Evidence map›Paper›PMID 38664468›Full record

ArticleCommunications biology2024

Absence of calcium-sensing receptor basal activity due to inter-subunit disulfide bridges.

Shumin Ma, Xueliang Yin, Jean-Philippe Pin, Philippe Rondard, Ping Yi, Jianfeng Liu

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 32% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Functional assessment of a constitutively activatingJournal of the Endocrine Society · 2026
    Article
  2. Review
  3. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Shumin MaCellular Signaling Laboratory, International Research Center for Sensory Biology and Technology of MOST, Key Laboratory of Molecular Biophysics of MOE, and College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, China.
Xueliang YinCellular Signaling Laboratory, International Research Center for Sensory Biology and Technology of MOST, Key Laboratory of Molecular Biophysics of MOE, and College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, China.
Jean-Philippe PinInstitut de Génomique Fonctionnelle (IGF), Université de Montpellier, CNRS, INSERM, Montpellier, Cedex 5, France.ORCID 0000-0002-1423-345X
Philippe RondardInstitut de Génomique Fonctionnelle (IGF), Université de Montpellier, CNRS, INSERM, Montpellier, Cedex 5, France. philippe.rondard@igf.cnrs.fr.ORCID 0000-0003-1134-2738
Ping YiCellular Signaling Laboratory, International Research Center for Sensory Biology and Technology of MOST, Key Laboratory of Molecular Biophysics of MOE, and College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, China. pingy@hust.edu.cn.ORCID 0000-0002-6954-102X
Jianfeng LiuCellular Signaling Laboratory, International Research Center for Sensory Biology and Technology of MOST, Key Laboratory of Molecular Biophysics of MOE, and College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, China. jfliu@mail.hust.edu.cn.ORCID 0000-0002-0284-8377
Huazhong University of Science and Technology · CNCentre National de la Recherche Scientifique · FR

Funding

Fondation pour la Recherche Médicale (Foundation for Medical Research in France) EQU202303016470National Natural Science Foundation of China (National Science Foundation of China) 31070737National Natural Science Foundation of China (National Science Foundation of China) 31371423National Natural Science Foundation of China (National Science Foundation of China) 32330049
6 · The paper itself

Abstract

G protein-coupled receptors naturally oscillate between inactive and active states, often resulting in receptor constitutive activity with important physiological consequences. Among the class C G protein-coupled receptors that typically sense amino-acids and their derivatives, the calcium sensing receptor (CaSR) tightly controls blood calcium levels. Its constitutive activity has not yet been studied. Here, we demonstrate the importance of the inter-subunit disulfide bridges in maintaining the inactive state of CaSR, resulting in undetectable constitutive activity, unlike the other class C receptors. Deletion of these disulfide bridges results in strong constitutive activity that is abolished by mutations preventing amino acid binding. It shows that this inter-subunit disulfide link is necessary to limit the agonist effect of amino acids on CaSR. Furthermore, human genetic mutations deleting these bridges and associated with hypocalcemia result in elevated CaSR constitutive activity. These results highlight the physiological importance of fine tuning the constitutive activity of G protein-coupled receptors.

Indexed as

DisulfidesReceptors, Calcium-SensingAnimalsCalciumHEK293 CellsHumansMutationCalciumCASR protein, humanDisulfidesReceptors, Calcium-Sensing

Identifiers

PMID38664468
PMCPMC11045811
OpenAlexW4395447695

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.