A transgenic mouse model of the ubiquitin/proteasome system (original) (raw)

• Sherman, M.Y. & Goldberg, A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29, 15–32 (2001).
  Article CAS Google Scholar
• DeSalle, L.M. & Pagano, M. Regulation of the G1 to S transition by the ubiquitin pathway. FEBS Lett. 490, 179–189 (2001).
  Article CAS Google Scholar
• Karin, M. & Ben-Neriah, Y. Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu. Rev. Immunol. 18, 621–663 (2000).
  Article CAS Google Scholar
• Baumeister, W., Walz, J., Zuhl, F. & Seemuller, E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367–380 (1998).
  Article CAS Google Scholar
• Hershko, A. & Ciechanover, A. The ubiquitin system. Annu. Rev. Biochem. 67, 425–479 (1998).
  Article CAS Google Scholar
• Bence, N.F., Sampat, R.M. & Kopito, R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552–1555 (2001).
  Article CAS Google Scholar
• Cummings, C.J. et al. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19, 148–154 (1998).
  Article CAS Google Scholar
• Lam, Y.A. et al. Inhibition of the ubiquitin-proteasome system in Alzheimer's disease. Proc. Natl. Acad. Sci. USA 97, 9902–9906 (2000).
  Article CAS Google Scholar
• Lindsten, K. et al. Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J. Cell Biol. 157, 417–427 (2002).
  Article CAS Google Scholar
• Mizuno, Y., Hattori, N., Mori, H., Suzuki, T. & Tanaka, K. Parkin and Parkinson's disease. Curr. Opin. Neurol. 14, 477–482 (2001).
  Article CAS Google Scholar
• Carrell, R.W. & Lomas, D.A. Conformational disease. Lancet 350, 134–138 (1997).
  Article CAS Google Scholar
• Muchowski, P.J. Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron 35, 9–12 (2002).
  Article CAS Google Scholar
• Soto, C. Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498, 204–207 (2001).
  Article CAS Google Scholar
• Verhoef, L.G., Lindsten, K., Masucci, M.G. & Dantuma, N.P. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet. 11, 2689–2700 (2002).
  Article CAS Google Scholar
• Floyd, J.A. & Hamilton, B.A. Intranuclear inclusions and the ubiquitin-proteasome pathway: digestion of a red herring? Neuron 24, 765–766 (1999).
  Article CAS Google Scholar
• Saudou, F., Finkbeiner, S., Devys, D. & Greenberg, M.E. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55–66 (1998).
  Article CAS Google Scholar
• Watase, K. et al. A long CAG repeat in the mouse Sca1 locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration. Neuron 34, 905–919 (2002).
  Article CAS Google Scholar
• Ryan, K.M., Phillips, A.C. & Vousden, K.H. Regulation and function of the p53 tumor suppressor protein. Curr. Opin. Cell. Biol. 13, 332–337 (2001).
  Article CAS Google Scholar
• Slingerland, J. & Pagano, M. Regulation of the cdk inhibitor p27 and its deregulation in cancer. J. Cell Physiol. 183, 10–17 (2000).
  Article CAS Google Scholar
• Meng, L. et al. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA 96, 10403–10408 (1999).
  Article CAS Google Scholar
• Meng, L., Kwok, B.H., Sin, N. & Crews, C.M. Eponemycin exerts its antitumor effect through the inhibition of proteasome function. Cancer Res. 59, 2798–2801 (1999).
  CAS PubMed Google Scholar
• Aghajanian, C. et al. A phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies. Clin. Cancer Res. 8, 2505–2511 (2002).
  CAS PubMed Google Scholar
• Pati, S. et al. Antitumorigenic effects of HIV protease inhibitor ritonavir: inhibition of Kaposi sarcoma. Blood 99, 3771–3779 (2002).
  Article CAS Google Scholar
• Sgadari, C. et al. HIV protease inhibitors are potent anti-angiogenic molecules and promote regression of Kaposi sarcoma. Nat. Med. 8, 225–232 (2002).
  Article CAS Google Scholar
• Hosseini, H. et al. Protection against experimental autoimmune encephalomyelitis by a proteasome modulator. J. Neurobiol. 118, 233–244 (2001).
  CAS Google Scholar
• Zollner, T.M. et al. Proteasome inhibition reduces superantigen-mediated T cell activation and the severity of psoriasis in a SCID-hu model. J. Clin. Invest. 109, 671–679 (2002).
  Article CAS Google Scholar
• Luo, H. et al. A proteasome inhibitor effectively prevents mouse heart allograft rejection. Transplantation 72, 196–202 (2001).
  Article CAS Google Scholar
• Rock, K.L. & Goldberg, A.L. Degradation of cell proteins and the generation of MHC class I–presented peptides. Annu. Rev. Immunol. 17, 739–779 (1999).
  Article CAS Google Scholar
• Rubinsztein, D.C. Lessons from animal models of Huntington's disease. Trends Genet. 18, 202–209 (2002).
  Article CAS Google Scholar
• Wong, P.C., Cai, H., Borchelt, D.R. & Price, D.L. Genetically engineered mouse models of neurodegenerative diseases. Nat. Neurosci. 5, 633–639 (2002).
  Article CAS Google Scholar
• Dantuma, N.P., Lindsten, K., Glas, R., Jellne, M. & Masucci, M.G. Short-lived green fluorescent proteins for quantification of ubiquitin/proteasome-dependent proteolysis in living cells. Nat. Biotechnol. 18, 538–543 (2000).
  Article CAS Google Scholar
• Johnson, E.S., Ma, P.C., Ota, I.M. & Varshavsky, A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442–17456 (1995).
  Article CAS Google Scholar
• Okabe, M., Ikawa, M., Kominami, K., Nakanishi, T. & Nishimune, Y. 'Green mice' as a source of ubiquitous green cells. FEBS Lett. 407, 313–319 (1997).
  Article CAS Google Scholar
• Jensen, T.J. et al. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129–135 (1995).
  Article CAS Google Scholar
• McCormack, T. et al. Active site-directed inhibitors of Rhodococcus 20 S proteasome. Kinetics and mechanism. J. Biol. Chem. 272, 26103–26109 (1997).
  Article CAS Google Scholar
• Bogyo, M. et al. Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proc. Natl. Acad. Sci. USA 94, 6629–6634 (1997).
  Article CAS Google Scholar
• Kisselev, A.F. & Goldberg, A.L. Proteasome inhibitors: from research tools to drug candidates. Chem. Biol. 8, 739–758 (2001).
  Article CAS Google Scholar
• Myung, J., Kim, K.B., Lindsten, K., Dantuma, N.P. & Crews, C.M. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors. Mol. Cell 7, 411–420 (2001).
  Article CAS Google Scholar
• van Leeuwen, F.W. et al. Frameshift mutants of β-amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 279, 242–247 (1998).
  Article CAS Google Scholar
• Perutz, M.F. & Windle, A.H. Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats. Nature 412, 143–144 (2001).
  Article CAS Google Scholar
• Sisodia, S.S. Nuclear inclusions in glutamine repeat disorders: are they pernicious, coincidental, or beneficial? Cell 95, 1–4 (1998).
  Article CAS Google Scholar
• Lindsten, K. & Dantuma, N.P. Monitoring the ubiquitin/proteasome system in conformational diseases. Ageing Res. Rev. in the press.
• French, B.A. et al. Aggresome formation in liver cells in response to different toxic mechanisms: role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin. Exp. Mol. Pathol. 71, 241–246 (2001).
  Article CAS Google Scholar
• Denk, H., Stumptner, C. & Zatloukal, K. Mallory bodies revisited. J. Hepatol. 32, 689–702 (2000).
  Article CAS Google Scholar
• Dallaporta, B. et al. Proteasome activation as a critical event of thymocyte apoptosis. Cell Death Differ. 7, 368–373 (2000).
  Article CAS Google Scholar
• Yang, Y., Fang, S., Jensen, J.P., Weissman, A.M. & Ashwell, J.D. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288, 874–877 (2000).
  Article CAS Google Scholar
• Naldini, L. et al. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272, 263–267 (1996).
  Article CAS Google Scholar