ArticleJournal of molecular neuroscience : MN2008
Pattern of intra-family hetero-oligomerization involving the G-protein-coupled secretin receptor.
Article in Journal of molecular neuroscience : MN, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Impact of secretin receptor homo-dimerization on natural ligand binding.Nature communications · 2024Article
- Angiotensin and Endothelin Receptor Structures With Implications for Signaling Regulation and Pharmacological Targeting.Frontiers in endocrinology · 2022Review
- Identification of the Ghrelin and Cannabinoid CBInternational journal of molecular sciences · 2021Article
- DR10601, a novel recombinant long-acting dual glucagon-like peptide-1 and glucagon receptor agonist for the treatment of obesity and type 2 diabetes mellitus.Journal of endocrinological investigation · 2020Article
- Structural Basis for Allosteric Modulation of Class B G Protein-Coupled Receptors.Annual review of pharmacology and toxicology · 2020Review
- Oligomeric Receptor Complexes and Their Allosteric Receptor-Receptor Interactions in the Plasma Membrane Represent a New Biological Principle for Integration of Signals in the CNS.Frontiers in molecular neuroscience · 2019Article
- Structural-Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at Work.Frontiers in endocrinology · 2017Review
- Functional consequences of glucagon-like peptide-1 receptor cross-talk and trafficking.The Journal of biological chemistry · 2015Article
- Oligomerization of Family B GPCRs: Exploration in Inter-Family Oligomer Formation.Frontiers in endocrinology · 2015Review
- Structure and function of LGR5: an enigmatic G-protein coupled receptor marking stem cells.Protein science : a publication of the Protein Society · 2014Review
- Molecular mechanisms underlying physiological and receptor pleiotropic effects mediated by GLP-1R activation.British journal of pharmacology · 2014Review
- Structure and function of Norrin in assembly and activation of a Frizzled 4-Lrp5/6 complex.Genes & development · 2013Article
- Alternative Splicing of the Pituitary Adenylate Cyclase-Activating Polypeptide Receptor PAC1: Mechanisms of Fine Tuning of Brain Activity.Frontiers in endocrinology · 2013Article
- Glucagon-like peptide-1 receptor dimerization differentially regulates agonist signaling but does not affect small molecule allostery.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs?British journal of pharmacology · 2012Review
- Ligand binding and activation of the secretin receptor, a prototypic family B G protein-coupled receptor.British journal of pharmacology · 2012Review
- Structure and mechanism for recognition of peptide hormones by Class B G-protein-coupled receptors.Acta pharmacologica Sinica · 2012Review
- Receptor oligomerization: from early evidence to current understanding in class B GPCRs.Frontiers in endocrinology · 2012Article
- Receptor oligomerization in family B1 of G-protein-coupled receptors: focus on BRET investigations and the link between GPCR oligomerization and binding cooperativity.Frontiers in endocrinology · 2012Article
- Regulation of GIP and GLP1 receptor cell surface expression by N-glycosylation and receptor heteromerization.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Oligomerization of G-protein-coupled receptors (GPCRs) is emerging as a mechanism for regulation and functional modification, although it has been studied most extensively for Family A receptors. Family B receptors have clear structural differences from Family A. In this paper, we have systematically evaluated GPCRs that are capable of association with the prototypic Family B secretin receptor. All of the receptor constructs were shown to traffic normally to the plasma membrane. We utilized receptor bioluminescence resonance energy transfer (BRET) to determine the presence of constitutive and ligand-dependent receptor association. Extensive intra-family and no cross-family association was observed. Of the nine Family B receptors studied, all constitutively yielded a significant BRET signal with the secretin receptor, except for the calcitonin receptor. Each of the associating hetero-oligomeric receptor pairs generated a BRET signal of similar intensity, less than that of homo-oligomeric secretin receptors. BRET signals from some receptor pairs were reduced by ligand occupation, but none were increased by this treatment. Thus, Family B GPCR oligomerization occurs, with many structurally related members associating with each other. The specific functional implications of this need to be further evaluated.
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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.