
| pubmed-article:7499384 | pubmed:dateCreated | 1996-1-18 | lld:pubmed |
| pubmed-article:7499384 | pubmed:abstractText | The abundant, cytoplasmic 90-kDa heat-shock protein associates transiently with the Rous sarcoma virus oncogenic protein tyrosine kinase, pp60v-src, directs its cellular trafficking and negatively regulates its kinase activity. Here we report that the serine/threonine phosphatase inhibitor, okadaic acid, destabilized the heat-shock protein 90-pp60v-src chaperone complex in v-src-transfected cells. Concomitant with complex destabilization by okadaic acid, phosphoserine was doubled and phosphothreonine was increased 20-fold in the heat-shock protein 90. Although phosphorylation of the total pool of immunoprecipitable pp60v-src was unchanged, okadaic acid slightly increased phosphoserine and phosphothreonine levels specifically in pp60v-src bound to heat-shock protein 90. The low level of tyrosine phosphorylation in the pp60v-src complexed with heat-shock protein 90 was further decreased by okadaic acid. Interestingly, okadaic acid-stabilized hyperphosphorylation of the heat-shock protein 90-pp60v-src complex lowered the level of pp60v-src in cell membranes, the functional location for pp60v-src. We suggest that serine/threonine phosphorylation of heat-shock protein 90 and/or pp60v-src functions as a regulatory molecular trigger to release pp60v-src from the chaperone complex at the inner surface of cell membranes. | lld:pubmed |
| pubmed-article:7499384 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7499384 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7499384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499384 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7499384 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:7499384 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7499384 | pubmed:author | pubmed-author:MimnaughE GEG | lld:pubmed |
| pubmed-article:7499384 | pubmed:author | pubmed-author:NeckersL MLM | lld:pubmed |
| pubmed-article:7499384 | pubmed:author | pubmed-author:WhitesellLL | lld:pubmed |
| pubmed-article:7499384 | pubmed:author | pubmed-author:WorlandP JPJ | lld:pubmed |
| pubmed-article:7499384 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7499384 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7499384 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7499384 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7499384 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7499384 | pubmed:pagination | 28654-9 | lld:pubmed |
| pubmed-article:7499384 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:7499384 | pubmed:meshHeading | pubmed-meshheading:7499384-... | lld:pubmed |
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| pubmed-article:7499384 | pubmed:meshHeading | pubmed-meshheading:7499384-... | lld:pubmed |
| pubmed-article:7499384 | pubmed:meshHeading | pubmed-meshheading:7499384-... | lld:pubmed |
| pubmed-article:7499384 | pubmed:meshHeading | pubmed-meshheading:7499384-... | lld:pubmed |
| pubmed-article:7499384 | pubmed:meshHeading | pubmed-meshheading:7499384-... | lld:pubmed |
| pubmed-article:7499384 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7499384 | pubmed:articleTitle | Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the hsp90 stress protein and the pp60v-src tyrosine kinase. | lld:pubmed |
| pubmed-article:7499384 | pubmed:affiliation | Clinical Pharmacology Branch, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA. | lld:pubmed |
| pubmed-article:7499384 | pubmed:publicationType | Journal Article | lld:pubmed |
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