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TGFB1I1
Protein-coding gene in the species Homo sapiens
Protein-coding gene in the species Homo sapiens
Transforming growth factor beta-1-induced transcript 1 protein is a protein that in humans is encoded by the TGFB1I1 gene. TGFB1I1 is also sometimes called HIC-5 (Hydrogen Peroxide-Inducible Clone-5) or ARA55 (Androgen Receptor Coactivator 55kDA).
As its 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, migration, differentiation, and senescence in multiple contexts including in cancer. TGFB1I1 is most localized at focal adhesion complexes of cells, although it may be found active in the cytosol, nucleus and cell membrane as well.
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. During this, TGFB1I1 was also being independently discovered by numerous other groups and was characterized as a focal adhesion protein, an androgen and glucocorticoid receptor co-activator, a negative regulator of muscle differentiation, and major player in the recovery of arterial media.
Interactions
TGFB1I1 has been shown to interact with:
- Androgen receptor,
- Dopamine transporter
- Hsp27,
- PTK2B,
- PTK2, and
- PTPN12.
References
References
- (January 1998). "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions". The Journal of Biological Chemistry.
- (March 1999). "Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate". The Journal of Biological Chemistry.
- (2019-11-18). "HIC-5 in cancer-associated fibroblasts contributes to esophageal squamous cell carcinoma progression". Cell Death & Disease.
- (2020-03-04). "ARA55 in Cancers: A Double-Edged Sword". Biomedical Journal of Scientific & Technical Research.
- (July 2006). "Hic-5/ARA55, a LIM domain-containing nuclear receptor coactivator expressed in prostate stromal cells". Cancer Research.
- (August 1999). "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.
- (October 1994). "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.
- (June 2000). "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.
- (March 2003). "Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal". Molecular Biology of the Cell.
- (April 1999). "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain". The Journal of Biological Chemistry.
- (January 1999). "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin". Journal of Cell Science.
- (March 1999). "Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate". The Journal of Biological Chemistry.
- (September 2015). "Non-receptor tyrosine kinases and the actin cytoskeleton in contractile vascular smooth muscle". The Journal of Physiology.
- (2012). "Hydrogen peroxide-inducible clone 5 (Hic-5) as a potential therapeutic target for vascular and other disorders". Journal of Atherosclerosis and Thrombosis.
- (May 2002). "Suppression of androgen receptor transactivation by Pyk2 via interaction and phosphorylation of the ARA55 coregulator". The Journal of Biological Chemistry.
- (March 2002). "The FXXLF motif mediates androgen receptor-specific interactions with coregulators". The Journal of Biological Chemistry.
- (August 2002). "The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter". The Journal of Neuroscience.
- (October 2001). "Identification and characterization of hic-5/ARA55 as an hsp27 binding protein". The Journal of Biological Chemistry.
- (January 1999). "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin". Journal of Cell Science.
- (August 2001). "Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase". Molecular and Cellular Biology.
- (April 1999). "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain". The Journal of Biological Chemistry.
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