Enhancement of proteasome activity by a small-molecule inhibitor of USP14 (original) (raw)

• Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477–513 (2009)
  Article CAS Google Scholar
• Schrader, E. K., Harstad, K. G. & Matouschek, A. Targeting proteins for degradation. Nature Chem. Biol. 5, 815–822 (2009)
  Article CAS Google Scholar
• Thrower, J. S., Hoffman, L., Rechsteiner, M. & Pickart, C. M. Recognition of the polyubiquitin proteolytic signal. EMBO J. 19, 94–102 (2000)
  Article CAS Google Scholar
• Verma, R. et al. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611–615 (2002)
  Article ADS CAS Google Scholar
• Yao, T. & Cohen, R. E. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403–407 (2002)
  Article ADS CAS Google Scholar
• Lam, Y. A., Xu, W., DeMartino, G. N. & Cohen, R. E. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385, 737–740 (1997)
  Article ADS CAS Google Scholar
• Koulich, E., Li, X. & DeMartino, G. N. Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol. Biol. Cell 19, 1072–1082 (2008)
  Article CAS Google Scholar
• Jacobson, A. D. et al. The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26S proteasome. J. Biol. Chem. 284, 35485–35494 (2009)
  Article CAS Google Scholar
• Verma, R. et al. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 11, 3425–3439 (2000)
  Article CAS Google Scholar
• Borodovsky, A. et al. A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO J. 20, 5187–5196 (2001)
  Article CAS Google Scholar
• Leggett, D. S. et al. Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10, 495–507 (2002)
  Article CAS Google Scholar
• Wilson, S. M. et al. Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease. Nature Genet. 32, 420–425 (2002)
  Article CAS Google Scholar
• Chernova, T. A. et al. Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. J. Biol. Chem. 278, 52102–52115 (2003)
  Article CAS Google Scholar
• Anderson, C. et al. Loss of Usp14 results in reduced levels of ubiquitin in ataxia mice. J. Neurochem. 95, 724–731 (2005)
  Article CAS Google Scholar
• Hu, M. et al. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme Usp14. EMBO J. 24, 3747–3756 (2005)
  Article CAS Google Scholar
• Hanna, J. et al. Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell 127, 99–111 (2006)
  Article CAS Google Scholar
• Hanna, J., Meides, A., Zhang, D. P. & Finley, D. A ubiquitin stress response induces altered proteasome composition. Cell 129, 747–759 (2007)
  Article CAS Google Scholar
• Crimmins, S. et al. Transgenic rescue of ataxia mice with neuronal-specific expression of ubiquitin-specific protease 14. J. Neurosci. 26, 11423–11431 (2006)
  Article CAS Google Scholar
• Crimmins, S. et al. Transgenic rescue of ataxia mice reveals a male-specific sterility defect. Dev. Biol. 325, 33–42 (2009)
  Article CAS Google Scholar
• Chen, P.-C. et al. The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions. J. Neurosci. 29, 10909–10919 (2009)
  Article CAS Google Scholar
• Peth, A., Besche, H. C. & Goldberg, A. L. Ubiquitinated proteins activate the proteasome by binding to Usp14/Upb6, which cause 20S gate opening. Mol. Cell 36, 794–804 (2009)
  Article CAS Google Scholar
• Catic, A. et al. Screen for ISG15-crossreactive deubiquitinases. PLoS ONE 2, e679 (2007)
  Article ADS Google Scholar
• Wang, X. et al. Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry 46, 3553–3565 (2007)
  Article CAS Google Scholar
• Yao, T. et al. Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nature Cell Biol. 8, 994–1002 (2006)
  Article CAS Google Scholar
• Spires-Jones, T. L., Stoothoff, W. H., de Calignon, A., Jones, P. B. & Hyman, B. T. Tau pathophysiology in neurodegeneration: a tangled issue. Trends Neurosci. 32, 150–159 (2009)
  Article CAS Google Scholar
• Kwong, L. K., Uryu, K., Trojanowski, J. Q. & Lee, V. M. TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis. Neurosignals 16, 41–51 (2008)
  Article CAS Google Scholar
• David, D. C. et al. Proteasomal degradation of tau protein. J. Neurochem. 83, 176–185 (2002)
  Article CAS Google Scholar
• Petrucelli, L. et al. CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum. Mol. Genet. 13, 703–714 (2004)
  Article CAS Google Scholar
• Todi, S. V. et al. Cellular turnover of the polyglutamine disease protein ataxin-3 is regulated by its catalytic activity. J. Biol. Chem. 282, 29348–29358 (2007)
  Article CAS Google Scholar
• Varshavsky, A., Turner, G., Du, F. & Xie, Y. The ubiquitin system and the N-end rule pathway. Biol. Chem. 381, 779–789 (2000)
  Article CAS Google Scholar
• Dantuma, N. P., Lindsten, K., Glas, R., Jellne, M. & Masucci, M. G. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nature Biotechnol. 18, 538–543 (2000)
  Article CAS Google Scholar
• Saeki, Y., Isono, E. & Toh-E, A. Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring proteasome activity. Methods Enzymol. 399, 215–227 (2005)
  Article CAS Google Scholar
• Kirkpatrick, D. S. et al. Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology. Nature Cell Biol. 8, 700–710 (2006)
  Article CAS Google Scholar
• Amerik, A. Y., Li, S. J. & Hochstrasser, M. Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae . Biol. Chem. 381, 981–992 (2000)
  Article CAS Google Scholar
• Hanna, J., Leggett, D. S. & Finley, D. Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Mol. Cell. Biol. 23, 9251–9261 (2003)
  Article CAS Google Scholar
• Shabek, N., Herman-Bachinsky, Y. & Ciechanover, A. Ubiquitin degradation with its substrate, or as a monomer in a ubiquitination-independent mode, provides clues to proteasome regulation. Proc. Natl Acad. Sci. USA 106, 11907–11912 (2009)
  Article ADS CAS Google Scholar
• Hoyt, M. A., Zhang, M. & Coffino, P. Probing the ubiquitin/proteasome system with ornithine decarboxylase, a ubiquitin-independent substrate. Methods Enzymol. 398, 399–413 (2005)
  Article CAS Google Scholar
• Stadtman, E. R. Protein oxidation and aging. Free Radic. Res. 40, 1250–1258 (2006)
  Article CAS Google Scholar
• Ahmed, E. K., Picot, C. R., Bulteau, A. L. & Friguet, B. Protein oxidative modifications and replicative senescence of WI-38 human embryonic fibroblasts. Ann. NY Acad. Sci. 1119, 88–96 (2007)
  Article ADS CAS Google Scholar
• Hamazaki, J. et al. A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J. 25, 4524–4536 (2006)
  Article CAS Google Scholar
• Qiu, X. B. et al. hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37. EMBO J. 25, 5742–5753 (2006)
  Article CAS Google Scholar
• Husnjak, K. et al. Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453, 481–488 (2008)
  Article ADS CAS Google Scholar
• Chauhan, D., Bianchi, G. & Anderson, K. C. Targeting the UPS as therapy in multiple myeloma. BMC Biochem. 9 (Suppl. 1). S1 (2008)
  Article Google Scholar
• Muchamuel, T. et al. A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis. Nature Med. 15, 781–787 (2009)
  Article CAS Google Scholar
• Chondrogianni, N. et al. Overexpression of proteasome β5 subunit increases the amount of assembled proteasome and confers ameliorated response to oxidative stress and higher survival rates. J. Biol. Chem. 280, 11840–11850 (2005)
  Article CAS Google Scholar
• Tonoki, A. et al. Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process. Mol. Cell. Biol. 29, 1095–1106 (2009)
  Article CAS Google Scholar
• Lehman, N. L. The ubiquitin proteasome system in neuropathology. Acta Neuropathol. 118, 329–347 (2009)
  Article CAS Google Scholar
• Hinault, M. P., Ben-Zvi, A. & Goloubinoff, P. Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging. J. Mol. Neurosci. 30, 249–265 (2006)
  Article CAS Google Scholar
• Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Adapting proteostasis for disease intervention. Science 319, 916–919 (2008)
  Article ADS CAS Google Scholar
• Goldberg, A. L. Protein degradation and protection against misfolded and damaged proteins. Nature 426, 895–899 (2003)
  Article ADS CAS Google Scholar
• Sowa, M. E., Bennett, E. J., Gygi, S. P. & Harper, J. W. Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389–403 (2009)
  Article CAS Google Scholar
• Elsasser, S., Schmidt, M. & Finley, D. Characterization of the proteasome using native gel electrophoresis. Methods Enzymol. 398, 353–363 (2005)
  Article CAS Google Scholar
• Kleijnen, M. F. et al. Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites. Nature Struct. Mol. Biol. 14, 1180–1188 (2007)
  Article CAS Google Scholar
• Kusmierczyk, A. R., Kunjappu, M. J., Funakoshi, M. & Hochstrasser, M. A multimeric assembly factor controls the formation of alternative 20S proteasomes. Nature Struct. Mol. Biol. 15, 237–244 (2008)
  Article CAS Google Scholar
• Park, S. et al. Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature 459, 866–870 (2009)
  Article ADS CAS Google Scholar
• Malo, N., Hanley, J., Cerquozzi, S., Pelletier, J. & Nadon, R. Statistical practice in high-throughput screening data analysis. Nature Biotechnol. 24, 167–175 (2006)
  Article CAS Google Scholar
• Kobayashi, H. et al. Hrs, a mammalian master molecule in vesicular transport and protein sorting, suppresses the degradation of ESCRT proteins signal transducing adaptor molecule 1 and 2. J. Biol. Chem. 280, 10468–10477 (2005)
  Article CAS Google Scholar
• Kuma, A. et al. The role of autophagy during the early neonatal starvation period. Nature 432, 1032–1036 (2004)
  Article ADS CAS Google Scholar
• Mizushima, N., Yoshimori, T. & Levine, B. Methods in mammalian autophagy research. Cell 140, 313–326 (2010)
  Article CAS Google Scholar
• Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65, 55–63 (1983)
  Article CAS Google Scholar
• Li, X., Traganos, F., Melamed, M. R. & Darzynkiewicz, Z. Single-step procedure for labeling DNA strand breaks with fluorescein- or BODIPY-conjugated deoxynucleotides: detection of apoptosis and bromodeoxyuridine incorporation. Cytometry 20, 172–180 (1995)
  Article CAS Google Scholar
• Jordan, M. A., Thrower, D. & Wilson, L. Mechanism of inhibition of cell proliferation by Vinca Alkaloids. Cancer Res. 51, 2212–2222 (1991)
  CAS PubMed Google Scholar
• Chondrogianni, N. et al. Central role of the proteasome in senescence and survival of human fibroblasts. J. Biol. Chem. 278, 28026–28037 (2003)
  Article CAS Google Scholar
• Kwak, M. K. et al. Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol. Cell. Biol. 23, 8786–8794 (2003)
  Article CAS Google Scholar