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 journalReview articlepeer-review

33 Citations (Scopus)


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 languageEnglish
Pages (from-to)568-573
Number of pages6
JournalBiochemical Society Transactions
Issue number2
Publication statusPublished - 11 Apr 2016
Externally publishedYes


  • Adrenomedullin
  • Amylin
  • Calcitonin gene-related peptide (CGRP)
  • Calcitonin receptor
  • Calcitonin receptor-like receptor
  • Family B G protein-coupled receptor
  • Receptor activity-modifying protein (RAMP)

ASJC Scopus subject areas

  • Biochemistry


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