ArticleBritish journal of pharmacology2014
Receptor activity-modifying protein-dependent effects of mutations in the calcitonin receptor-like receptor: implications for adrenomedullin and calcitonin gene-related peptide pharmacology.
Article in British journal of pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Adrenomedullin 2/intermedin is a slow off-rate, long-acting endogenous agonist of the adrenomedullinbioRxiv : the preprint server for biology · 2023Article
- Novel Fluorescently Labeled PACAP and VIP Highlight Differences between Peptide Internalization and Receptor Pharmacology.ACS pharmacology & translational science · 2023Article
- Molecular interaction of an antagonistic amylin analog with the extracellular domain of receptor activity-modifying protein 2 assessed by fluorescence polarization.Biophysical chemistry · 2020Article
- Discovery of a First-in-Class Potent Small Molecule Antagonist against the Adrenomedullin-2 Receptor.ACS pharmacology & translational science · 2020Article
- Agonist bias and agonist-dependent antagonism at corticotrophin releasing factor receptors.Pharmacology research & perspectives · 2020Article
- Structure and Dynamics of Adrenomedullin Receptors AMACS pharmacology & translational science · 2020Article
- Molecular Mechanisms of Class B GPCR Activation: Insights from Adrenomedullin Receptors.ACS pharmacology & translational science · 2020Article
- RAMPs as allosteric modulators of the calcitonin and calcitonin-like class B G protein-coupled receptors.Advances in pharmacology (San Diego, Calif.) · 2020Review
- Molecular Signature for Receptor Engagement in the Metabolic Peptide Hormone Amylin.ACS pharmacology & translational science · 2018Article
- GPCR Modulation of Thieno[2,3-b]pyridine Anti-Proliferative Agents.Molecules (Basel, Switzerland) · 2017Article
- Receptor activity-modifying protein dependent and independent activation mechanisms in the coupling of calcitonin gene-related peptide and adrenomedullin receptors to Gs.Biochemical pharmacology · 2017Article
- Haplotype-based, case-control study of the receptor (calcitonin) activity-modifying protein (RAMP) 1 gene in essential hypertension.Journal of human hypertension · 2017Article
- Cardiovascular effects of exogenous adrenomedullin and CGRP in Ramp and Calcrl deficient mice.Peptides · 2017Article
- Loss of receptor activity-modifying protein 2 in mice causes placental dysfunction and alters PTH1R regulation.PloS one · 2017Article
- Receptor Activity-modifying Protein-directed G Protein Signaling Specificity for the Calcitonin Gene-related Peptide Family of Receptors.The Journal of biological chemistry · 2016Article
- Receptor Activity-modifying Proteins 2 and 3 Generate Adrenomedullin Receptor Subtypes with Distinct Molecular Properties.The Journal of biological chemistry · 2016Article
- Receptor Activity-Modifying Proteins (RAMPs): New Insights and Roles.Annual review of pharmacology and toxicology · 2016Review
- Modulation of Glucagon Receptor Pharmacology by Receptor Activity-modifying Protein-2 (RAMP2).The Journal of biological chemistry · 2015Article
- Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor.Molecular cell · 2015Article
- Intrathecal Amylin and Salmon Calcitonin Affect Formalin Induced c-Fos Expression in the Spinal Cord of Rats.Iranian journal of medical sciences · 2014Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
background and purposeReceptor activity-modifying proteins (RAMPs) define the pharmacology of the calcitonin receptor-like receptor (CLR). The interactions of the different RAMPs with this class B GPCR yield high-affinity calcitonin gene-related peptide (CGRP) or adrenomedullin (AM) receptors. However, the mechanism for this is unclear. EXPERIMENTAL APPROACH: Guided by receptor models, we mutated residues in the N-terminal helix of CLR, RAMP2 and RAMP3 hypothesized to be involved in peptide interactions. These were assayed for cAMP production with AM, AM2 and CGRP together with their cell surface expression. Binding studies were also conducted for selected mutants. KEY
resultsAn important domain for peptide interactions on CLR from I32 to I52 was defined. Although I41 was universally important for binding and receptor function, the role of other residues depended on both ligand and RAMP. Peptide binding to CLR/RAMP3 involved a more restricted range of residues than that to CLR/RAMP1 or CLR/RAMP2. E101 of RAMP2 had a major role in AM interactions, and F111/W84 of RAMP2/3 was important with each peptide. CONCLUSIONS AND IMPLICATIONS: RAMP-dependent effects of CLR mutations suggest that the different RAMPs control accessibility of peptides to binding residues situated on the CLR N-terminus. RAMP3 appears to alter the role of specific residues at the CLR-RAMP interface compared with RAMP1 and RAMP2.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.