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Session 7: Ubiquitin & Proteasomes
References
- Hershko, A., and Ciechanover, A. (1998). The ubiquitin system. Annu Rev Biochem 67, 425—79.[CrossRef][Web of Science][Medline]
[Order article via Infotrieve]
- Weissman, A.M. (2001). Themes and variations on ubiquitylation. Natl Rev Mol Cell Biol 2, 169—78.[CrossRef][Web of Science][Medline]
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- Ciechenover, A. (1998). The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J 17, 7151—60.[CrossRef][Web of Science][Medline]
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- Rock, K.L. et al. (1994). Inhibitors of the proteosome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761—71.[CrossRef][Web of Science][Medline]
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- Zwickl, P., Voges, D., and Baumeister, W. (1999). The proteasome: a macromolecular assembly designed for controlled proteolysis. Philos Trans R Soc London B Biol Sci 354, 1501—11.[Abstract/Free Full Text]
- Wilkinson, K.D. (1999). Ubiquitin-dependent signaling: the role of ubiquitination in the response of cells to their environment. J Nutr 129, 1933—6.[Abstract/Free Full Text]
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- Albanell, J., and Adams, J. (2002). Bortezomib, a proteasome inhibitor in cancer therapy: from concept to clinic. Drugs of the future 27(11), 1079—92.[CrossRef][Web of Science]
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- Sakamoto, K.M. (2002). Ubiquitin-dependent proteolysis: its role in human diseases and the design of therapeutic strategies. Molec Genet Metabol 77, 44—56.[CrossRef]
- Rolfe, M., Chiu, M.I., and Pagano, M. (1997). The ubiquitin-mediated proteolytic pathways as a therapeutic area. J Mol Med 75, 5—17.[CrossRef][Web of Science][Medline]
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- Elliott, P.J., and Zollner, T.M. (2003). Proteasome inhibition: a new antiinflammatory strategy. J Mol Med 81, 235—45.[CrossRef][Web of Science][Medline]
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- McBride, W.H. et al. (2003). The role of ubiquitin/proteasome system in cellular responses to radiation. Oncogene 22, 5755—73.[CrossRef][Web of Science][Medline]
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- Drexler, H.C. (1997). Activation of the cell death program by inhibition of proteasome function. Proc Natl Acad Sci USA 94, 855—60.[Abstract/Free Full Text]
- Fang, S. et al. (2003). RING finger ubiquitin protein ligases: implications for tumorogenesis, metastasis and for molecular targets in cancer. Seminars in Cancer Biology, 13, 5—14.[CrossRef][Web of Science][Medline]
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- Shinohara, K. et al. (1996). Apoptosis induction resulting from proteasome inhibition. Biochem J 317, 385—8.[Web of Science][Medline]
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- Adams, J., Palombella, V.J., and Elliot, P.J. (2000). Proteasome inhibition: a new strategy in cancer treatment. Investigational New Drugs 18, 109—21.[CrossRef][Web of Science][Medline]
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- Leem, M.-H., and Yang, H.-Y. (2003). Molecular targets for cell cycle inhibition and cancer therapy. Expert Opin Ther Patents 13(3), 329—46.[CrossRef]
- Murray, R.Z., and Norbury, C. (2000). Proteasome inhibitors as anti-cancer agents. Anti-Cancer Drugs 11, 407—17.[CrossRef][Medline]
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- Almond, J.B., and Cohen, G.M. (2002). The proteasome: a novel target for anticancer chemotherapy. Leukemia 16, 433—43.[CrossRef][Web of Science][Medline]
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- Cadavid, A.L.M., Ginzel, A., and Fischer, J.A. (2000). The function of the Drosophila Fat facets deubiquitinating enzyme in limiting photoreceptor cell number is intimately associated with endocytosis. Development 127, 1727—36.[Abstract]
- Chen, X., Zhang, B., and Fischer, J.A. (2002). A specific protein substrate for a deubiquitinating enzyme: liquid facets is the substrate of Fat facets. Genes Dev 16, 289—94.[Abstract/Free Full Text]
- De Camilli, P., Chen, H., Hyman, J., Panepucci, E., Bateman, A., and Brunger, A.T. (2001). The ENTH domain. FEBS Lett 25686, 1—6.
- Fischer, J.A. (2003). Deubiquitinating enzymes: their roles in development, differentiation, and disease. Int Rev Cytol 229, 43—72.[Web of Science][Medline]
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- Fischer, J.A., Leavell, S., and Li, Q. (1997). Mutagenesis screens for interacting genes reveal three role for fat facets during Drosophila eye development. Dev Genet 21, 167—74.[CrossRef][Web of Science][Medline]
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- Fischer-Vize, J.A., Rubin, G.M., and Lehmann, R. (1992). The fat facets gene is required for Drosophila eye and embryo development. Development 116, 985—1000.[Abstract]
- Huang, Y., Baker, R.T., and Fischer-Vize, J.A. (1995). Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene. Science 270, 1828—31.[Abstract/Free Full Text]
- Parks, A.L., Klueg, K.M., Stout, J.R., and Muskavitch, M. A. T (2000). Ligand endocytosis drives receptor dissociation and activation in the Notch pathway. Development 127, 1373—85.[Abstract]
- Weissman, A.M. (2001). Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2, 169—78.[CrossRef][Web of Science][Medline]
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- Weng, A.P., and Aster, J.C. (2004). Multiple niches for Notch in cancer: context is everything. Curr Opin Genet Dev 14, 48—54.[CrossRef][Web of Science][Medline]
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- Wu, Z., Li, Q., Fortini, M.E., and Fischer, J.A. (1999). Genetic analysis of the role of the Drosophila fat facets gene in the ubiquitin pathway. Dev Genet 25, 312—20.[CrossRef][Web of Science][Medline]
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- Borden, K.L. (2000). RING domains: master builders of molecular scaffolds? J Mol Biol 295, 1103—12.[CrossRef][Web of Science][Medline]
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- Hu, G., Zhang, S., Vidal, M., Baer, J.L., Xu, T., and Fearon, E.R. (1997). Mammalian homologs of seven in absentia regulate DCC via the ubiquitinproteasome pathway. Genes Dev 11, 2701—14.[Abstract/Free Full Text]
- Matsuzawa, S.I., and Reed, J.C. (2001) Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses. Mol Cell 7, 915—26[CrossRef][Web of Science][Medline]
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- Habelhah, H., Takahashi, S., Cho, S.G., Kadoya, T., and Ronai, Z. (2004). TRAF2 ubiquitination is required for its translocation to the cell membrane and activation of JNK but not p38 or NF-
 B signaling. EMBO J 23, 322—32.[CrossRef][Web of Science][Medline]
[Order article via Infotrieve] - Habelhah, H., Frew, I., Laine, A., Janes, P., Relaix, F., Sassoon D., Bowtell, D., and Ze'ev Ronai. (2002). Siah2 as regulator of TRAF2 stability. EMBO J 21, 5756—65.[CrossRef][Web of Science][Medline]
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- Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J.M., Lane, W.S., and Kaelin Jr., W.G. (2001). HIF targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 292, 464—8.[Abstract/Free Full Text]
- Koh Nakayama, K., Frew, I.J., Hagensen, M., Skals, M., Habelhah, H., Erdjument-Bromage, H., Tempst, P., Frappell, P.B., Bowtell, D.D., and Ronai, Z. (2004). Siah2 regulates stability of the prolyl-hydroxylase SM20, controls HIF1
 abundance and modulates physiological responses to hypoxia. Cell, In Press, June 2004.
Toxicologic Pathology, Vol. 32, No. 6,
740-742 (2004)
DOI: 10.1080/01926230490882475
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