Author
Listed:
- Linda M. McLatchie
(Receptor Systems and Cell Biology Units, GlaxoWellcome Medicines Research Centre
The Novartis Institute for Medical Sciences)
- Neil J. Fraser
(Receptor Systems and Cell Biology Units, GlaxoWellcome Medicines Research Centre)
- Martin J. Main
(Receptor Systems and Cell Biology Units, GlaxoWellcome Medicines Research Centre)
- Alan Wise
(Receptor Systems and Cell Biology Units, GlaxoWellcome Medicines Research Centre)
- Jason Brown
(Receptor Systems and Cell Biology Units, GlaxoWellcome Medicines Research Centre)
- Nicola Thompson
(Receptor Systems and Cell Biology Units, GlaxoWellcome Medicines Research Centre)
- Roberto Solari
(Receptor Systems and Cell Biology Units, GlaxoWellcome Medicines Research Centre)
- Melanie G. Lee
(Receptor Systems and Cell Biology Units, GlaxoWellcome Medicines Research Centre)
- Steven M. Foord
(Receptor Systems and Cell Biology Units, GlaxoWellcome Medicines Research Centre)
Abstract
Calcitonin-gene-related peptide (CGRP) and adrenomedullin are related peptides with distinct pharmacological profiles. Here we show that a receptor with seven transmembrane domains, the calcitonin-receptor-like receptor (CRLR), can function as either a CGRP receptor or an adrenomedullin receptor, depending on which members of a new family of single-transmembrane-domain proteins, which we have called receptor-activity-modifying proteins or RAMPs, are expressed. RAMPs are required to transport CRLR to the plasma membrane. RAMP1 presents the receptor at the cell surface as a mature glycoprotein and a CGRP receptor. RAMP2-transported receptors are core-glycosylated and are adrenomedullin receptors.
Suggested Citation
Linda M. McLatchie & Neil J. Fraser & Martin J. Main & Alan Wise & Jason Brown & Nicola Thompson & Roberto Solari & Melanie G. Lee & Steven M. Foord, 1998.
"RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor,"
Nature, Nature, vol. 393(6683), pages 333-339, May.
Handle:
RePEc:nat:nature:v:393:y:1998:i:6683:d:10.1038_30666
DOI: 10.1038/30666
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