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G蛋白偶联受体辅助蛋白的受体活性修饰蛋白家族。

The receptor activity modifying protein family of G protein coupled receptor accessory proteins.

作者信息

Udawela Madhara, Hay Debbie L, Sexton Patrick M

机构信息

Molecular Pharmacology Group, Howard Florey Institute, The University of Melbourne, Gate 11, Royal Parade, Melbourne, Vic. 3010, Australia.

出版信息

Semin Cell Dev Biol. 2004 Jun;15(3):299-308. doi: 10.1016/j.semcdb.2003.12.019.

Abstract

Receptor diversity for the calcitonin peptide family is created by the interaction of two 7-transmembrane proteins--the calcitonin receptor (CTR) or the calcitonin receptor-like receptor (CL-R)--with the receptor activity modifying protein (RAMP) family. The discovery of heterodimeric complexes of these proteins heralded a new era in the study of G protein coupled receptors (GPCRs), whereby receptor phenotype is no longer governed by just the GPCR. In this article, recent advances in the study of RAMPs are discussed--from our current understanding of the molecular basis of RAMP-receptor interaction to a broader role for RAMPs outside the calcitonin receptor family.

摘要

降钙素肽家族的受体多样性是由两种7跨膜蛋白——降钙素受体(CTR)或降钙素受体样受体(CL-R)——与受体活性修饰蛋白(RAMP)家族相互作用产生的。这些蛋白异二聚体复合物的发现开创了G蛋白偶联受体(GPCR)研究的新纪元,即受体表型不再仅由GPCR决定。本文讨论了RAMP研究的最新进展——从我们目前对RAMP-受体相互作用分子基础的理解到RAMP在降钙素受体家族之外更广泛的作用。

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