Calcitonin receptor

The calcitonin receptor (CT) is a G protein-coupled receptor that binds the peptide hormone calcitonin and is involved in maintenance of calcium homeostasis,[5] particularly with respect to bone formation and metabolism.[6][7][8]

CALCR
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCALCR, CRT, CT-R, CTR, CTR1, calcitonin receptor
External IDsOMIM: 114131 MGI: 101950 HomoloGene: 1320 GeneCards: CALCR
Orthologs
SpeciesHumanMouse
Entrez

799

12311

Ensembl

ENSG00000004948

ENSMUSG00000023964

UniProt

P30988

Q60755

RefSeq (mRNA)

NM_001742
NM_001164737
NM_001164738

NM_001042725
NM_007588
NM_001355192
NM_001377018

RefSeq (protein)

NP_001158209
NP_001158210
NP_001733

NP_001036190
NP_031614
NP_001342121
NP_001363947

Location (UCSC)Chr 7: 93.42 – 93.57 MbChr 6: 3.69 – 3.76 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

CT works by activating the G-proteins Gs and Gq often found on osteoclasts, on cells in the kidney, and on cells in a number of regions of the brain.[9] It may also affect the ovaries in women and the testes in men.

The function of the CT receptor protein is modified through its interaction with Receptor activity-modifying proteins (RAMPs), forming the multimeric amylin receptors AMY1 (CT + RAMP1), AMY2 (CT + RAMP2), and AMY3 (CT+ RAMP3).[10]

Interactions

Structure of human calcitonin recptor-Gs complex. The transmembrane calcitonin receptor (blue) is bound to human calcitonin (red) and the Gs complex (yellow). PDB: 7TYO

Calcitonin receptor has been shown to interact with Apolipoprotein B[11][12] and LRP1.[13]

References

  1. GRCh38: Ensembl release 89: ENSG00000004948 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000023964 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Purdue BW, Tilakaratne N, Sexton PM (2002). "Molecular pharmacology of the calcitonin receptor". Receptors & Channels. 8 (3–4): 243–55. doi:10.1080/10606820213681. PMID 12529940.
  6. Chambers TJ, Magnus CJ (January 1982). "Calcitonin alters behaviour of isolated osteoclasts". The Journal of Pathology. 136 (1): 27–39. doi:10.1002/path.1711360104. PMID 7057295. S2CID 8395420.
  7. Dacquin R, Davey RA, Laplace C, Levasseur R, Morris HA, Goldring SR, Gebre-Medhin S, Galson DL, Zajac JD, Karsenty G (February 2004). "Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo". The Journal of Cell Biology. 164 (4): 509–14. doi:10.1083/jcb.200312135. PMC 2171986. PMID 14970190.
  8. Davey RA, Turner AG, McManus JF, Chiu WS, Tjahyono F, Moore AJ, Atkins GJ, Anderson PH, Ma C, Glatt V, MacLean HE, Vincent C, Bouxsein M, Morris HA, Findlay DM, Zajac JD (August 2008). "Calcitonin receptor plays a physiological role to protect against hypercalcemia in mice". Journal of Bone and Mineral Research. 23 (8): 1182–93. doi:10.1359/jbmr.080310. PMC 2680171. PMID 18627265.
  9. senselab Archived February 28, 2009, at the Wayback Machine
  10. "Calcitonin Receptors: Introduction". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
  11. Zhang J, Herscovitz H (February 2003). "Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B". The Journal of Biological Chemistry. 278 (9): 7459–68. doi:10.1074/jbc.M207976200. PMID 12397072.
  12. Linnik KM, Herscovitz H (August 1998). "Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state". The Journal of Biological Chemistry. 273 (33): 21368–73. doi:10.1074/jbc.273.33.21368. PMID 9694898.
  13. Orr AW, Pedraza CE, Pallero MA, Elzie CA, Goicoechea S, Strickland DK, Murphy-Ullrich JE (June 2003). "Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly". The Journal of Cell Biology. 161 (6): 1179–89. doi:10.1083/jcb.200302069. PMC 2172996. PMID 12821648.

Further reading

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