ArticleThe Journal of biological chemistry2009
Bioluminescence resonance energy transfer studies reveal constitutive dimerization of the human lutropin receptor and a lack of correlation between receptor activation and the propensity for dimerization.
Article in The Journal of biological chemistry, 2009. 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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Who cites it
28 citing papers in PubMed, 61 citations in OpenAlex.
- Conformational equilibria in the activation of cystine-knot hormone receptors.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structure of an LGR dimer, an evolutionary predecessor of glycoprotein hormone receptors.Nature communications · 2025Article
- Mechanistic insight into how gonadotropin hormone receptor complexes direct signaling†.Biology of reproduction · 2020Review
- Molecular and functional insights into gonadotropin hormone receptor dimerization and oligomerization.Minerva ginecologica · 2018Review
- Temporal reprogramming of calcium signalling via crosstalk of gonadotrophin receptors that associate as functionally asymmetric heteromers.Scientific reports · 2018Article
- Identification of danthron as an isoform-specific inhibitor of HEME OXYGENASE-1/cytochrome P450 reductase interaction with anti-tumor activity.Journal of biomedical science · 2018Article
- Misfolding Ectodomain Mutations of the Lutropin Receptor Increase Efficacy of Hormone Stimulation.Molecular endocrinology (Baltimore, Md.) · 2016Article
- Single-molecule analyses of fully functional fluorescent protein-tagged follitropin receptor reveal homodimerization and specific heterodimerization with lutropin receptor.Biology of reproduction · 2015Article
- Discovery and Development of Small Molecule Allosteric Modulators of Glycoprotein Hormone Receptors.Frontiers in endocrinology · 2015Review
- Crystal structure of a TSH receptor monoclonal antibody: insight into Graves' disease pathogenesis.Molecular endocrinology (Baltimore, Md.) · 2015Article
- ER reorganization is remarkably induced in COS-7 cells accumulating transmembrane protein receptors not competent for export from the endoplasmic reticulum.The Journal of membrane biology · 2014Article
- Mutations in G protein-coupled receptors that impact receptor trafficking and reproductive function.Molecular and cellular endocrinology · 2014Review
- Novel insights on thyroid-stimulating hormone receptor signal transduction.Endocrine reviews · 2013Review
- Heterodimerization between the lutropin and follitropin receptors is associated with an attenuation of hormone-dependent signaling.Endocrinology · 2013Article
- The roles played by highly truncated splice variants of G protein-coupled receptors.Journal of molecular signaling · 2012Article
- Revisiting and questioning functional rescue between dimerized LH receptor mutants.Molecular endocrinology (Baltimore, Md.) · 2012Article
- Setting Up a Bioluminescence Resonance Energy Transfer High throughput Screening Assay to Search for Protein/Protein Interaction Inhibitors in Mammalian Cells.Frontiers in endocrinology · 2012Article
- LH and hCG action on the same receptor results in quantitatively and qualitatively different intracellular signalling.PloS one · 2012Article
- Article
- Restricted lateral diffusion of luteinizing hormone receptors in membrane microdomains.The Journal of biological chemistry · 2011Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Previous studies from our laboratory using co-immunoprecipitation techniques suggested that the human lutropin receptor (hLHR) constitutively self-associates into dimers/oligomers and that agonist treatment of cells either increased hLHR dimerization/oligomerization and/or stabilized hLHR dimers/oligomers to detergent solubilization (Tao, Y. X., Johnson, N. B., and Segaloff, D. L. (2004) J. Biol. Chem. 279, 5904-5914). In this study, bioluminescence resonance energy transfer (BRET(2)) analyses confirmed that the hLHR constitutively self-associates in living cells. After subcellular fractionation, hLHR dimers/oligomers were detected in both the plasma membrane and endoplasmic reticulum (ER). Further evidence supporting the constitutive formation of hLHR dimer/oligomers in the ER is provided by data showing homodimerization of misfolded hLHR mutants that are retained in the ER. These mutants, when co-expressed with wild-type receptor, are shown by BRET(2) to heterodimerize, accounting for their dominant-negative effects on cell surface receptor expression. Hormone desorption assays using intact cells demonstrate allosterism between hLHR protomers, indicating functional cell surface hLHR dimers. However, quantitative BRET(2) analyses in intact cells indicate a lack of effect of agonist on the propensity of the hLHR to dimerize. Using purified plasma membranes, human chorionic gonadotropin was similarly observed to have no effect on the BRET(2) signal. An examination of the propensity for constitutively active and signaling inactive hLHR mutants to dimerize further showed no correlation between dimerization and the activation state of the hLHR. Taken altogether, our data suggest that hLHR dimers/oligomers are formed early in the biosynthetic pathway in the ER, are constitutively expressed on the plasma membrane, and are not affected by the activation state of the hLHR.
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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.