FAT10, a Ubiquitin-Independent Signal for Proteasomal Degradation

REFERENCES

• Bates, E. F. M., O. Ravel, M. C. Dieu, S. Ho, C. Guret, J. M. Bridon, S. Ait-Yahia, F. Briere, C. Caux, J. Banchereau, and S. Lebecque. 1997. Identification and analysis of a novel member of the ubiquitin family expressed in dendritic cells and mature B cells. Eur. J. Immunol. 27:2471–2477.
   PubMed Web of Science ®Google Scholar
• Bossis, G., P. Ferrara, C. Acquaviva, I. Jariel-Encontre, and M. Piechaczyk. 2003. c-Fos proto-oncoprotein is degraded by the proteasome independently of its own ubiquitinylation in vivo. Mol. Cell. Biol. 23:7425–7436.
   PubMedGoogle Scholar
• Chowdary, D. R., J. J. Dermody, K. K. Jha, and H. L. Ozer. 1994. Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway. Mol. Cell. Biol. 14:1997–2003.
   PubMed Web of Science ®Google Scholar
• Ciechanover, A., and R. Ben-Saadon. 2004. N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol. 14:103–106.
   PubMed Web of Science ®Google Scholar
• Elsasser, S., R. R. Gali, M. Schwickart, C. N. Larsen, D. S. Leggett, B. Muller, M. T. Feng, F. Tubing, G. A. G. Dittmar, and D. Finley. 2002. Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat. Cell Biol. 4:725–730.
   PubMed Web of Science ®Google Scholar
• Fan, W., W. Cai, S. Parimoo, G. G. Lennon, and S. M. Weissman. 1996. Identification of seven new human MHC class I region genes around the HLA-F locus. Immunogenetics 44:97–103.
   PubMed Web of Science ®Google Scholar
• Funakoshi, M., T. Sasaki, T. Nishimoto, and H. Kobayashi. 2002. Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc. Natl. Acad. Sci. USA 99:745–750.
   PubMedGoogle Scholar
• Gropper, R., R. A. Brandt, S. Elias, C. F. Bean, A. Mayer, A. L. Schwartz, and A. Ciechanover. 1991. The ubiquitin-activating enzyme, E1, is required for stress induced lysosomal degradation of cellular proteins. J. Biol. Chem. 266:3602–3610.
   PubMed Web of Science ®Google Scholar
• Haas, A. L., and P. M. Bright. 1987. The dynamics of ubiquitin pools within cultured human lung fibroblasts. J. Biol. Chem. 262:345–351.
   PubMedGoogle Scholar
• Handley-Gearhart, P. M., J. S. Trausch-Azar, A. Ciechanover, and A. L. Schwartz. 1994. Rescue of the complex temperature-sensitive phenotype of Chinese hamster ovary E36ts20 cells by expression of the human ubiquitin-activating enzyme cDNA. Biochem. J. 304:1015–1020.
   PubMedGoogle Scholar
• Hershko, A., and A. Ciechanover. 1998. The ubiquitin system. Annu. Rev. Biochem. 67:425–479.
   PubMed Web of Science ®Google Scholar
• Hipp, M. S., S. Raasi, M. Groettrup, and G. Schmidtke. 2004. NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation. J. Biol. Chem. 279:16503–16510.
   PubMed Web of Science ®Google Scholar
• Janse, D. M., B. Crosas, D. Finley, and G. M. Church. 2004. Localization to the proteasome is sufficient for degradation. J. Biol. Chem. 279:21415–21420.
   PubMed Web of Science ®Google Scholar
• Jentsch, S., and G. Pyrowolakis. 2000. Ubiquitin and its kin: how close are the family ties. Trends Cell Biol. 10:335–342.
   PubMedGoogle Scholar
• Johnson, E. S., B. Bartel, W. Seufert, and A. Varshavsky. 1992. Ubiquitin as a degradation signal. EMBO J. 11:497–505.
   PubMedGoogle Scholar
• Kamitani, T., K. Kito, T. Fukuda-Kamitani, and E. T. H. Yeh. 2001. Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1. J. Biol. Chem. 276:46655–46660.
   PubMed Web of Science ®Google Scholar
• Kito, K., E. T. H. Yeh, and T. Kamitani. 2001. NUB1, a NEDD8-interacting protein, is induced by interferon and down-regulates the NEDD8 expression. J. Biol. Chem. 276:20603–20609.
   PubMed Web of Science ®Google Scholar
• Kulka, R. G., B. Raboy, R. Schuster, H. A. Parag, G. Diamond, A. Ciechanover, and M. Marcus. 1988. A Chinese hamster cell cycle mutant arrested at G2 phase has a temperature-sensitive ubiquitin-activating enzyme, E1. J. Biol. Chem. 263:15726–15731.
   PubMedGoogle Scholar
• Lee, C. G., J. Ren, I. S. Cheong, K. H. Ban, L. L. Ooi, S. Yong Tan, A. Kan, I. Nuchprayoon, R. Jin, K. H. Lee, M. Choti, and L. A. Lee. 2003. Expression of the FAT10 gene is highly upregulated in hepatocellular carcinoma and other gastrointestinal and gynecological cancers. Oncogene 22:2592–2603.
   PubMed Web of Science ®Google Scholar
• Leggett, D. S., J. Hanna, A. Borodovsky, B. Crosas, M. Schmidt, R. T. Baker, T. Walz, H. Ploegh, and D. Finley. 2002. Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10:495–507.
   PubMed Web of Science ®Google Scholar
• Levy, F., N. Johnsson, T. Rümenapf, and A. Varshavsky. 1996. Using ubiquitin to follow the metabolic fate of a protein. Proc. Natl. Acad. Sci. USA 93:4907–4912.
   PubMedGoogle Scholar
• Liu, C. W., M. J. Corboy, G. N. DeMartino, and P. J. Thomas. 2003. Endoproteolytic activity of the proteasome. Science 299:408–411.
   PubMed Web of Science ®Google Scholar
• Liu, Y., J. Pan, C. Zhang, W. Fan, M. Collinge, J. R. Bender, and S. M. Weissman. 1999. A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2. Proc. Natl. Acad. Sci. USA 96:4313–4318.
   PubMedGoogle Scholar
• Luders, J., J. Demand, and J. Hohfeld. 2000. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 275:4613–4617.
   PubMed Web of Science ®Google Scholar
• Murakami, Y., S. Matsufuji, T. Kameji, S. Hayashi, K. Igarashi, T. Tamura, K. Tanaka, and A. Ichihara. 1992. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 360:597–599.
   PubMed Web of Science ®Google Scholar
• Neff, N. T., L. Bourret, P. Miao, and J. F. Dice. 1981. Degradation of proteins microinjected into IMR-90 human diploid fibroblasts. J. Cell Biol. 91:184–194.
   PubMedGoogle Scholar
• Polevoda, B., and F. Sherman. 2003. N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins. J. Mol. Biol. 325:595–622.
   PubMed Web of Science ®Google Scholar
• Raasi, S., G. Schmidtke, R. D. Giuli, and M. Groettrup. 1999. A ubiquitin-like protein which is synergistically inducible by interferon-γ and tumor necrosis factor-α. Eur. J. Immunol. 29:4030–4036.
   PubMedGoogle Scholar
• Raasi, S., G. Schmidtke, and M. Groettrup. 2001. The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis. J. Biol. Chem. 276:35334–35343.
   PubMedGoogle Scholar
• Schauber, C., L. Chen, P. Tongaonkar, I. Vega, D. Lambertson, W. Potts, and K. Madura. 1998. Rad23 links DNA repair to the ubiquitin/proteasome pathway. Nature 391:715–718.
   PubMed Web of Science ®Google Scholar
• Sheaff, R. J., J. D. Singer, J. Swanger, M. Smitherman, J. M. Roberts, and B. E. Clurman. 2000. Proteasomal turnover of p21Cip1 does not require p21Cip1 ubiquitination. Mol. Cell 5:403–410.
   PubMed Web of Science ®Google Scholar
• Stancovski, I., H. Gonen, A. Orian, A. L. Schwartz, and A. Ciechanover. 1995. Degradation of the proto-oncogene product c-Fos by the ubiquitin proteolytic system in vivo and in vitro: identification and characterization of the conjugating enzymes. Mol. Cell. Biol. 15:7106–7116.
   PubMed Web of Science ®Google Scholar
• Swaminathan, S., A. Y. Amerik, and M. Hochstrasser. 1999. The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Mol. Biol. Cell 10:2583–2594.
   PubMed Web of Science ®Google Scholar
• Tanaka, T., H. Kawashima, E. T. H. Yeh, and T. Kamitani. 2003. Regulation of the NEDD8 conjugation system by a splicing variant, NUB1L. J. Biol. Chem. 278:32905–32913.
   PubMed Web of Science ®Google Scholar
• Thrower, J. S., L. Hoffman, M. Rechsteiner, and C. M. Pickart. 2000. Recognition of the polyubiquitin proteolytic signal. EMBO J. 19:94–102.
   PubMed Web of Science ®Google Scholar
• Turner, G. C., and A. Varshavsky. 2000. Detecting and measuring cotranslational protein degradation in vivo. Science 289:2117–2120.
   PubMed Web of Science ®Google Scholar
• Voges, D., P. Zwickl, and W. Baumeister. 1999. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68:1015–1068.
   PubMed Web of Science ®Google Scholar
• Wilkinson, K. D. 2000. Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Semin. Cell Dev. Biol. 11:141–148.
   PubMed Web of Science ®Google Scholar
• Zhang, M. S., C. M. Pickart, and P. Coffino. 2003. Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate. EMBO J. 22:1488–1496.
   PubMed Web of Science ®Google Scholar