Identification of a novel mechanism of regulation of Ah (dioxin) receptor function

被引：444

作者：

Mimura, J ^{[1
]}

Ema, M ^{[1
]}

Sogawa, K ^{[1
]}

Fujii-Kuriyama, Y ^{[1
]}

机构：

[1] Tohoku Univ, Grad Sch Sci, Dept Chem, Sendai, Miyagi 9808578, Japan

来源：

GENES & DEVELOPMENT | 1999年 / 13卷 / 01期

关键词：

AhR; Arnt; bHLH-PAS; TCDD; XRE;

D O I：

10.1101/gad.13.1.20

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Ah receptor (AhR) is a ligand-activated transcription factor that mediates pleiotropic effects of environmental pollutants such as 2,3,7,8-tetrachlorodibenzo-p-dioxin on host animals. In addition to induction of drug-metabolizing enzymes, the liganded AM complex was found to activate gene expression of a factor designated AhR repressor (AhRR), which inhibits AhR function by competing with AhR for dimerizing with Amt and binding to the XRE sequence. Thus, AhR and AhRR form a regulatory circuit in the xenobiotic signal transduction pathway and provide a novel mechanism of regulation of AhR function that may determine tissue-specific sensitivity to environmental pollutants.

引用

页码：20 / 25

页数：6

共 37 条

[1] MAD - A HETERODIMERIC PARTNER FOR MAX THAT ANTAGONIZES MYC TRANSCRIPTIONAL ACTIVITY [J].

AYER, DE ;

KRETZNER, L ;

EISENMAN, RN .

CELL, 1993, 72 (02) :211-222

[2] A SWITCH FROM MYC-MAX TO MAD-MAX HETEROCOMPLEXES ACCOMPANIES MONOCYTE/MACROPHAGE DIFFERENTIATION [J].

AYER, DE ;

EISENMAN, RN .

GENES & DEVELOPMENT, 1993, 7 (11) :2110-2119

[3] THE PROTEIN ID - A NEGATIVE REGULATOR OF HELIX-LOOP-HELIX DNA-BINDING PROTEINS [J].

BENEZRA, R ;

DAVIS, RL ;

LOCKSHON, D ;

TURNER, DL ;

WEINTRAUB, H .

CELL, 1990, 61 (01) :49-59

[4] AN ID-RELATED HELIX LOOP HELIX PROTEIN ENCODED BY A GROWTH FACTOR-INDUCIBLE GENE [J].

CHRISTY, BA ;

SANDERS, LK ;

LAU, LF ;

COPELAND, NG ;

JENKINS, NA ;

NATHANS, D .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (05) :1815-1819

[5] INTRACELLULAR LEUCINE ZIPPER INTERACTIONS SUGGEST C-MYC HETERO-OLIGOMERIZATION [J].

DANG, CV ;

BARRETT, J ;

VILLAGARCIA, M ;

RESAR, LMS ;

KATO, GJ ;

FEARON, ER .

MOLECULAR AND CELLULAR BIOLOGY, 1991, 11 (02) :954-962

[6] CDNA CLONING AND STRUCTURE OF MOUSE PUTATIVE AH RECEPTOR [J].

EMA, M ;

SOGAWA, K ;

WATANABE, N ;

CHUJOH, Y ;

MATSUSHITA, N ;

GOTOH, O ;

FUNAE, Y ;

FUJIIKURIYAMA, Y .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1992, 184 (01) :246-253

[7] Aryl-hydrocarbon receptor-deficient mice are resistant to 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced toxicity [J].

FernandezSalguero, PM ;

Hilbert, DM ;

Rudikoff, S ;

Ward, JM ;

Gonzalez, FJ .

TOXICOLOGY AND APPLIED PHARMACOLOGY, 1996, 140 (01) :173-179

[8] CHARACTERIZATION OF XENOBIOTIC RESPONSIVE ELEMENTS UPSTREAM FROM THE DRUG-METABOLIZING CYTOCHROME P-450C GENE - A SIMILARITY TO GLUCOCORTICOID REGULATORY ELEMENTS [J].

FUJISAWASEHARA, A ;

SOGAWA, K ;

YAMANE, M ;

FUJIIKURIYAMA, Y .

NUCLEIC ACIDS RESEARCH, 1987, 15 (10) :4179-4191

[9] Role of the CLOCK protein in the mammalian circadian mechanism [J].

Gekakis, N ;

Staknis, D ;

Nguyen, HB ;

Davis, FC ;

Wilsbacher, LD ;

King, DP ;

Takahashi, JS ;

Weitz, CJ .

SCIENCE, 1998, 280 (5369) :1564-1569

[10] THE ARYL-HYDROCARBON RECEPTOR COMPLEX [J].

HANKINSON, O .

ANNUAL REVIEW OF PHARMACOLOGY AND TOXICOLOGY, 1995, 35 :307-340

← 1 2 3 4 →