The role of chaperone proteins in the aryl hydrocarbon receptor core complex
The role of chaperone proteins in the aryl hydrocarbon receptor core complex
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DOI：
10.1016/s0009-2797(02)00064-9
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发表时间：
2002-09-20
影响因子：
5.1
通讯作者：
Perdew, GH
中科院分区：
文献类型：
--
作者：
Petrulis, JR;Perdew, GH
芳烃受体（AhR）在不存在配体的情况下作为由95-105 kDa配体结合亚基、hsp 90的二聚体和亲免疫素样X相关蛋白2（XAP 2）组成的四聚体复合物存在。XAP 2具有高度保守的羧基末端三肽重复结构域，其是hsp 90和AhR结合所需的。热休克蛋白90似乎参与了新合成的AhR的初始折叠，稳定受体的配体结合构象，并抑制ARNT的组成性二聚化。XAP 2能够稳定AhR，以及增强受体的细胞质定位。XAP 2结合受体复合物中的AhR和hsp 90两者，并且能够独立地结合hsp 90和AhR两者。然而，XAP 2在AhR复合物中的确切功能作用仍有待完全确定。(C)2002爱思唯尔科学爱尔兰有限公司保留所有权利。
The aryl hydrocarbon receptor (AhR) exists in the absence of a ligand as a tetrameric complex composed of a 95-105 kDa ligand binding subunit, a dimer of hsp90, and the immunophilin-like X-associated protein 2 (XAP2). XAP2 has a highly conserved carboxy terminal tetratricopeptide repeat domain that is required for both hsp90 and AhR binding. Hsp 90 appears to be involved in the initial folding of newly synthesized AhR, stabilization of ligand binding conformation of the receptor, and inhibition of constitutive dimerization with ARNT. XAP2 is capable of stabilizing the AhR, as well as enhancing cytoplasmic localization of the receptor. XAP2 binds to both the AhR and hsp90 in the receptor complex, and is capable of independently binding to both hsp90 and the AhR. However, the exact functional role for XAP2 in the AhR complex remains to be fully established. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.