Journal article
Calreticulin modulates the in vitro DNA binding but not the in vivo transcriptional activation by peroxisome proliferator-activated receptor/retinoid X receptor heterodimers
Abstract
Calreticulin is a ubiquitous calcium binding/storage protein found primarily in the endoplasmic reticulum. Calreticulin has been shown to inhibit DNA binding and transcriptional activation by glucocorticoid and androgen hormone receptors by binding to the conserved sequence KXFF(K/R)R, present in the DNA-binding domains of all known members of the steroid/nuclear hormone receptor superfamily. To determine whether calreticulin might be a general …
Authors
Winrow CJ; Miyata KS; Marcus SL; Burns K; Michalak M; Capone JP; Rachubinski RA
Journal
Molecular and Cellular Endocrinology, Vol. 111, No. 2, pp. 175–179
Publisher
Elsevier
Publication Date
6 1995
DOI
10.1016/0303-7207(95)03563-m
ISSN
0303-7207
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceAnimalsBase SequenceBinding SitesCalcium-Binding ProteinsCalreticulinDNAMacromolecular SubstancesMolecular Sequence DataRatsReceptors, Cytoplasmic and NuclearReceptors, Retinoic AcidRetinoid X ReceptorsRibonucleoproteinsTranscription FactorsTranscription, GeneticTranscriptional ActivationTransfection