Biology:TGFB1I1
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Short description: Protein-coding gene in the species Homo sapiens
 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] Often put together with and studied alongside TGFB1I1 is the mouse homologue HIC-5 ( Hydrogen Peroxide-Inducible Clone-5). As the name suggests, TGFB1I1 is an induced form of the larger family of TGFB1. Studies suggest TGFB1I1 plays a role in processes of cell growth, proliferation,[3] migration, differentiation[4] and senescence.[5] 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.[3][6][7]
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.[5] During this, TGFB1I1 was also being independently discovered by numerous other groups and was characterized as a focal adhesion protein,[8][9] an androgen and glucocorticoid receptor co-activator,[6][10] a negative regulator of muscle differentiation,[4] and major player in the recovery of arterial media.[11][12]
Interactions
TGFB1I1 has been shown to interact with:
- Androgen receptor,[13][14]
- Dopamine transporter[15]
- Hsp27,[16]
- PTK2B,[1][13][17]
- PTK2,[1][17][18] and
- PTPN12.[19]
See also
References
- ↑ 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.
- ↑ "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.
- ↑ 3.0 3.1 "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.
- ↑ 4.0 4.1 "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.
- ↑ 5.0 5.1 "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.
- ↑ 6.0 6.1 "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ 13.0 13.1 "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ 17.0 17.1 "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.
- ↑ "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.
- ↑ "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
- "Functional analysis of androgen receptor N-terminal and ligand binding domain interacting coregulators in prostate cancer". Journal of the Formosan Medical Association = Taiwan Yi Zhi 99 (12): 885–894. December 2000. PMID 11155740.
- "Hic-5/ARA55: a prostate stroma-specific AR coactivator". Steroids 72 (2): 218–220. February 2007. doi:10.1016/j.steroids.2006.11.010. PMID 17166536.
- "Epidermal growth factor and its receptor, basic fibroblast growth factor, transforming growth factor beta-1, and interleukin-1 alpha messenger RNA production in human corneal endothelial cells". Investigative Ophthalmology & Visual Science 32 (10): 2747–2756. September 1991. PMID 1716619.
- "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.
- "Induction of senescence-like phenotypes by forced expression of hic-5, which encodes a novel LIM motif protein, in immortalized human fibroblasts". Molecular and Cellular Biology 17 (3): 1224–1235. March 1997. doi:10.1128/mcb.17.3.1224. PMID 9032249.
- "Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase". The Journal of Biological Chemistry 273 (41): 26516–26521. October 1998. doi:10.1074/jbc.273.41.26516. PMID 9756887.
- "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.
- "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.
- "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling". The Journal of Cell Biology 145 (4): 851–863. May 1999. doi:10.1083/jcb.145.4.851. PMID 10330411.
- "Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses". Nature 402 (6762): 676–681. December 1999. doi:10.1038/45264. PMID 10604475. Bibcode: 1999Natur.402..676L.
- "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.
- "CrkL is an adapter for Wiskott-Aldrich syndrome protein and Syk". Blood 97 (9): 2633–2639. May 2001. doi:10.1182/blood.V97.9.2633. PMID 11313252.
- "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.
- "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.
- "Supervillin associates with androgen receptor and modulates its transcriptional activity". Proceedings of the National Academy of Sciences of the United States of America 99 (2): 661–666. January 2002. doi:10.1073/pnas.022469899. PMID 11792840. Bibcode: 2002PNAS...99..661T.
- "Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5". The Journal of Biological Chemistry 277 (14): 12270–12274. April 2002. doi:10.1074/jbc.M110291200. PMID 11805099.
- "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.
External links
- TGFB1I1 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
- NURSA C148
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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