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Btrc  -  beta-transducin repeat containing protein

Mus musculus

Synonyms: Beta-TrCP, Beta-TrCP protein E3RS-IkappaB, Beta-Trcp1, Beta-transducin repeat-containing protein, E3RS-IkappaB, ...
 
 
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Disease relevance of Btrc

 

High impact information on Btrc

 

Biological context of Btrc

  • Furthermore, the rate of proliferation was reduced and both cell size and the percentage of polyploid cells were increased in embryonic fibroblasts derived from beta-TrCP1-/- mice compared with the corresponding wild-type cells [5].
  • The nuclear translocation and DNA-binding activity of NF-kappa B as well as the ability of this transcription factor to activate a luciferase reporter gene were also inhibited in beta-TrCP1-/- cells compared with those apparent in wild-type cells [5].
  • We have examined the expression pattern of the putative antagonists Rab23 and Slimb/betaTrCP during early murine odontogenesis and find that these molecules are expressed in the developing tooth [6].
  • We have inactivated the gene encoding the Fbp beta-Trcp1 in mice. beta-Trcp1(-/-) males show reduced fertility correlating with an accumulation of methaphase I spermatocytes. beta-Trcp1(-/-) MEFs display a lengthened mitosis, centrosome overduplication, multipolar metaphase spindles, and misaligned chromosomes [7].
  • Through mutagenesis studies, we found that dual replacement of Ser 32 and 36 with Glu permitted beta-TrCP and proteasome-dependent, but not PIR, degradation [8].
 

Associations of Btrc with chemical compounds

  • Mutation of either serine 866 or serine 870 abolishes the beta-TrCP recruitment and ubiquitination of p100 [9].
  • These results show that the overexpression of Delta F beta TrCP1 or beta TrCP1 in vivo induce tumors through beta-catenin activation [10].
 

Other interactions of Btrc

References

  1. SCF(beta-TrCP1) controls Smad4 protein stability in pancreatic cancer cells. Wan, M., Huang, J., Jhala, N.C., Tytler, E.M., Yang, L., Vickers, S.M., Tang, Y., Lu, C., Wang, N., Cao, X. Am. J. Pathol. (2005) [Pubmed]
  2. Maturational differences in lung NF-kappaB activation and their role in tolerance to hyperoxia. Yang, G., Abate, A., George, A.G., Weng, Y.H., Dennery, P.A. J. Clin. Invest. (2004) [Pubmed]
  3. Prophase I arrest and progression to metaphase I in mouse oocytes are controlled by Emi1-dependent regulation of APCCdh1. Marangos, P., Verschuren, E.W., Chen, R., Jackson, P.K., Carroll, J. J. Cell Biol. (2007) [Pubmed]
  4. An F-box protein, FWD1, mediates ubiquitin-dependent proteolysis of beta-catenin. Kitagawa, M., Hatakeyama, S., Shirane, M., Matsumoto, M., Ishida, N., Hattori, K., Nakamichi, I., Kikuchi, A., Nakayama, K., Nakayama, K. EMBO J. (1999) [Pubmed]
  5. Impaired degradation of inhibitory subunit of NF-kappa B (I kappa B) and beta-catenin as a result of targeted disruption of the beta-TrCP1 gene. Nakayama, K., Hatakeyama, S., Maruyama, S., Kikuchi, A., Onoé, K., Good, R.A., Nakayama, K.I. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  6. Expression of the Hedgehog antagonists Rab23 and Slimb/betaTrCP during mouse tooth development. Miletich, I., Cobourne, M.T., Abdeen, M., Sharpe, P.T. Arch. Oral Biol. (2005) [Pubmed]
  7. Control of meiotic and mitotic progression by the F box protein beta-Trcp1 in vivo. Guardavaccaro, D., Kudo, Y., Boulaire, J., Barchi, M., Busino, L., Donzelli, M., Margottin-Goguet, F., Jackson, P.K., Yamasaki, L., Pagano, M. Dev. Cell (2003) [Pubmed]
  8. Evidence for a phosphorylation-independent role for Ser 32 and 36 in proteasome inhibitor-resistant (PIR) IkappaBalpha degradation in B cells. O'Connor, S., Markovina, S., Miyamoto, S. Exp. Cell Res. (2005) [Pubmed]
  9. beta-TrCP binding and processing of NF-kappaB2/p100 involve its phosphorylation at serines 866 and 870. Liang, C., Zhang, M., Sun, S.C. Cell. Signal. (2006) [Pubmed]
  10. Overexpression of human beta TrCP1 deleted of its F box induces tumorigenesis in transgenic mice. Belaïdouni, N., Peuchmaur, M., Perret, C., Florentin, A., Benarous, R., Besnard-Guérin, C. Oncogene (2005) [Pubmed]
  11. Characterization of the human suppressor of fused, a negative regulator of the zinc-finger transcription factor Gli. Stone, D.M., Murone, M., Luoh, S., Ye, W., Armanini, M.P., Gurney, A., Phillips, H., Brush, J., Goddard, A., de Sauvage, F.J., Rosenthal, A. J. Cell. Sci. (1999) [Pubmed]
  12. ATF4, the osteoblast accumulation of which is determined post-translationally, can induce osteoblast-specific gene expression in non-osteoblastic cells. Yang, X., Karsenty, G. J. Biol. Chem. (2004) [Pubmed]
 
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