Chaperone functions of the heat shock proteins associated with steroid receptors
dc.contributor.author | Pratt, William B. | en_US |
dc.contributor.author | Welsh, Michael J. | en_US |
dc.date.accessioned | 2006-04-10T18:13:51Z | |
dc.date.available | 2006-04-10T18:13:51Z | |
dc.date.issued | 1994-04 | en_US |
dc.identifier.citation | Pratt, William B., Welsh, Michael J. (1994/04)."Chaperone functions of the heat shock proteins associated with steroid receptors." Seminars in Cell Biology 5(2): 83-93. <http://hdl.handle.net/2027.42/31652> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WX1-45NJF45-19/2/b0bc05fb65456a5096b048b2b8a42247 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/31652 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=7915146&dopt=citation | en_US |
dc.description.abstract | 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 hetorocomplexes 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. | en_US |
dc.format.extent | 936150 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Chaperone functions of the heat shock proteins associated with steroid receptors | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pharmacology and Anatomy and Cell Biology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. | en_US |
dc.contributor.affiliationum | Department of Pharmacology and Anatomy and Cell Biology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. | en_US |
dc.identifier.pmid | 7915146 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/31652/1/0000586.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1006/scel.1994.1012 | en_US |
dc.identifier.source | Seminars in Cell Biology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.