ArticleProceedings of the National Academy of Sciences of the United States of America1999
Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 182 citations in OpenAlex.
- Both calcium-sensing receptor intracellular C-terminal domains support homodimer signaling.Molecular pharmacology · 2025Article
- Case Presentation: Functional Assessment of aCase reports in endocrinology · 2024Article
- Cell Surface Calcium-Sensing Receptor Heterodimers: Mutant Gene Dosage Affects CaJournal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2022Article
- Calcium sensing receptor stimulates breast cancer cell migration via the Gβγ-AKT-mTORC2 signaling pathway.Journal of cell communication and signaling · 2022Article
- Functional Assessment of Calcium-Sensing Receptor Variants Confirms Familial Hypocalciuric Hypercalcemia.Journal of the Endocrine Society · 2022Article
- Adipocyte calcium sensing receptor is not involved in visceral adipose tissue inflammation or atherosclerosis development in hyperlipidemic ApoeScientific reports · 2021Article
- Case Report: Unusual Presentations of Loss-of-Function Mutations of the Calcium-Sensing Receptor.Frontiers in medicine · 2021Article
- The Different Facets of Extracellular Calcium Sensors: Old and New Concepts in Calcium-Sensing Receptor Signalling and Pharmacology.International journal of molecular sciences · 2018Review
- Article
- Investigating the molecular mechanism of positive and negative allosteric modulators in the calcium-sensing receptor dimer.Scientific reports · 2017Article
- Molecular Basis for Modulation of Metabotropic Glutamate Receptors and Their Drug Actions by Extracellular CaInternational journal of molecular sciences · 2017Review
- The Calcium-Sensing Receptor and Integrins in Cellular Differentiation and Migration.Frontiers in physiology · 2016Review
- Calcium-Sensing Receptor in Breast Physiology and Cancer.Frontiers in physiology · 2016Review
- Molecular Basis of the Extracellular Ligands Mediated Signaling by the Calcium Sensing Receptor.Frontiers in physiology · 2016Review
- The Calcium-Sensing Receptor and the Parathyroid: Past, Present, Future.Frontiers in physiology · 2016Review
- TACR3 mutations disrupt NK3R function through distinct mechanisms in GnRH-deficient patients.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Calcium signaling regulates trafficking of familial hypocalciuric hypercalcemia (FHH) mutants of the calcium sensing receptor.Molecular endocrinology (Baltimore, Md.) · 2012Article
- Enhanced Ca(2+)-sensing receptor function in idiopathic pulmonary arterial hypertension.Circulation research · 2012Article
- A novel CaSR mutation presenting as a severe case of neonatal familial hypocalciuric hypercalcemia.International journal of pediatric endocrinology · 2012Article
- Pathophysiology of GPCR Homo- and Heterodimerization: Special Emphasis on Somatostatin Receptors.Pharmaceuticals (Basel, Switzerland) · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
We recently demonstrated that the G protein-coupled, extracellular calcium-sensing receptor (CaR) forms disulfide-linked dimers. The functional significance of dimerization of this receptor was suggested by our earlier observations that CaRs carrying certain point mutations exert dominant negative effects on the function of the coexpressed wild-type receptor both in vivo and when cotransfected in human embryonic kidney cells. In this study, we explored the functional consequences of CaR dimerization. Coexpression in human embryonic kidney cells of specific pairs of mutant CaRs, each with reduced or absent activity because of distinct loss-of-function mutations, results in the formation of heterodimers and partially reconstitutes extracellular calcium-dependent signaling. Moreover, our results suggest that the CaR has at least two functionally separable domains. However, the presence of an abnormal domain in each mutant monomer substantially impairs the function of the CaR heterodimer, resulting in the reconstituted CaRs having characteristics distinct from those of the wild-type CaR. Our study suggests that intermolecular interactions within the dimeric CaR are important for the receptor's function.
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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.