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蚂蚁两两前行:G蛋白偶联受体的寡聚体结构

The ants go marching two by two: oligomeric structure of G-protein-coupled receptors.

作者信息

Javitch Jonathan A

机构信息

Center for Molecular Recognition, Department of Psychiatry, Columbia University, P&S 11-401, 630 W. 168th Street, New York, NY 10032, USA.

出版信息

Mol Pharmacol. 2004 Nov;66(5):1077-82. doi: 10.1124/mol.104.006320. Epub 2004 Aug 19.

DOI:10.1124/mol.104.006320
PMID:15319448
Abstract

A number of class C G-protein coupled receptors (GPCRs) have been shown to form dimers in the plasma membrane, and mounting evidence supports the hypothesis that many, if not all, class A rhodopsin-like receptors also form dimers or higher-order oligomers. Evidence for this hypothesis has come from SDS-polyacrylamide gel electrophoresis, coimmunoprecipitation, resonance energy transfer, atomic force microscopy, and cross-linking studies, approaches that are reviewed in this article. Like any method, each has its strengths and limitations, and these must be kept in mind when interpreting the data for oligomerization. Recent experimental evidence supports the hypothesis that class A receptors may exist as higher-order oligomers, or even as arrays, with distinct symmetrical interfaces in both the first and fourth transmembrane segments.

摘要

许多C类G蛋白偶联受体(GPCR)已被证明能在质膜中形成二聚体,越来越多的证据支持这样一种假说:即便不是全部,许多A类视紫红质样受体也会形成二聚体或更高阶的寡聚体。这一假说的证据来自SDS聚丙烯酰胺凝胶电泳、免疫共沉淀、共振能量转移、原子力显微镜和交联研究,本文将对这些方法进行综述。与任何方法一样,每种方法都有其优点和局限性,在解释寡聚化数据时必须牢记这些。最近的实验证据支持这样的假说:A类受体可能以更高阶的寡聚体形式存在,甚至以阵列形式存在,在第一和第四跨膜段具有独特的对称界面。

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