Linked Life Data

8584032

Source:http://linkedlifedata.com/resource/pubmed/id/8584032

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1996-3-20
pubmed:abstractText
The FK506-binding immunophilin hsp56 (FKBP52) is one of several chaperone proteins associated with untrasformed steroid receptors in a multiprotein heterocomplex. The function of heat shock protein 56 (hsp56) with respect to receptor action is unknown. hsp56 is not required for glucocorticoid receptor heterocomplex assembly or for proper folding of the receptor hormone-binding domain into a high affinity steroid-binding conformation. In intact cells, the majority of the hsp56 is located in the nucleus, with a minority colocalizing with microtubules in the cytoplasm. hsp56 contains a conserved negatively charged domain that we speculate might serve as a nuclear localization signal recognition sequence. Here we show that injection of an antibody raised against this negative sequence into intact L cells impedes subsequent dexamethasone-mediated shift of the glucocorticoid receptor into the nucleus. Nonimmune rabbit serum and an antibody raised against another site on hsp56 do not affect receptor movement. Inhibition of receptor movement by the 419 antibody against the negative sequence is blocked by preincubation with purified hsp56, but not by preincubation with purified hsp90, hsp70, or BSA. These observations are consistent with the possibility that hsp56 is involved in receptor trafficking to the nucleus, possibly functioning as the nuclear localization signal recognition protein. Receptor trafficking to the nucleus is not affected by FK506, indicating that the peptidylprolyl isomerase activity of hsp56 is not involved.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1549-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8584032-Amino Acid Sequence, pubmed-meshheading:8584032-Animals, pubmed-meshheading:8584032-Antibodies, Monoclonal, pubmed-meshheading:8584032-Biological Transport, pubmed-meshheading:8584032-Carrier Proteins, pubmed-meshheading:8584032-Cell Nucleus, pubmed-meshheading:8584032-Cytoplasm, pubmed-meshheading:8584032-DNA-Binding Proteins, pubmed-meshheading:8584032-Fluorescent Antibody Technique, Indirect, pubmed-meshheading:8584032-HSP90 Heat-Shock Proteins, pubmed-meshheading:8584032-Heat-Shock Proteins, pubmed-meshheading:8584032-L Cells (Cell Line), pubmed-meshheading:8584032-Macromolecular Substances, pubmed-meshheading:8584032-Mice, pubmed-meshheading:8584032-Microinjections, pubmed-meshheading:8584032-Microtubules, pubmed-meshheading:8584032-Molecular Sequence Data, pubmed-meshheading:8584032-Rabbits, pubmed-meshheading:8584032-Receptors, Glucocorticoid, pubmed-meshheading:8584032-Tacrolimus Binding Proteins
pubmed:year
1995
pubmed:articleTitle
Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus.
pubmed:affiliation
Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't