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Titolo:
Glucocorticoid receptor homodimers and glucocorticoid-mineralcorticoid receptor heterodimers form in the cytoplasm through alternative dimerization interfaces
Autore:
Savory, JGA; Prefontaine, GG; Lamprecht, C; Liao, MM; Walther, RF; Lefebvre, YA; Hache, RJG;
Indirizzi:
Univ Ottawa, Ottawa Hosp, Loeb Hlth Res Inst, Dept Biochem Microbiol & Immunol, Ottawa, ON K1Y 4E9, Canada Univ Ottawa Ottawa ON Canada K1Y 4E9 Immunol, Ottawa, ON K1Y 4E9, Canada Univ Ottawa, Ottawa Hosp, Loeb Hlth Res Inst, Dept Med, Ottawa, ON K1Y 4E9, Canada Univ Ottawa Ottawa ON Canada K1Y 4E9 Dept Med, Ottawa, ON K1Y 4E9, Canada Univ Ottawa, Ottawa Hosp, Loeb Hlth Res Inst, Grad Program Biochem, Ottawa, ON K1Y 4E9, Canada Univ Ottawa Ottawa ON Canada K1Y 4E9 Biochem, Ottawa, ON K1Y 4E9, Canada
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 3, volume: 21, anno: 2001,
pagine: 781 - 793
SICI:
0270-7306(200102)21:3<781:GRHAGR>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
DNA-BINDING DOMAIN; STEROID-HORMONE RECEPTORS; HEAT-SHOCK-PROTEIN; NUCLEAR RECEPTOR; PROGESTERONE RECEPTORS; MINERALOCORTICOID RECEPTORS; TRANSCRIPTIONAL ACTIVATION; CRYSTALLOGRAPHIC ANALYSIS; ESTROGEN-RECEPTOR; IN-VITRO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
68
Recensione:
Indirizzi per estratti:
Indirizzo: Lefebvre, YA Univ Ottawa, Ottawa Hosp, Loeb Hlth Res Inst, Dept Biochem Microbiol & Immunol, 725 Parkdale Ave, Ottawa, ON K1Y 4E9, Canada Univ Ottawa725 Parkdale Ave Ottawa ON Canada K1Y 4E9 Canada
Citazione:
J.G.A. Savory et al., "Glucocorticoid receptor homodimers and glucocorticoid-mineralcorticoid receptor heterodimers form in the cytoplasm through alternative dimerization interfaces", MOL CELL B, 21(3), 2001, pp. 781-793

Abstract

Steroid hormone receptors act to regulate specific gene transcription primarily as steroid-specific dimers bound to palindromic DNA response elements. DNA-dependent dimerization contacts mediated between the receptor DNA binding domains stabilize DNA binding. Additionally, some steroid receptors dimerize prior to their arrival on DNA through interactions mediated through the receptor ligand binding domain. In this report, we describe the steroid-induced homomeric interaction of the rat glucocorticoid receptor (GR) in solution in vivo. Our results demonstrate that GR interacts in solution at least as a dimer, and we have delimited this interaction to a novel interface within the hinge region of GR that appears to be both necessary and sufficient for direct binding. Strikingly, we also demonstrate an interaction between GR and the mineralocorticoid receptor in solution in vivo that is dependent on the ligand binding domain of GR alone and is separable from homodimerization of the glucocorticoid receptor. These results indicate that functional interactions between the glucocorticoid and mineralocorticoid receptors in activating specific gene transcription are probably more complex than has been previously appreciated.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 01:51:02