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Enhancement of proteasome activity by a small-molecule inhibitor of USP14

Lee, Byung-Hoon, Lee, Min Jae, Park, Soyeon, Oh, Dong-Chan, Elsasser, Suzanne, Chen, Ping-Chung, Gartner, Carlos, Dimova, Nevena, Hanna, John, Gygi, Steven P., Wilson, Scott M., King, Randall W., Finley, Daniel·2010·Nature
DOI 10.1038/nature09299PMC PMC2939003
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Crossref · 10.1038/nature09299

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  • Enhancement of proteasome activity by deubiquitylase inhibitors or proteasome activators accelerates the clearance of toxic proteins in human cultured cells.

    “Likewise, the enhancement of proteasome activity by deubiquitylase inhibitors or proteasome activators accelerates the clearance of toxic proteins in human cultured cells (Lee et al., 2010), and extends replicative lifespan in yeast (Kruegel et al., 2011).”

    From The Hallmarks of Aging (2013) · cites this paper as Lee et al., 2010

    In “A Usp14 inhibitor accelerates proteolysis in cells” (page unavailable), the paper reports that the deubiquitylase inhibitor IU1 enhanced degradation of Tau and depleted other proteins implicated in proteotoxicity, but those experiments used mouse embryonic fibroblasts. It also reports reduced accumulation of oxidized proteins and reduced toxicity in cultured human HEK293 cells. The claim overgeneralizes these findings to deubiquitylase inhibitors or proteasome activators as broader classes, and places the demonstrated clearance of the named toxic proteins in human cells. (LLM, conf=0.87)

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Research works printed but not linked: 60

  1. Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477–513 (2009) · DOI · Paper page
  2. Thrower, J. S., Hoffman, L., Rechsteiner, M. & Pickart, C. M. Recognition of the polyubiquitin proteolytic signal. EMBO J. 19, 94–102 (2000) · DOI
  3. Verma, R. et al. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611–615 (2002) · DOI
  4. Yao, T. & Cohen, R. E. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403–407 (2002) · DOI
  5. 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) · DOI
  6. 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) · DOI
  7. 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) · DOI
  8. 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) · DOI
  9. 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) · DOI
  10. Leggett, D. S. et al. Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10, 495–507 (2002) · DOI
  11. 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) · DOI
  12. 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) · DOI
  13. Anderson, C. et al. Loss of Usp14 results in reduced levels of ubiquitin in ataxia mice. J. Neurochem. 95, 724–731 (2005) · DOI
  14. Hu, M. et al. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme Usp14. EMBO J. 24, 3747–3756 (2005) · DOI
  15. Hanna, J. et al. Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell 127, 99–111 (2006) · DOI
  16. Hanna, J., Meides, A., Zhang, D. P. & Finley, D. A ubiquitin stress response induces altered proteasome composition. Cell 129, 747–759 (2007) · DOI
  17. Crimmins, S. et al. Transgenic rescue of ataxia mice with neuronal-specific expression of ubiquitin-specific protease 14. J. Neurosci. 26, 11423–11431 (2006) · DOI
  18. Crimmins, S. et al. Transgenic rescue of ataxia mice reveals a male-specific sterility defect. Dev. Biol. 325, 33–42 (2009) · DOI
  19. 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) · DOI
  20. 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) · DOI
  21. Catic, A. et al. Screen for ISG15-crossreactive deubiquitinases. PLoS ONE 2, e679 (2007) · DOI
  22. Wang, X. et al. Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry 46, 3553–3565 (2007) · DOI · Paper page
  23. Yao, T. et al. Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nature Cell Biol. 8, 994–1002 (2006) · DOI
  24. 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) · DOI
  25. 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) · DOI
  26. David, D. C. et al. Proteasomal degradation of tau protein. J. Neurochem. 83, 176–185 (2002) · DOI · Paper page
  27. 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) · DOI
  28. Varshavsky, A., Turner, G., Du, F. & Xie, Y. The ubiquitin system and the N-end rule pathway. Biol. Chem. 381, 779–789 (2000) · DOI
  29. 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) · DOI · Paper page
  30. 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) · DOI
  31. Kirkpatrick, D. S. et al. Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology. Nature Cell Biol. 8, 700–710 (2006) · DOI
  32. Amerik, A. Y., Li, S. J. & Hochstrasser, M. Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae . Biol. Chem. 381, 981–992 (2000) · DOI
  33. 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) · DOI
  34. 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) · DOI
  35. 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) · DOI
  36. Stadtman, E. R. Protein oxidation and aging. Free Radic. Res. 40, 1250–1258 (2006) · DOI
  37. 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) · DOI
  38. Hamazaki, J. et al. A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J. 25, 4524–4536 (2006) · DOI
  39. 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) · DOI
  40. Husnjak, K. et al. Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453, 481–488 (2008) · DOI
  41. Chauhan, D., Bianchi, G. & Anderson, K. C. Targeting the UPS as therapy in multiple myeloma. BMC Biochem. 9 (Suppl. 1). S1 (2008) · DOI
  42. 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) · DOI
  43. 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) · DOI
  44. 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) · DOI
  45. Lehman, N. L. The ubiquitin proteasome system in neuropathology. Acta Neuropathol. 118, 329–347 (2009) · DOI
  46. 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) · DOI
  47. Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Adapting proteostasis for disease intervention. Science 319, 916–919 (2008) · DOI · Paper page
  48. Sowa, M. E., Bennett, E. J., Gygi, S. P. & Harper, J. W. Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389–403 (2009) · DOI
  49. Elsasser, S., Schmidt, M. & Finley, D. Characterization of the proteasome using native gel electrophoresis. Methods Enzymol. 398, 353–363 (2005) · DOI
  50. 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) · DOI
  51. 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) · DOI
  52. Park, S. et al. Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature 459, 866–870 (2009) · DOI
  53. Malo, N., Hanley, J., Cerquozzi, S., Pelletier, J. & Nadon, R. Statistical practice in high-throughput screening data analysis. Nature Biotechnol. 24, 167–175 (2006) · DOI · Paper page
  54. 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) · DOI
  55. Mizushima, N., Yoshimori, T. & Levine, B. Methods in mammalian autophagy research. Cell 140, 313–326 (2010) · DOI · Paper page
  56. Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65, 55–63 (1983) · DOI · Paper page
  57. 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) · DOI
  58. Jordan, M. A., Thrower, D. & Wilson, L. Mechanism of inhibition of cell proliferation by Vinca Alkaloids. Cancer Res. 51, 2212–2222 (1991)
  59. Chondrogianni, N. et al. Central role of the proteasome in senescence and survival of human fibroblasts. J. Biol. Chem. 278, 28026–28037 (2003) · DOI
  60. Kwak, M. K. et al. Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol. Cell. Biol. 23, 8786–8794 (2003) · DOI

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Metadata

Authors
Lee, B.-H., Lee, M. J., Park, S., Oh, D.-C., Elsasser, S., Chen, P.-C., Gartner, C., Dimova, N., Hanna, J., Gygi, S. P., Wilson, S. M., King, R. W., & Finley, D.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2010-09
Volume
467
Issue
7312
Pages
179-184
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature09299
PMC
PMC2939003
Cited by
893
References
4
Language
en
Licence
www.springer.com/tdm (tdm)

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