ATP-Dependent Inactivation and Sequestration of Ornithine Decarboxylase by the 26S Proteasome Are Prerequisites for Degradation

REFERENCES

• Armon, T., D. Ganoth, and J. Hershko 1990. Assembly of the 26S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity. J. Biol. Chem. 265:20723–20726.
   PubMedGoogle Scholar
• Auvinen, M., A. Paasinen, L. C. Andersson, and J. Hölttä 1992. Ornithine decarboxylase activity is critical for cell transformation. Nature 360:355–359.
   PubMed Web of Science ®Google Scholar
• Baumeister, W., J. Walz, F. Zuhl, and J. Seemuller 1998. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92:367–380.
   PubMed Web of Science ®Google Scholar
• Bercovich, Z., and J. Kahana 1993. Involvement of the 20S proteasome in the degradation of ornithine decarboxylase. Eur. J. Biochem. 213:205–210.
   PubMedGoogle Scholar
• Chu-Ping, M., J. H. Vu, R. J. Proske, C. A. Slaughter, and J. DeMartino 1994. Identification, purification, and characterization of a high molecular weight ATP-dependent activator (PA700) of the 20S proteasome. J. Biol. Chem. 269:3539–3547.
   PubMed Web of Science ®Google Scholar
• Coffino, P. 1998. Degradation of ornithine decarboxylase, p. 411–428. In J.-M. Peters, J. D. Harris, D. Finley (ed.), Ubiquitin and the biology of the cell. Plenum Press, New York, N.Y.
   Google Scholar
• Coleman, C. S., B. A. Stanley, R. Viswanath, and J. Pegg 1994. Rapid exchange of subunits of mammalian ornithine decarboxylase. J. Biol. Chem. 269:3155–3158.
   PubMedGoogle Scholar
• Coux, O., K. Tanaka, and J. Goldberg 1996. Structure and function of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:801–847.
   PubMed Web of Science ®Google Scholar
• Deveraux, Q., S. van Nocker, D. Mahaffey, R. Vierstra, and J. Rechsteiner 1995. Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26S protease subunit S5a. J. Biol. Chem. 270:29660–29663.
   PubMed Web of Science ®Google Scholar
• Dick, L. R., A. A. Cruikshank, A. T. Destree, L. Grenier, T. A. McCormack, F. D. Melandri, S. L. Nunes, V. T. Palombella, L. A. Perent, L. Plamondon, and J. Stein 1997. Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells. J. Biol. Chem. 272:182–188.
   PubMed Web of Science ®Google Scholar
• Elias, S., B. Bercovich, C. Kahana, P. Coffino, M. Fischer, W. Hilt, D. H. Wolf, and J. Ciechanover 1995. Degradation of ornithine decarboxylase by the mammalian and yeast 26S proteasome complexes requires all the components of the protease. Eur. J. Biochem. 229:276–283.
   PubMedGoogle Scholar
• Feldman, S. R., S. L. Gonias, and J. Pizzo 1985. Model of α2-macroglobulin structure and function. Proc. Natl. Acad. Sci. USA 82:5700–5704.
   PubMedGoogle Scholar
• Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and J. Schreiber 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726–731.
   PubMed Web of Science ®Google Scholar
• Finley, D., K. Tanaka, C. Mann, H. Feldmann, M. Hochstrasser, R. Vierstra, S. Johnston, R. Hampton, J. Haber, P. Silver et al.. 1998. Unified nomenclature for subunits of the S. cerevisiae proteasome regulatory particle. Trends Biochem. Sci. 271:244–245.
   Google Scholar
• Ghoda, L., T. van Daalen Wetters, M. Macrae, D. Ascherman, and J. Coffino 1989. Prevention of rapid intracellular degradation of ODC by a carboxy-terminal truncation. Science 243:1493–1495.
   PubMedGoogle Scholar
• Glickman, M. H., D. M. Rubin, O. Coux, I. Wefes, G. Pfeifer, Z. Cjeka, W. Baumeister, V. A. Fried, and J. Finley 1998. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9 signalosome and elF3. Cell 94:615–623.
   PubMed Web of Science ®Google Scholar
• Groll, M., L. Ditzel, J. Lowe, D. Stock, M. Bochtler, H. D. Bartnik, and J. Huber 1997. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386:463–471.
   PubMed Web of Science ®Google Scholar
• Hayashi, S., Y. Murakami, and J. Matsufuji 1996. Ornithine decarboxylase antizyme: a novel type of regulatory protein. Trends Biochem. Sci. 21:27–30.
   PubMed Web of Science ®Google Scholar
• Hershko, A., and J. Ciechanover 1998. The ubiquitin system. Annu. Rev. Biochem. 67:425–479.
   PubMed Web of Science ®Google Scholar
• Hochstrasser, M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:405–439.
   PubMed Web of Science ®Google Scholar
• Hoffman, L., and J. Rechsteiner 1996. Nucleotidase activities of the 26S proteasome and its regulatory complex. J. Biol. Chem. 271:32538–32545.
   PubMedGoogle Scholar
• Hoffman, L., G. Pratt, and J. Rechsteiner 1992. Multiple forms of 20S multicatalytic and the 26S ubiquitin/ATP-dependent proteases from rabbit reticulocyte lysate. J. Biol. Chem. 267:22362–22368.
   PubMed Web of Science ®Google Scholar
• Li, X., and J. Coffino 1993. Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-indelible inhibitory protein. Mol. Cell. Biol. 13:2377–2383.
   PubMed Web of Science ®Google Scholar
• Li, X., B. Stubbiness, L. Hoffman, G. Pratt, M. Rechsteiner, and J. Coffino 1996. The N-terminus of antizyme promotes degradation of heterologous proteins. J. Biol. Chem. 271:4441–4446.
   PubMedGoogle Scholar
• Lin, L., G. N. DeMartino, and J. Greene 1998. Cotranslational biogenesis of NF-κB p50 by the 26S proteasome. Cell 92:819–828.
   PubMed Web of Science ®Google Scholar
• Mamroud-Kidron, E., M. Omer-Itsicovich, Z. Bercovich, K. Tobias, E. Rom, and J. Kahana 1994. A unified pathway for degradation of ornithine decarboxylase in reticulocytes requires interaction with the polyamine-induced protein, ornithine decarboxylase antizyme. Eur. J. Biochem. 226:547–555.
   PubMedGoogle Scholar
• Matsufuji, S., K. Fujita, T. Kameji, R. Kanamoto, Y. Murakami, and J. Hayashi 1984. Monoclonal antibody to rat liver ornithine decarboxylase. J. Biochem. 96:1525–1530.
   PubMedGoogle Scholar
• Matsufuji, S., R. Kanamoto, Y. Murakamia, and J. Hayashi 1990. Monoclonal antibody studies on the properties and regulation of murine ornithine decarboxylase antizyme. J. Biochem. 107:87–91.
   PubMedGoogle Scholar
• Matsufuji, S., Y. Miyazaki, R. Kanamoto, T. Kameji, Y. Murakami, T. G. Baby, K. Fujita, T. Ohno, and J. Hayashi 1990. Analyses of ornithine decarboxylase antizyme mRNA with a cDNA cloned from rat liver. J. Biochem. 108:365–371.
   PubMedGoogle Scholar
• Matsufuji, S., T. Matsufuji, Y. Miyazaki, Y. Murakami, J. F. Atkins, R. F. Gesteland, and J. Hayashi 1995. Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme. Cell 80:51–60.
   PubMed Web of Science ®Google Scholar
• Mitchell, J. L., and J. Chen 1990. Conformational changes in ornithine decarboxylase enable recognition by antizyme. Biochim. Biophys. Acta 1037:115–121.
   PubMedGoogle Scholar
• Mitchell, J. L., G. G. Judd, and J. Bareyal-Leyser 1994. Feedback repression of polyamine transport is mediated by antizyme in mammalian tissue-culture cells. Biochem. J. 299:19–22.
   PubMedGoogle Scholar
• Mitchell, J. L. A., C.-Y. Choe, G. G. Judd, D. J. Daghfal, R. J. Kurzeja, and J. Leyser 1996. Overproduction of stable ornithine decarboxylase and antizyme in the difluoromethylornithine-resistant cell line DH23b. Biochem. J. 317:811–816.
   PubMedGoogle Scholar
• Miyazaki, Y., S. Matsufuji, Y. Murakami, and J. Hayashi 1993. Single amino-acid replacement is responsible for the stabilization of ornithine decarboxylase in HMOA cells. Eur. J. Biochem. 214:837–844.
   PubMedGoogle Scholar
• Moshier, J. A., J. Dosescu, M. Skunca, and J. Luk 1993. Transformation of NIH/3T3 cells by ornithine decarboxylase overexpression. Cancer Res. 53:2618–2622.
   PubMed Web of Science ®Google Scholar
• Murakami, Y., K. Fujita, T. Kameji, and J. Hayashi 1985. Accumulation of ornithine decarboxylase-antizyme complex in HMOA cells. Biochem. J. 225:689–697.
   PubMedGoogle Scholar
• Murakami, Y., T. Ichiba, S. Matsufuji, and J. Hayashi 1996. Cloning of antizyme inhibitor, a highly homologous protein to ornithine decarboxylase. J. Biol. Chem. 271:3340–3342.
   PubMedGoogle Scholar
• Murakami, Y., S. Matsufuji, T. Kameji, S. Hayashi, K. Igarashi, T. Tamura, K. Tanaka, and J. Ichihara 1992. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 360:597–599.
   PubMed Web of Science ®Google Scholar
• Murakami, Y., K. Tanaka, S. Matsufuji, Y. Miyazaki, and J. Hayashi 1992. Antizyme, a protein induced by polyamines, accelerates the degradation of ornithine decarboxylase in Chinese hamster ovary-cell extracts. Biochem. J. 283:661–664.
   PubMedGoogle Scholar
• Nishiyama, M., S. Matsufuji, R. Kanamoto, M. Takano, Y. Murakami, and J. Hayashi 1988. Two-step purification of mouse kidney ornithine decarboxylase. Prep. Biochem. 18:227–238.
   PubMed Web of Science ®Google Scholar
• Piotrowski, J., R. Beal, L. Hoffman, K. D. Wilkinson, R. Cohen, and J. Pickart 1997. Inhibition of the 26S proteasome by polyubiquitin chains synthesized to have defined lengths. J. Biol. Chem. 272:23712–23721.
   PubMed Web of Science ®Google Scholar
• Pritchard, M. L., A. E. Pegg, and J. Jefferson 1982. Ornithine decarboxylase from hepatoma cells and a variant cell line in which the enzyme is more stable. J. Biol. Chem. 257:5892–5899.
   PubMedGoogle Scholar
• Poulin, R., G. Pelletier, and J. Pegg 1995. Induction of apoptosis by excessive polyamine accumulation in ornithine decarboxylase-overproducing L1210 cells. Biochem. J. 311:723–727.
   PubMed Web of Science ®Google Scholar
• Rechsteiner, M. 1998. The 26S proteasomes, p. 147–189. In J.-M. Peters, J. D. Harris, D. Finley (ed.), Ubiquitin and the biology of the cell. Plenum Press, New York, N.Y.
   Google Scholar
• Rom, E., and J. Kahana 1994. Polyamines regulate the expression of ornithine decarboxylase antizyme in vitro by inducing ribosomal frame-shifting. Proc. Natl. Acad. Sci. USA 91:3959–3963.
   PubMedGoogle Scholar
• Suzuki, T., Y. He, K. Kashiwagi, Y. Murakami, S. Hayashi, and J. Igarashi 1994. Antizyme protects against abnormal accumulation and toxicity of polyamines in ornithine decarboxylase-overproducing cells. Proc. Natl. Acad. Sci. USA 91:8930–8934.
   PubMedGoogle Scholar
• Tanaka, K. 1998. Molecular biology of the proteasome. Biochem. Biophys. Res. Commun. 247:537–541.
   PubMedGoogle Scholar
• Tanaka, K., N. Tanahashi 1997. Preparation of proteasomes, p. 129–134 In J. E. Celis (ed.), Cell biology: a laboratory handbook, 2nd ed. Academic Press, New York, N.Y.
   Google Scholar
• Tokunaga, F., T. Goto, T. Koide, Y. Murakami, S. Hayashi, T. Tamura, K. Tanaka, and J. Ichihara 1994. ATP- and antizyme-dependent endoproteolysis of ornithine decarboxylase to oligopeptides by the 26S proteasome. J. Biol. Chem. 269:17382–17385.
   PubMedGoogle Scholar