The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

Tgfb1i1  -  transforming growth factor beta 1 induced...

Mus musculus

Synonyms: ARA55, Androgen receptor-associated protein of 55 kDa, Ara55, Hic-5, Hic5, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

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

References

  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]
 
WikiGenes - Universities