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Gene Review

Tgfb1i1  -  transforming growth factor beta 1 induced...

Mus musculus

Synonyms: ARA55, Androgen receptor-associated protein of 55 kDa, Ara55, Hic-5, Hic5, ...
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Disease relevance of Tgfb1i1

  • Finally, a colony formation assay using an hic-5 expression vector driven by the cytomegalovirus promoter suggested that hic-5 overexpression had a cytostatic effect on cellular growth, depending upon the cell type [1].

High impact information on Tgfb1i1

  • Hic-5 and PPARgamma colocalize to the villus epithelium of the small intestine, and their expression during embryonic gut development correlates with the transition from endoderm to a specialized epithelium; expression of both these factors is reduced in tumors [2].
  • We show here that PPARgamma interacts with Hic-5, a coactivator protein expressed in gut epithelial cells [2].
  • Taken together, these data suggest that DALP and Hic-5 act upstream of MyoD and function as phylogenetically conserved "switches" to block muscle differentiation and induce death [3].
  • Hic-5 expression is specifically and dramatically induced in normal myoblasts that die after removal of trophic support [3].
  • Ectopic expression of DALP, or its mammalian ortholog Hic-5, blocks differentiation and induces apoptosis in mouse C(2)C(12) myoblasts [3].

Biological context of Tgfb1i1

  • The ability of Hic-5/ARA55 to shuttle between the nuclear and cytoplasmic compartments was revealed on inhibition of nuclear export with leptomycin B [4].
  • From in vitro binding experiments using deletion and point mutations, it was demonstrated that the essential domain in Hic-5 for the binding was LIM 3 [5].
  • Finally, forced expression of Hic-5 during 3T3-L1 preadipocyte differentiation inhibits adipogenesis while inducing inappropriate expression of several mRNAs characteristic of gut epithelium in these mesenchymal cells [2].
  • We conclude that hic-5 is a true hsp27 binding protein and inhibits the ability of hsp27 to provide protection against heat shock in an interaction-dependent manner [6].
  • 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 [1].

Anatomical context of Tgfb1i1


Associations of Tgfb1i1 with chemical compounds

  • Finally, the mechanism of Hic-5/ARA55 coactivator activity in WPMY-1 cells was revealed by chromatin immunoprecipitation analysis that showed its androgen-dependent recruitment to the promoter of the stromal androgen-responsive keratinocyte growth factor gene [4].
  • In conclusion, Hic-5 may participate in the regulation of signaling cascade through its interaction with distinct tyrosine kinases and phosphatases [5].
  • In this study, we found that Hic-5 accumulated in the nucleus in response to oxidants such as H(2)O(2) [8].
  • Identification and analysis of Hic-5/ARA55 isoforms: Implications for integrin signaling and steroid hormone action [9].

Regulatory relationships of Tgfb1i1

  • Our previous study suggested that Hic-5 participates in the transcriptional control of several genes such as the c-fos and p21 genes [10].

Other interactions of Tgfb1i1

  • However, this interaction was not essential for recruitment of Hic-5 to focal adhesions, since its subcellular localization was similar in FAK(-/-) cells [11].
  • The Hic-5 level was markedly decreased when cells became immortalized, whereas that of paxillin was increased [11].
  • The steady-state levels of TSC-36, TSC-128 and TSC-160 increased almost tenfold, whereas those of TSC-5, TSC-115 and TSC-161 were elevated at most threefold [12].
  • Two of these genes, Hic-5, a possible negative regulator of muscle differentiation, and the transcription enhancing factor TEF-5 were selected and shown by in situ hybridizations to be expressed in the early developing heart [13].
  • Thus, Hic-5 was suggested to have a potential function as a cofactor in the transcriptional complex that contains Sp1, playing a role in gene transcription in the nucleus as well as in integrin signaling at focal adhesion sites [10].

Analytical, diagnostic and therapeutic context of Tgfb1i1


  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. Shibanuma, M., Mashimo, J., Kuroki, T., Nose, K. J. Biol. Chem. (1994) [Pubmed]
  2. Hic-5 regulates an epithelial program mediated by PPARgamma. Drori, S., Girnun, G.D., Tou, L., Szwaya, J.D., Mueller, E., Xia, K., Kia, X., Shivdasani, R.A., Spiegelman, B.M. Genes Dev. (2005) [Pubmed]
  3. Lepidopteran DALP, and its mammalian ortholog HIC-5, function as negative regulators of muscle differentiation. Hu, Y., Cascone, P.J., Cheng, L., Sun, D., Nambu, J.R., Schwartz, L.M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  4. Hic-5/ARA55, a LIM domain-containing nuclear receptor coactivator expressed in prostate stromal cells. Heitzer, M.D., DeFranco, D.B. Cancer Res. (2006) [Pubmed]
  5. Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain. Nishiya, N., Iwabuchi, Y., Shibanuma, M., Côté, J.F., Tremblay, M.L., Nose, K. J. Biol. Chem. (1999) [Pubmed]
  6. Identification and characterization of hic-5/ARA55 as an hsp27 binding protein. Jia, Y., Ransom, R.F., Shibanuma, M., Liu, C., Welsh, M.J., Smoyer, W.E. J. Biol. Chem. (2001) [Pubmed]
  7. Uni-axial stretching regulates intracellular localization of Hic-5 expressed in smooth-muscle cells in vivo. Kim-Kaneyama, J.R., Suzuki, W., Ichikawa, K., Ohki, T., Kohno, Y., Sata, M., Nose, K., Shibanuma, M. J. Cell. Sci. (2005) [Pubmed]
  8. Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal. Shibanuma, M., Kim-Kaneyama, J.R., Ishino, K., Sakamoto, N., Hishiki, T., Yamaguchi, K., Mori, K., Mashimo, J., Nose, K. Mol. Biol. Cell (2003) [Pubmed]
  9. Identification and analysis of Hic-5/ARA55 isoforms: Implications for integrin signaling and steroid hormone action. Gao, Z., Schwartz, L.M. FEBS Lett. (2005) [Pubmed]
  10. A LIM protein, Hic-5, functions as a potential coactivator for Sp1. Shibanuma, M., Kim-Kaneyama, J.R., Sato, S., Nose, K. J. Cell. Biochem. (2004) [Pubmed]
  11. Specific decrease in the level of Hic-5, a focal adhesion protein, during immortalization of mouse embryonic fibroblasts, and its association with focal adhesion kinase. Ishino, K., Kaneyama, n.u.l.l., Shibanuma, M., Nose, K. J. Cell. Biochem. (2000) [Pubmed]
  12. Cloning from a mouse osteoblastic cell line of a set of transforming-growth-factor-beta 1-regulated genes, one of which seems to encode a follistatin-related polypeptide. Shibanuma, M., Mashimo, J., Mita, A., Kuroki, T., Nose, K. Eur. J. Biochem. (1993) [Pubmed]
  13. Novel cell lines promote the discovery of genes involved in early heart development. Brunskill, E.W., Witte, D.P., Yutzey, K.E., Potter, S.S. Dev. Biol. (2001) [Pubmed]
  14. Genomic structure and chromosomal mapping of the mouse hic-5 gene that encodes a focal adhesion protein. Mashimo, J., Shibanuma, M., Satoh, H., Chida, K., Nose, K. Gene (2000) [Pubmed]
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