Calcium-sensing receptor residues with loss- and gain-of-function mutations are located in regions of conformational change and cause signalling bias Article Swipe
Caroline M. Gorvin
,
Morten Frost
,
Tomas Malinauskas
,
Treena Cranston
,
Hannah Boon
,
Christian Siebold
,
E. Yvonne Jones
,
Fadil Hannan
,
Rajesh V. Thakker
·
YOU?
·
· 2018
· Open Access
·
· DOI: https://doi.org/10.1093/hmg/ddy263
YOU?
·
· 2018
· Open Access
·
· DOI: https://doi.org/10.1093/hmg/ddy263
The calcium-sensing receptor (CaSR) is a homodimeric G-protein-coupled receptor that signals via intracellular calcium (Ca2+i) mobilisation and phosphorylation of extracellular signal-regulated kinase 1/2 (ERK) to regulate extracellular calcium (Ca2+e) homeostasis. The central importance of the CaSR in Ca2+e homeostasis has been demonstrated by the identification of loss- or gain-of-function CaSR mutations that lead to familial hypocalciuric hypercalcaemia (FHH) or autosomal dominant hypocalcaemia (ADH), respectively. However, the mechanisms determining whether the CaSR signals via Ca2+i or ERK have not been established, and we hypothesised that some CaSR residues, which are the site of both loss- and gain-of-function mutations, may act as molecular switches to direct signalling through these pathways. An analysis of CaSR mutations identified in >300 hypercalcaemic and hypocalcaemic probands revealed five 'disease-switch' residues (Gln27, Asn178, Ser657, Ser820 and Thr828) that are affected by FHH and ADH mutations. Functional expression studies using HEK293 cells showed disease-switch residue mutations to commonly display signalling bias. For example, two FHH-associated mutations (p.Asn178Asp and p.Ser820Ala) impaired Ca2+i signalling without altering ERK phosphorylation. In contrast, an ADH-associated p.Ser657Cys mutation uncoupled signalling by leading to increased Ca2+i mobilization while decreasing ERK phosphorylation. Structural analysis of these five CaSR disease-switch residues together with four reported disease-switch residues revealed these residues to be located at conformationally active regions of the CaSR such as the extracellular dimer interface and transmembrane domain. Thus, our findings indicate that disease-switch residues are located at sites critical for CaSR activation and play a role in mediating signalling bias.
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- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1093/hmg/ddy263
- https://academic.oup.com/hmg/article-pdf/27/21/3720/26127123/ddy263.pdf
- OA Status
- hybrid
- Cited By
- 28
- References
- 58
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2884306505
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W2884306505Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1093/hmg/ddy263Digital Object Identifier
- Title
-
Calcium-sensing receptor residues with loss- and gain-of-function mutations are located in regions of conformational change and cause signalling biasWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2018Year of publication
- Publication date
-
2018-07-19Full publication date if available
- Authors
-
Caroline M. Gorvin, Morten Frost, Tomas Malinauskas, Treena Cranston, Hannah Boon, Christian Siebold, E. Yvonne Jones, Fadil Hannan, Rajesh V. ThakkerList of authors in order
- Landing page
-
https://doi.org/10.1093/hmg/ddy263Publisher landing page
- PDF URL
-
https://academic.oup.com/hmg/article-pdf/27/21/3720/26127123/ddy263.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
hybridOpen access status per OpenAlex
- OA URL
-
https://academic.oup.com/hmg/article-pdf/27/21/3720/26127123/ddy263.pdfDirect OA link when available
- Concepts
-
Calcium-sensing receptor, Biology, Extracellular, Phosphorylation, Receptor, Mutation, MAPK/ERK pathway, Signal transduction, Cell biology, G protein-coupled receptor, Calcium, Calcium metabolism, Biochemistry, Internal medicine, Gene, MedicineTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
28Total citation count in OpenAlex
- Citations by year (recent)
-
2024: 5, 2023: 2, 2022: 2, 2021: 7, 2020: 7Per-year citation counts (last 5 years)
- References (count)
-
58Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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