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Titolo:
DNA binding domains in diverse nuclear receptors function as nuclear export signals
Autore:
Black, BE; Holaska, JM; Rastinejad, F; Paschal, BM;
Indirizzi:
Univ Virginia, Ctr Cell Signaling, Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA Univ Virginia, Dept Biochem & Mol Genet, Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA Univ Virginia, Cell & Mol Biol Program, Charlottesville, VA 22908 USA UnivVirginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA Univ Virginia, Dept Pharmacol, Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA
Titolo Testata:
CURRENT BIOLOGY
fascicolo: 22, volume: 11, anno: 2001,
pagine: 1749 - 1758
SICI:
0960-9822(20011113)11:22<1749:DBDIDN>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUCOCORTICOID RECEPTOR; LIVING CELLS; ANDROGEN RECEPTOR; PROGESTERONE-RECEPTOR; LOCALIZATION SIGNAL; CALRETICULIN; TRANSPORT; COMPLEX; RAN; TRANSCRIPTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Paschal, BM Univ Virginia, Ctr Cell Signaling, Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 ille, VA 22908 USA
Citazione:
B.E. Black et al., "DNA binding domains in diverse nuclear receptors function as nuclear export signals", CURR BIOL, 11(22), 2001, pp. 1749-1758

Abstract

Background: The nuclear receptor superfamily of transcription factors directs gene expression through DNA sequence-specific interactions with target genes. Nuclear import of these receptors involves recognition of a nuclear localization signal (NLS) by importins, which mediate translocation into the nucleus. Nuclear receptors lack a leucine-rich nuclear export signal (NES), and export is insensitive to leptomycin B, indicating that nuclear export is not mediated by Crm1. Results: We set out to define the NES in the glucocorticoid receptor (GR) and to characterize the export pathway. We found that the 69 amino acid DNAbinding domain (DBD) of GR, which is unrelated to any known NES, is necessary and sufficient for export. Mutational analysis revealed that a 15 aminoacid sequence between the two zinc binding loops in the GR-DBD confers nuclear export to a GFP reporter protein, and alanine-scanning mutagenesis wasused to identify the residues within this sequence that are critical for export. The DBD is highly related (41 %-88% identity) in steroid, nonsteroid, and orphan nuclear receptors, and we found that the DBDs from ten different nuclear receptors all function as export signals. DBD-dependent nuclear export is saturable, and prolonged nuclear localization of the GR increasesits transcriptional activity. Conclusions: Multiple members of the nuclear receptor superfamily use a common pathway to exit the nucleus. We propose that NLS-mediated import and DBD-mediated export define a shuttling cycle that integrates the compartmentalization and activity of nuclear receptors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 06:54:25