Modulating receptor function through RAMPs: can they represent drug targets in themselves?

Patrick M Sexton, David R Poyner, John Simms, Arthur Christopoulos, Debbie L Hay

Research output: Contribution to journalReview article

53 Citations (Scopus)

Abstract

G protein-coupled receptors (GPCRs) are successfully exploited as drug targets. As our understanding of how distinct GPCR subtypes can be generated expands, so do possibilities for therapeutic intervention via these receptors. Receptor activity-modifying proteins (RAMPs) are excellent examples of proteins that enhance diversity in GPCR function. They facilitate the creation of binding pockets, controlling the pharmacology of some GPCRs. Moreover, they have the ability to regulate cell-surface trafficking, internalisation and signalling of GPCRs, creating novel opportunities for drug discovery. RAMPs could be directly targeted by drugs, or advantage could be taken of unique RAMP/GPCR interfaces for generating highly selective ligands.

Original languageEnglish
Pages (from-to)413-419
Number of pages7
JournalDrug Discovery Today
Volume14
Issue number7-8
DOIs
Publication statusPublished - Apr 2009

Fingerprint

Receptor Activity-Modifying Proteins
G-Protein-Coupled Receptors
Pharmaceutical Preparations
Drug Discovery
Pharmacology
Ligands

Keywords

  • Animals
  • Binding Sites
  • Drug Delivery Systems
  • Drug Design
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Molecular Structure
  • Protein Binding
  • Protein Transport
  • Receptor Activity-Modifying Proteins
  • Receptors, G-Protein-Coupled
  • Signal Transduction
  • Journal Article
  • Review

Cite this

Modulating receptor function through RAMPs : can they represent drug targets in themselves? / Sexton, Patrick M; Poyner, David R; Simms, John; Christopoulos, Arthur; Hay, Debbie L.

In: Drug Discovery Today, Vol. 14, No. 7-8, 04.2009, p. 413-419.

Research output: Contribution to journalReview article

Sexton, PM, Poyner, DR, Simms, J, Christopoulos, A & Hay, DL 2009, 'Modulating receptor function through RAMPs: can they represent drug targets in themselves?' Drug Discovery Today, vol. 14, no. 7-8, pp. 413-419. https://doi.org/10.1016/j.drudis.2008.12.009
Sexton, Patrick M ; Poyner, David R ; Simms, John ; Christopoulos, Arthur ; Hay, Debbie L. / Modulating receptor function through RAMPs : can they represent drug targets in themselves?. In: Drug Discovery Today. 2009 ; Vol. 14, No. 7-8. pp. 413-419.
@article{8937efe14f7347049ddfd243399d4ed9,
title = "Modulating receptor function through RAMPs: can they represent drug targets in themselves?",
abstract = "G protein-coupled receptors (GPCRs) are successfully exploited as drug targets. As our understanding of how distinct GPCR subtypes can be generated expands, so do possibilities for therapeutic intervention via these receptors. Receptor activity-modifying proteins (RAMPs) are excellent examples of proteins that enhance diversity in GPCR function. They facilitate the creation of binding pockets, controlling the pharmacology of some GPCRs. Moreover, they have the ability to regulate cell-surface trafficking, internalisation and signalling of GPCRs, creating novel opportunities for drug discovery. RAMPs could be directly targeted by drugs, or advantage could be taken of unique RAMP/GPCR interfaces for generating highly selective ligands.",
keywords = "Animals, Binding Sites, Drug Delivery Systems, Drug Design, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Molecular Structure, Protein Binding, Protein Transport, Receptor Activity-Modifying Proteins, Receptors, G-Protein-Coupled, Signal Transduction, Journal Article, Review",
author = "Sexton, {Patrick M} and Poyner, {David R} and John Simms and Arthur Christopoulos and Hay, {Debbie L}",
year = "2009",
month = "4",
doi = "10.1016/j.drudis.2008.12.009",
language = "English",
volume = "14",
pages = "413--419",
journal = "Drug Discovery Today",
issn = "1359-6446",
publisher = "Elsevier",
number = "7-8",

}

TY - JOUR

T1 - Modulating receptor function through RAMPs

T2 - can they represent drug targets in themselves?

AU - Sexton, Patrick M

AU - Poyner, David R

AU - Simms, John

AU - Christopoulos, Arthur

AU - Hay, Debbie L

PY - 2009/4

Y1 - 2009/4

N2 - G protein-coupled receptors (GPCRs) are successfully exploited as drug targets. As our understanding of how distinct GPCR subtypes can be generated expands, so do possibilities for therapeutic intervention via these receptors. Receptor activity-modifying proteins (RAMPs) are excellent examples of proteins that enhance diversity in GPCR function. They facilitate the creation of binding pockets, controlling the pharmacology of some GPCRs. Moreover, they have the ability to regulate cell-surface trafficking, internalisation and signalling of GPCRs, creating novel opportunities for drug discovery. RAMPs could be directly targeted by drugs, or advantage could be taken of unique RAMP/GPCR interfaces for generating highly selective ligands.

AB - G protein-coupled receptors (GPCRs) are successfully exploited as drug targets. As our understanding of how distinct GPCR subtypes can be generated expands, so do possibilities for therapeutic intervention via these receptors. Receptor activity-modifying proteins (RAMPs) are excellent examples of proteins that enhance diversity in GPCR function. They facilitate the creation of binding pockets, controlling the pharmacology of some GPCRs. Moreover, they have the ability to regulate cell-surface trafficking, internalisation and signalling of GPCRs, creating novel opportunities for drug discovery. RAMPs could be directly targeted by drugs, or advantage could be taken of unique RAMP/GPCR interfaces for generating highly selective ligands.

KW - Animals

KW - Binding Sites

KW - Drug Delivery Systems

KW - Drug Design

KW - Humans

KW - Intracellular Signaling Peptides and Proteins

KW - Membrane Proteins

KW - Molecular Structure

KW - Protein Binding

KW - Protein Transport

KW - Receptor Activity-Modifying Proteins

KW - Receptors, G-Protein-Coupled

KW - Signal Transduction

KW - Journal Article

KW - Review

U2 - 10.1016/j.drudis.2008.12.009

DO - 10.1016/j.drudis.2008.12.009

M3 - Review article

VL - 14

SP - 413

EP - 419

JO - Drug Discovery Today

JF - Drug Discovery Today

SN - 1359-6446

IS - 7-8

ER -