Linked Life Data

7915146

Source:http://linkedlifedata.com/resource/pubmed/id/7915146

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-9-29
pubmed:abstractText
Mammalian steroid receptors exist in hormone-free cells in a heterocomplex that contains the three heat shock proteins hsp90, hsp70 and hsp56. Some protein kinases, including pp60v-src and v-Raf, exist in similar cytosolic heterocomplexes containing hsp90 and a 50 kDa protein of unknown function, pp50. The four proteins--hsp90, hsp70, hsp56 and pp50--exist together in a heterocomplex independent of the presence of steroid receptors and protein kinases. Both the receptor and the protein kinase heterocomplexes can be formed by a protein folding-heterocomplex assembly system in reticulocyte lysate that carries out an hsp70-dependent attachment of the proteins to the preformed heat shock protein complex. Association of receptors with this structure occurs at the termination of receptor translation and is critical for maintenance of the receptors in a transcriptionally inactive state in the absence of hormone. We discuss how this preformed protein folding structure may be involved in the subsequent targeted trafficking of steroid receptors through the cytoplasmic space to the nucleus.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1043-4682
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
83-93
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Chaperone functions of the heat shock proteins associated with steroid receptors.
pubmed:affiliation
Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review