ArticleBiochimica et biophysica acta2008
Dimerization in the absence of higher-order oligomerization of the G protein-coupled secretin receptor.
Article in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- Secretin Receptor as a Target in Gastrointestinal Cancer: Expression Analysis and Ligand Development.Biomedicines · 2022Article
- The Class-A GPCR Dopamine D2 Receptor Forms Transient Dimers Stabilized by Agonists: Detection by Single-Molecule Tracking.Cell biochemistry and biophysics · 2018Article
- Spatial Intensity Distribution Analysis: Studies of G Protein-Coupled Receptor Oligomerisation.Trends in pharmacological sciences · 2018Review
- Spatial intensity distribution analysis quantifies the extent and regulation of homodimerization of the secretin receptor.The Biochemical journal · 2017Article
- Structure and Function of Cross-class Complexes of G Protein-coupled Secretin and Angiotensin 1a Receptors.The Journal of biological chemistry · 2016Article
- Structure and function of Norrin in assembly and activation of a Frizzled 4-Lrp5/6 complex.Genes & development · 2013Article
- Fluorescence correlation spectroscopy analysis of serotonin, adrenergic, muscarinic, and dopamine receptor dimerization: the oligomer number puzzle.Molecular pharmacology · 2013Article
- Emerging paradigms in GPCR allostery: implications for drug discovery.Nature reviews. Drug discovery · 2013Review
- A novel approach to quantify G-protein-coupled receptor dimerization equilibrium using bioluminescence resonance energy transfer.Methods in molecular biology (Clifton, N.J.) · 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
- Oligomer size of the serotonin 5-hydroxytryptamine 2C (5-HT2C) receptor revealed by fluorescence correlation spectroscopy with photon counting histogram analysis: evidence for homodimers without monomers or tetramers.The Journal of biological chemistry · 2012Article
- Ligand binding and activation of the secretin receptor, a prototypic family B G protein-coupled receptor.British journal of pharmacology · 2012Review
- Consequences of splice variation on Secretin family G protein-coupled receptor function.British journal of pharmacology · 2012Review
- Differential determinants for coupling of distinct G proteins with the class B secretin receptor.American journal of physiology. Cell physiology · 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
- BRET biosensors to study GPCR biology, pharmacology, and signal transduction.Frontiers in endocrinology · 2012Article
- Receptor oligomerization: from early evidence to current understanding in class B GPCRs.Frontiers in endocrinology · 2012Article
- FRET in Membrane Biophysics: An Overview.Frontiers in physiology · 2011Article
- Importance of lipid-exposed residues in transmembrane segment four for family B calcitonin receptor homo-dimerization.Regulatory peptides · 2010Article
- Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery.Pharmacological reviews · 2010Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Oligomerization of G protein-coupled receptors has been proposed to affect receptor function and regulation; however, little is known about the molecular nature of such complexes. We previously utilized bioluminescence resonance energy transfer (BRET) to demonstrate that the prototypic Family B secretin receptor can form oligomers. We now explore the order of oligomerization present utilizing unique bimolecular fluorescence complementation and energy transfer techniques. The non-fluorescent carboxyl-terminal and amino-terminal halves of yellow fluorescent protein (YFP) were fused to the carboxyl terminus of the secretin receptor. These constructs bound secretin normally and signaled in response to secretin like wild type receptor. When co-expressed on COS cells, these constructs physically interacted to yield typical YFP fluorescence in biosynthetic compartments and at the plasma membrane, reflecting receptor homo-dimerization. However, the addition of another potential partner in form of Rlu- or CFP-tagged secretin receptor yielded no significant BRET or FRET signal, respectively, under conditions in which intact YFP-tagged secretin receptor yielded such a signal. Absence of higher-order receptor oligomers was further confirmed using saturation BRET techniques. Absence of significant resonance transfer to the secretin receptor homo-dimer was true for carboxyl-terminally-tagged secretin receptor, as well as for receptor incorporating the transfer partner into each of the three distinct intracellular loop domains. These results suggest that the secretin receptor can exist only as a structurally-specific homo-dimer, without being present as higher-order oligomers.
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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.