Receptor activity-modifying proteins (RAMPs) are single pass membrane proteins initially identified by their ability to determine the pharmacology of the calcitonin receptor-like receptor (CLR), a family B G protein-coupled receptor (GPCR). It is now known that RAMPs can interact with a much wider range of GPCRs. This review considers recent developments on the structure of the complexes formed between the extracellular domains (ECDs) of CLR and RAMP1 or RAMP2 as these provide insights as to how the RAMPs direct ligand binding. The range of RAMP interactions is also considered; RAMPs can interact with numerous family B GPCRs as well as examples of family A and family C GPCRs. They influence receptor expression at the cell surface, trafficking, ligand binding and G protein coupling. The GPCR–RAMP interface offers opportunities for drug targeting, illustrated by examples of drugs developed for migraine.
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April 2016
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Cover Image
Endoplasmic reticulumendosome contact sites. This pseudo-colored electron microscopy image shows the formation of inter-organelle membrane contact sites between late endosomes (magenta) and the endoplasmic reticulum (ER; green). This tethering results from the interaction between two ER-anchored proteins (VAP-A and VAP-B) and the late endosomeanchored protein STARD3NL. Mitochondria: brown; nucleus: blue. For further details see pp. 493-498. Image kindly provided by Fabien Alpy. - PDF Icon PDF LinkTable of Contents
Review Article|
April 11 2016
Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins
Debbie L. Hay;
Debbie L. Hay
1
*School of Biological Sciences, University of Auckland, Auckland 1010, New Zealand
1Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Christopher S. Walker;
Christopher S. Walker
*School of Biological Sciences, University of Auckland, Auckland 1010, New Zealand
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Joseph J. Gingell;
Joseph J. Gingell
*School of Biological Sciences, University of Auckland, Auckland 1010, New Zealand
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Graham Ladds;
Graham Ladds
†Department of Pharmacology, Cambridge University, Cambridge CB2 1PD, U.K.
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Christopher A. Reynolds;
Christopher A. Reynolds
‡School of Biological Sciences, Essex University, Colchester CO4 3SQ, U.K.
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David R. Poyner
David R. Poyner
1
§School of Life and Health Sciences, Aston University, Birmingham B4 7ET, U.K.
1Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Publisher: Portland Press Ltd
Received:
December 15 2015
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2016 Authors; published by Portland Press Limited
2016
Biochem Soc Trans (2016) 44 (2): 568–573.
Article history
Received:
December 15 2015
Citation
Debbie L. Hay, Christopher S. Walker, Joseph J. Gingell, Graham Ladds, Christopher A. Reynolds, David R. Poyner; Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins. Biochem Soc Trans 15 April 2016; 44 (2): 568–573. doi: https://doi.org/10.1042/BST20150237
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