Overexpression of USP14 protease reduces I-κB protein levels and increases cytokine release in lung epithelial cells

Journal of Biological Chemistry

Volumn 288, Issue 22, 2013, Pages 15437-15441

  Mialki, Rachel K ^a   Zhao, Jing ^a   Wei, Jianxin ^a   Mallampalli, Daniel F ^a   Zhao, Yutong ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INTRACELLULAR PROTEINS; LIPOPOLYSACCHARIDES; LUNG EPITHELIAL CELLS; POLYUBIQUITINATION; PROTEIN DEGRADATION; REGULATORY SUBUNITS; SERINE PHOSPHORYLATION; UBIQUITIN-PROTEASOME SYSTEM;

AMINO ACIDS; CELL DEATH; CELL PROLIFERATION; DEGRADATION; ESCHERICHIA COLI;

PROTEINS;

I KAPPA B; INTERLEUKIN 8; LIPOPOLYSACCHARIDE; PROTEASOME; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN; UBIQUITIN SPECIFIC PROTEASE 14; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CYTOKINE RELEASE; DEUBIQUITINATION; GENE OVEREXPRESSION; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; LUNG ALVEOLUS EPITHELIUM; MOUSE; NONHUMAN; POLYUBIQUITINATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TARGETING; TRANSCRIPTION REGULATION; UBIQUITINATION;

CYTOKINE; DEUBIQUITINATION; NF-ΚB TRANSCRIPTION FACTOR; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; USP14;

ANIMALS; CELL LINE; EPITHELIAL CELLS; ESCHERICHIA COLI; HUMANS; I-KAPPA B PROTEINS; INTERLEUKIN-8; LIPOPOLYSACCHARIDES; LUNG; MICE; PHOSPHORYLATION; PROTEOLYSIS; RESPIRATORY MUCOSA; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR-ALPHA; UBIQUITIN; UBIQUITIN THIOLESTERASE; UBIQUITINATION;

ESCHERICHIA COLI;

EID: 84878393110     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C112.446682     Document Type: Article

References (26)

1. Hershko, A., and Ciechanover, A. (1992) The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61, 761-807
2. Schwartz, A. L., and Ciechanover, A. (1992) Ubiquitin-mediated protein modification and degradation. Am. J. Respir. Cell Mol. Biol. 7, 463-468
3. Ugai, S., Tamura, T., Tanahashi, N., Takai, S., Komi, N., Chung, C. H., Tanaka, K., and Ichihara, A. (1993) Purification and characterization of the 26S proteasome complex catalyzing ATP-dependent breakdown of ubiquitin-ligated proteins from rat liver. J. Biochem. 113, 754-768
4. Saeki, Y., and Tanaka, K. (2012) Assembly and function of the proteasome. Methods Mol. Biol. 832, 315-337
5. Kim, H. M., Yu, Y., and Cheng, Y. (2011) Structure characterization of the 26S proteasome. Biochim. Biophys. Acta 1809, 67-79
6. Adams, J. (2003) The proteasome: structure, function, and role in the cell. Cancer Treat. Rev. 29, Suppl. 1, 3-9
7. Lee, M. J., Lee, B. H., Hanna, J., King, R. W., and Finley, D. (2011) Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Mol. Cell. Proteomics 10, R110.003871
8. Hu, M., Li, P., Song, L., Jeffrey, P. D., Chenova, T. A., Wilkinson, K. D., Cohen, R. E., and Shi, Y. (2005) Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. EMBO J. 24, 3747-3756 (Pubitemid 41581691)
9. Hanna, J., Hathaway, N. A., Tone, Y., Crosas, B., Elsasser, S., Kirkpatrick, D. S., Leggett, D. S., Gygi, S. P., King, R. W., and Finley, D. (2006) Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell 127, 99-111 (Pubitemid 44466645)
10. Peth, A., Besche, H. C., and Goldberg, A. L. (2009) Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening. Mol. Cell 36, 794-804
11. 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., and Finley, D. (2010) Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467, 179-184
12. Crimmins, S., Jin, Y., Wheeler, C., Huffman, A. K., Chapman, C., Dobrunz, L. E., Levey, A., Roth, K. A., Wilson, J. A., and Wilson, S. M. (2006) Transgenic rescue of ataxia mice with neuronal-specific expression of ubiquitin-specific protease 14. J. Neurosci. 26, 11423-11431 (Pubitemid 44772172)
13. Chen, P. C., Qin, L. N., Li, X. M., Walters, B. J., Wilson, J. A., Mei, L., and Wilson, S. M. (2009) 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
14. Mines, M. A., Goodwin, J. S., Limbird, L. E., Cui, F. F., and Fan, G. H. (2009) Deubiquitination of CXCR4 by USP14 is critical for both CXCL12-induced CXCR4 degradation and chemotaxis but not ERK activation. J. Biol. Chem. 284, 5742-5752
15. Shinji, S., Naito, Z., Ishiwata, S., Ishiwata, T., Tanaka, N., Furukawa, K., Suzuki, H., Seya, T., Matsuda, A., Katsuta, M., and Tajiri, T. (2006) Ubiquitin-specific protease 14 expression in colorectal cancer is associated with liver and lymph node metastases. Oncol. Rep. 15, 539-543
16. D'Arcy, P., Brnjic, S., Olofsson, M. H., Fryknäs, M., Lindsten, K., De Cesare, M., Perego, P., Sadeghi, B., Hassan, M., Larsson, R., and Linder, S. (2011) Inhibition of proteasome deubiquitinating activity as a new cancer therapy. Nat. Med. 17, 1636-1640
17. A receptor turnover in mice. PLoS Genet. 5, e1000631
18. Perry, J. W., Ahmed, M., Chang, K. O., Donato, N. J., Showalter, H. D., and Wobus, C. E. (2012) Antiviral activity of a small molecule deubiquitinase inhibitor occurs via induction of the unfolded protein response. PLoS Pathog. 8, e1002783
19. Tak, P. P., and Firestein, G. S. (2001) NF-κB: a key role in inflammatory diseases. J. Clin. Invest. 107, 7-11 (Pubitemid 32047405)
20. Nagai, A., Kadowaki, H., Maruyama, T., Takeda, K., Nishitoh, H., and Ichijo, H. (2009) USP14 inhibits ER-associated degradation via interaction with IRE1α. Biochem. Biophys. Res. Commun. 379, 995-1000
21. Sun, W., Tan, X., Shi, Y., Xu, G., Mao, R., Gu, X., Fan, Y., Yu, Y., Burlingame, S., Zhang, H., Rednam, S. P., Lu, X., Zhang, T., Fu, S., Cao, G., Qin, J., and Yang, J. (2010) USP11 negatively regulates TNFα-induced NF-κB activation by targeting on IκBα. Cell Signal 22, 386-394
22. Reyes-Turcu, F. E., Ventii, K. H., and Wilkinson, K. D. (2009) Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annual review of biochemistry 78, 363-397
23. Lin, Z., Yang, H., Kong, Q., Li, J., Lee, S. M., Gao, B., Dong, H., Wei, J., Song, J., Zhang, D. D., and Fang, D. (2012) USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development. Mol. Cell 46, 484-494
24. Zhang, L., Zhou, F., Drabsch, Y., Gao, R., Snaar-Jagalska, B. E., Mickanin, C., Huang, H., Sheppard, K. A., Porter, J. A., Lu, C. X., and ten Dijke, P. (2012) USP4 is regulated by AKT phosphorylation and directly deubiquitylates TGF-β type I receptor. Nat. Cell Biol. 14, 717-726
25. Rivett, A. J., Bose, S., Brooks, P., and Broadfoot, K. I. (2001) Regulation of proteasome complexes by γ-interferon and phosphorylation. Biochimie 83, 363-366 (Pubitemid 32293658)
26. Djakovic, S. N., Marquez-Lona, E. M., Jakawich, S. K., Wright, R., Chu, C., Sutton, M. A., and Patrick, G. N. (2012) Phosphorylation of Rpt6 regulates synaptic strength in hippocampal neurons. J. Neurosci. 32, 5126-5131