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Receptor Activity-Modifying Proteins Differentially Modulate the G Protein-Coupling Efficiency of Amylin Receptors
Open accessAbstract
Receptor activity-modifying proteins (RAMPs) 1, 2, and 3 are prototypic G protein-coupled receptor accessory proteins that can alter not only receptor trafficking but also receptor phenotype. Specific RAMP interaction with the calcitonin receptor (CTR) generates novel and distinct receptors for the peptide amylin; however, the role of RAMPs in receptor signaling is not understood. The current study demonstrates that RAMP interaction with the CTRa in COS-7 or HEK-293 cells leads to selective modulation of signaling pathways activated by the receptor complex. There was a 20- to 30-fold induction in amylin potency at CTR/RAMP1 (AMY1) and CTR/RAMP3 (AMY3) receptors, compared with CTR alone, for formation of the second-messenger cAMP that parallels an increase in amylin binding affinity. In contrast, only 2- to 5-fold induction of amylin potency was seen for mobilization of intracellular Ca++ or activation of ERK1/2. In addition, in COS-7 cells, the increase in amylin potency for Ca++ mobilization was 2-fold greater for AMY3 receptors, compared with AMY1 receptors and this paralleled the relative capacity of overexpression of Gαq proteins to augment induction of high affinity 125I-amylin binding. These data demonstrate that RAMP-complexed receptors have a different signaling profile to CTRs expressed in the absence of RAMPs, and this is likely due to direct effects of the RAMP on G protein-coupling efficiency.
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“4) Signaling: studies of the amylin receptors (AMY 1-3 ) found that downstream signaling pathways of intracellular calcium production depend on the specific interacting RAMP and suggested that RAMP-complexed receptors have a different signaling profile to that of CTR expressed in the absence of RAMPs (152).”
From The Activity of Peptides of the Calcitonin Family in Bone (2019) · cites this paper as [152]
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RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
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Metadata
- Authors
- Morfis, M., Tilakaratne, N., Furness, S. G. B., Christopoulos, G., Werry, T. D., Christopoulos, A., & Sexton, P. M.
- Affiliations
- The University of Melbourne (AU)
- Monash University (AU)
- Corresponding author
- Sexton, Patrick M.
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2008-07-03
- Volume
- 149
- Issue
- 11
- Pages
- 5423-5431
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- OpenAlex
- W2101979449
- Semantic Scholar
- 2ad08a2ccb8e57ba63eab72d9571651ccbdaf556
- Cited by
- 134
- References
- 23
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 2 · 2023: 8 · 2022: 5 · 2021: 12 · 2020: 11 · 2019: 7 · 2018: 4 · 2017: 10 · 2016: 12 · 2015: 11 · 2014: 4 · 2013: 7 · 2012: 11
- FWCI
- 3.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Monash University Research Portal (Monash University) (submittedVersion, other-oa)
- Funders
- Bristol-Myers Squibb
- GlaxoSmithKline
- Monash University
- Medical Research Council
- National Health and Medical Research Council (299810, 436781)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Keywords
- receptor activity-modifying proteins, RAMP1, RAMP3, RAMP2, amylin receptor, calcitonin receptor, cAMP signaling, calcium mobilization, ERK1/2 activation, Gαq
- MeSH terms
- Cyclic AMP, Amyloid, Animals, Chlorocebus aethiops, Humans, Membrane Proteins, Protein Binding, Signal Transduction, Receptors, Peptide, Receptors, Calcitonin, GTP-Binding Proteins, COS Cells, Receptors, G-Protein-Coupled, Intracellular Signaling Peptides and Proteins, Rats, Islet Amyloid Polypeptide, Receptor Activity-Modifying Proteins, Receptor Activity-Modifying Protein 1, Receptor Activity-Modifying Protein 3, Receptors, Islet Amyloid Polypeptide
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