Biology:TGFB1I1

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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

Transforming growth factor beta-1-induced transcript 1 protein is a protein that in humans is encoded by the TGFB1I1 gene.[1][2] TGFB1I1 is also sometimes called HIC-5 (Hydrogen Peroxide-Inducible Clone-5)[3] or ARA55 (Androgen Receptor Coactivator 55kDA).[4]

As it's multiple names suggests, TGFB1I1 a protein whose expression is induced by TGFB1 and is both inducible by hydrogen peroxide, and a coactivator of the androgen receptors.

TGFB1I1 plays a role in processes of cell growth, proliferation,[5] migration, differentiation,[6] and senescence[7] in multiple contexts including in cancer. TGFB1I1 is most localized at focal adhesion complexes of cells,[1] although it may be found active in the cytosol, nucleus and cell membrane as well.[5][8][9]

Functions

Transforming growth factor beta-1-induced transcript 1 plays a role in a number of cell functions. Originally, TGFB1I1 was isolated as a senescence-inducing gene from mouse osteoblastic cells through treatment with transforming growth factor beta-1 and hydrogen peroxide.[7] During this, TGFB1I1 was also being independently discovered by numerous other groups and was characterized as a focal adhesion protein,[10][11] an androgen and glucocorticoid receptor co-activator,[8][12] a negative regulator of muscle differentiation,[6] and major player in the recovery of arterial media.[13][14]

Interactions

TGFB1I1 has been shown to interact with:

See also

References

  1. ↑ 1.0 1.1 1.2 1.3 "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions". The Journal of Biological Chemistry 273 (2): 1003–1014. January 1998. doi:10.1074/jbc.273.2.1003. PMID 9422762. 
  2. ↑ "Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate". The Journal of Biological Chemistry 274 (12): 8316–8321. March 1999. doi:10.1074/jbc.274.12.8316. PMID 10075738. 
  3. ↑ Du, Xuanling; Xu, Qiping; Pan, Duyi; Xu, Dongke; Niu, Baolin; Hong, Wenting; Zhang, Rui; Li, Xiaobo et al. (2019-11-18). "HIC-5 in cancer-associated fibroblasts contributes to esophageal squamous cell carcinoma progression" (in en). Cell Death & Disease 10 (12): 873. doi:10.1038/s41419-019-2114-z. ISSN 2041-4889. PMC 6861248. https://www.nature.com/articles/s41419-019-2114-z. 
  4. ↑ Cui, Zhaolei; Chen, Yan (2020-03-04). "ARA55 in Cancers: A Double-Edged Sword" (in English). Biomedical Journal of Scientific & Technical Research 26 (2): 19807–19811. doi:10.26717/BJSTR.2020.26.004326. ISSN 2574-1241. https://biomedres.us/fulltexts/BJSTR.MS.ID.004326.php. 
  5. ↑ 5.0 5.1 "Hic-5/ARA55, a LIM domain-containing nuclear receptor coactivator expressed in prostate stromal cells". Cancer Research 66 (14): 7326–7333. July 2006. doi:10.1158/0008-5472.can-05-2379. PMID 16849583. 
  6. ↑ 6.0 6.1 "Lepidopteran DALP, and its mammalian ortholog HIC-5, function as negative regulators of muscle differentiation". Proceedings of the National Academy of Sciences of the United States of America 96 (18): 10218–10223. August 1999. doi:10.1073/pnas.96.18.10218. PMID 10468589. Bibcode: 1999PNAS...9610218H. 
  7. ↑ 7.0 7.1 "Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence". The Journal of Biological Chemistry 269 (43): 26767–26774. October 1994. doi:10.1016/S0021-9258(18)47085-8. PMID 7929412. 
  8. ↑ 8.0 8.1 "Interaction of the tau2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix". Molecular Biology of the Cell 11 (6): 2007–2018. June 2000. doi:10.1091/mbc.11.6.2007. PMID 10848625. 
  9. ↑ "Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal". Molecular Biology of the Cell 14 (3): 1158–1171. March 2003. doi:10.1091/mbc.02-06-0099. PMID 12631731. 
  10. ↑ "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain" (in English). The Journal of Biological Chemistry 274 (14): 9847–9853. April 1999. doi:10.1074/jbc.274.14.9847. PMID 10092676. 
  11. ↑ "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin". Journal of Cell Science 112 ( Pt 2) (2): 181–190. January 1999. doi:10.1242/jcs.112.2.181. PMID 9858471. 
  12. ↑ "Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate" (in English). The Journal of Biological Chemistry 274 (12): 8316–8321. March 1999. doi:10.1074/jbc.274.12.8316. PMID 10075738. 
  13. ↑ "Non-receptor tyrosine kinases and the actin cytoskeleton in contractile vascular smooth muscle". The Journal of Physiology 593 (17): 3807–3814. September 2015. doi:10.1113/jphysiol.2014.284174. PMID 25433074. 
  14. ↑ "Hydrogen peroxide-inducible clone 5 (Hic-5) as a potential therapeutic target for vascular and other disorders". Journal of Atherosclerosis and Thrombosis 19 (7): 601–607. 2012. doi:10.5551/jat.10736. PMID 22472216. 
  15. ↑ 15.0 15.1 "Suppression of androgen receptor transactivation by Pyk2 via interaction and phosphorylation of the ARA55 coregulator". The Journal of Biological Chemistry 277 (18): 15426–15431. May 2002. doi:10.1074/jbc.M111218200. PMID 11856738. 
  16. ↑ "The FXXLF motif mediates androgen receptor-specific interactions with coregulators". The Journal of Biological Chemistry 277 (12): 10226–10235. March 2002. doi:10.1074/jbc.M111975200. PMID 11779876. 
  17. ↑ "The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter". The Journal of Neuroscience 22 (16): 7045–7054. August 2002. doi:10.1523/JNEUROSCI.22-16-07045.2002. PMID 12177201. 
  18. ↑ "Identification and characterization of hic-5/ARA55 as an hsp27 binding protein". The Journal of Biological Chemistry 276 (43): 39911–39918. October 2001. doi:10.1074/jbc.M103510200. PMID 11546764. 
  19. ↑ 19.0 19.1 "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin". Journal of Cell Science 112 ( Pt 2) (2): 181–190. January 1999. doi:10.1242/jcs.112.2.181. PMID 9858471. 
  20. ↑ "Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase". Molecular and Cellular Biology 21 (16): 5332–5345. August 2001. doi:10.1128/MCB.21.16.5332-5345.2001. PMID 11463817. 
  21. ↑ "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain". The Journal of Biological Chemistry 274 (14): 9847–9853. April 1999. doi:10.1074/jbc.274.14.9847. PMID 10092676. 

Further reading

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



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