Biology:Thyroid hormone receptor beta

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Thyroid hormone receptor beta (TR-beta) also known as nuclear receptor subfamily 1, group A, member 2 (NR1A2), is a nuclear receptor protein that in humans is encoded by the THRB gene.[1][2]

Function

The protein encoded by this gene is a nuclear hormone receptor for triiodothyronine. It is one of the several receptors for thyroid hormone, and has been shown to mediate the biological activities of thyroid hormone. Knockout studies in mice suggest that the different receptors, while having certain extent of redundancy, may mediate different functions of thyroid hormone. Defects in this gene are known to be a cause of generalized thyroid hormone resistance (GTHR), a syndrome characterized by goiter and high levels of circulating thyroid hormone (T3-T4), with normal or slightly elevated thyroid stimulating hormone (TSH). Several transcript variants have been observed for this gene, but the full-length nature of only one has been observed so far.[3]

Interactions

Thyroid hormone receptor beta has been shown to interact with:


References

  1. "Entrez Gene: THRA thyroid hormone receptor, alpha (erythroblastic leukemia viral (v-erb-a) oncogene homolog, avian)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7067. 
  2. "Structural analysis of human thyroid hormone receptor beta gene". Mol. Cell. Endocrinol. 71 (2): 83–91. June 1990. doi:10.1016/0303-7207(90)90245-4. PMID 1973914. 
  3. "Entrez Gene: THRB thyroid hormone receptor, beta (erythroblastic leukemia viral (v-erb-a) oncogene homolog 2, avian)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7068. 
  4. 4.0 4.1 "Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein". J. Biol. Chem. 272 (47): 29834–41. November 1997. doi:10.1074/jbc.272.47.29834. PMID 9368056. 
  5. "Cyclin D1 Is a Ligand-independent Co-repressor for Thyroid Hormone Receptors". J. Biol. Chem. 277 (32): 28733–41. August 2002. doi:10.1074/jbc.M203380200. PMID 12048199. 
  6. 6.0 6.1 "Lack of coactivator interaction can be a mechanism for dominant negative activity by mutant thyroid hormone receptors". Endocrinology 139 (10): 4197–204. October 1998. doi:10.1210/endo.139.10.6218. PMID 9751500. 
  7. 7.0 7.1 "Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor". Mol. Endocrinol. 11 (6): 755–67. June 1997. doi:10.1210/mend.11.6.0003. PMID 9171239. 
  8. "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2". Mol. Endocrinol. 15 (2): 241–54. February 2001. doi:10.1210/mend.15.2.0595. PMID 11158331. 
  9. "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo". J. Biol. Chem. 274 (48): 34283–93. November 1999. doi:10.1074/jbc.274.48.34283. PMID 10567404. 
  10. "Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator". Proc. Natl. Acad. Sci. U.S.A. 97 (11): 6212–7. May 2000. doi:10.1073/pnas.97.11.6212. PMID 10823961. Bibcode2000PNAS...97.6212K. 
  11. "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs". Mol. Endocrinol. 16 (1): 128–40. January 2002. doi:10.1210/mend.16.1.0755. PMID 11773444. 
  12. "The interaction of the vitamin D receptor with nuclear receptor corepressors and coactivators". Biochem. Biophys. Res. Commun. 253 (2): 358–63. December 1998. doi:10.1006/bbrc.1998.9799. PMID 9878542. 
  13. "Aberrant alternative splicing of thyroid hormone receptor in a TSH-secreting pituitary tumor is a mechanism for hormone resistance". Mol. Endocrinol. 15 (9): 1529–38. September 2001. doi:10.1210/mend.15.9.0687. PMID 11518802. 
  14. "The orphan nuclear receptor Ear-2 is a negative coregulator for thyroid hormone nuclear receptor function". Mol. Cell. Biol. 20 (7): 2604–18. April 2000. doi:10.1128/MCB.20.7.2604-2618.2000. PMID 10713182. 
  15. "Requirement of helix 1 and the AF-2 domain of the thyroid hormone receptor for coactivation by PGC-1". J. Biol. Chem. 277 (11): 8898–905. March 2002. doi:10.1074/jbc.M110761200. PMID 11751919. 

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.