Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins

Debbie L. Hay; Christopher S. Walker; Joseph J. Gingell; Graham Ladds; Christopher A. Reynolds; David R. Poyner

doi:10.1042/BST20150237

Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins

Debbie L. Hay, Christopher S. Walker, Joseph J. Gingell, Graham Ladds, Christopher A. Reynolds, David R. Poyner

Research output: Contribution to journal › Review article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	568-573
Number of pages	6
Journal	Biochemical Society Transactions
Volume	44
Issue number	2
Early online date	11 Apr 2016
DOIs	https://doi.org/10.1042/BST20150237
Publication status	Published - 15 Apr 2016

Bibliographical note

This is not the final peer-reviewed Version of Record; Hay, D. L., Walker, C. S., Gingell, J. J., Ladds, G., Reynolds, C. A., & Poyner, D. R. (2016). Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins. Biochemical Society Transactions, 44(2), 568-673. http://dx.doi.org/10.1042/BST20150237

Keywords

adrenomedullin
amylin
calcitonin gene-related peptide (CGRP)
calcitonin receptor
calcitonin receptor-like receptor
family B G protein-coupled receptor
receptor activity-modifying protein (RAMP)

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10.1042/BST20150237

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title = "Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins",

abstract = "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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note = "This is not the final peer-reviewed Version of Record; Hay, D. L., Walker, C. S., Gingell, J. J., Ladds, G., Reynolds, C. A., & Poyner, D. R. (2016). Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins. Biochemical Society Transactions, 44(2), 568-673. http://dx.doi.org/10.1042/BST20150237",

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AU - Ladds, Graham

AU - Reynolds, Christopher A.

AU - Poyner, David R.

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N2 - 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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Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins

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Bibliographical note

Keywords

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