The role of dimerisation in the cellular trafficking of G-protein-coupled receptors

被引：84

作者：

Milligan, Graeme ^{[1
]}

机构：

[1] Univ Glasgow, Mol Pharmacol Grp, Fac Biomed & Life Sci, Glasgow G12 8QQ, Lanark, Scotland

来源：

CURRENT OPINION IN PHARMACOLOGY | 2010年 / 10卷 / 01期

基金：

英国医学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

RESONANCE ENERGY-TRANSFER; SECRETIN RECEPTOR; ENDOPLASMIC-RETICULUM; PLASMA-MEMBRANE; PHARMACOLOGICAL CHAPERONES; HETERO-OLIGOMERIZATION; SURFACE DELIVERY; HETERODIMERIZATION; ACTIVATION; HOMODIMERIZATION;

D O I：

10.1016/j.coph.2009.09.010

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

The concept that G-protein-coupled receptors can exist as homomeric and/or heteromeric complexes is now well established. Despite this, how dynamic such interactions are and if this may be modulated during receptor trafficking remain topics of debate. Use of endoplasmic reticulum trapping strategies and the generation of asymmetric homomers have started to provide information on the contribution of protein-protein interactions to receptor maturation, cell surface delivery and ligand-mediated endocytosis. Although dimer/oligomer formation appears to be essential for cell surface delivery of class A and class C GPCRs, this may not be the case for class B receptors.

引用

页码：23 / 29

页数：7

共 53 条

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