Role of ubiquitin in proteasomal degradation of mutant α1-antitrypsin Z in the endoplasmic reticulum

American Journal of Physiology - Gastrointestinal and Liver Physiology

Volumn 278, Issue 1 41-1, 2000, Pages

  Teckman, Jeffrey H ^a,b   Gilmore, Reid ^c   Perlmutter, David H ^a,b  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b ST LOUIS CHILDREN S HOSPITAL   (United States)

^c UNIVERSITY OF MASSACHUSETTS BOSTON   (United States)

Author keywords

Emphysema; Endoplasmic reticulum; Liver disease; Protein degradation; Quality control apparatus; 1 antitrypsin deficiency

Indexed keywords

ALPHA 1 ANTITRYPSIN; PROTEASOME; UBIQUITIN;

ALPHA 1 ANTITRYPSIN DEFICIENCY; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME DEGRADATION; ENZYME MECHANISM; FIBROBLAST; GENE OVEREXPRESSION; NONHUMAN; PRIORITY JOURNAL; RABBIT; REGULATORY MECHANISM;

EID: 0033963160     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.2000.278.1.g39     Document Type: Article

References (42)

1. Bebok, Z., C. Mazzochi, S. A. King, J. S. Hong, and E. J. Sorscher. The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes SEC61-β and a cytosolic, deglycosylated intermediary. J. Biol. Chem. 273: 29873-29878, 1998.
2. Bennett, M. J., J. E. M. Van Leeuwen, and K. P. Kearse. Calnexin association is not sufficient to protect T cell receptor αproteins from rapid degradation in CD4+ CD8+ thymocytes. J. Biol. Chem. 273: 23674-23680, 1998.
3. Bercovich, Z., Y. Rosenberg-Hasson, A. Ciechanover, and C. Kahana. Degradation of ornithine decarboxylase in reticulocyte lysate is ATP-dependent but ubiquitin-independent. J. Biol. Chem. 264: 15949-15952, 1989.
4. Biederer, T., C. Volkwein, and T. Sommer. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15: 2069-2076, 1996.
5. Biederer, T., C. Volkwein, and T. Sommer. Role of the Cue1p in ubiquitination and degradation at the ER surface. Science 278: 1806-1809, 1997.
6. Blumenfeld, N., H. Gonen, A. Mayer, C. E. Smith, N. R. Siegel, A. L. Schwartz, and A. Ciechanover. Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-"N-end rule" protein substrates. J. Biol. Chem. 269: 9574-9581, 1994.
7. Bordallo, J., R. K. Plemper, A. Finger, and D. H. Wolf. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol. Cell. Biol. 9: 209-222, 1998.
8. Chen, Y., F. Le Caherec, and S. L. Chuck. Calnexin and other factors that alter translocation affect the rapid binding of ubiquitin to apoB in the SEC61 complex. J. Biol. Chem. 273: 11887-11894, 1998.
9. De Virgilio, M., H. Weninger, and N. E. Ivessa. Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J. Biol. Chem. 273: 9734-9743, 1998.
10. Finley, D., S. Sadis, B. P. Monia, P. Boucher, D. J. Ecker, S. T. Crooke, and V. Chau. Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Mol. Cell. Biol. 14: 5501-5509, 1994.
11. Haas, A. L., and T. J. Siepmann. Pathways of ubiquitin conjugation. FASEB J. 11: 1257-1268, 1997.
12. Hershko, A., H. Heller, S. Elias, and A. Ciechanover. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 258: 8206-8214, 1983.
13. Hiller, M. M., A. Finger, M. Schweiger, and D. H. Wolf. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273: 1725-1728, 1996.
14. Hughes, E. A., C. Hammond, and P. Cresswell. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc. Natl. Acad. Sci. USA 94: 1896-1901, 1997.
15. Jensen, T. J., M. A. Loo, S. Pind, D. B. Williams, A. L. Goldberg, and J. R. Riordan. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83: 129-135, 1995.
16. Liao, W., S.-C. J. Yeung, and L. Chan. Proteasome-mediated degradation of apolipoprotein B targets both nascent peptides cotranslationally before translocation and full-length apolipoprotein B after translocation into the endoplasmic reticulum. J. Biol. Chem. 273: 27225-27230, 1998.
17. Loayza, D., A. Tam, W. K. Schmidt, and S. Michaelis. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 18: 2767-2784, 1998.
18. 1-Antitrypsin deficiency: from genotype to childhood disease. J. Pediatr. Gastroenterol. Nutr. 27: 65-74, 1998.
19. Mayer, T. U., T. Braun, and S. Jentsch. Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO J. 17: 3251-3257, 1998.
20. Mayer, A., N. R. Siegel, A. L. Schwartz, and A. Ciechanover. Degradation of proteins with acetylated amino termini by the ubiquitin system. Science 244: 1480-1483, 1989.
21. McGee, T., H. Cheng, H. Kumagai, S. Omura, and R. Simoni. Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J. Biol. Chem. 271: 25630-25638, 1996.
22. Murakami, Y., S. Matsufuji, T. Kameji, S.-I. Hayashi, K. Igarashi, T. Tamura, K. Tanaka, and A. Ichihara. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 360: 597-599, 1992.
23. Nuber, U., S. Schwarz, P. Kaiser, R. Schneider, and M. Scheffner. Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. J. Biol. Chem. 271: 2795-2800, 1996.
24. Orian, A., S. Whiteside, A. Israel, I. Stancovski, A. L. Schwartz, and A. Ciechanover. Ubiquitin-mediated processing of NF-κB transcriptional activator precursor p105. Reconstitution of a cell-free system and identification of the ubiquitincarrier protein, E2, and a novel ubiquitin-protein ligase, E3, involved in conjugation. J. Biol. Chem. 270: 21707-21714, 1995.
25. Pilon, M., R. Schekman, and K. Romisch. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16: 4540-4548, 1997.
26. Plemper, R., S. Bohmler, J. Bordallo, T. Sommer, and D. Wolf. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388: 891-895, 1997.
27. 1-antitrypsin Z in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 271: 22791-22795, 1998.
28. Rapiejko, P. J., and R. Gilmore. Protein translocation across the ER requires a functional GTP binding site in the alpha subunit of the signal recognition particle receptor. J. Cell Biol. 117: 493-503, 1992.
29. Sato, S., C. L. Ward, and R. R. Kopito. Cotranslational ubiquitination of a cystic fibrosis transmembrane conductance regulator in vitro. J. Biol. Chem. 273: 7189-7192, 1998.
30. 1-antitrypsin deficiency detected by screening of 200,000 infants. N. Engl. J. Med. 294: 1316-1321, 1976.
31. 1-antitrypsin deficiency. Hepatology 22: 514-517, 1995.
32. 1-antitrypsin Z and S is distinct from that for an unassembled membrane protein. J. Biol. Chem. 271: 13215-13220, 1996.
33. 1-antitrypsin deficiency. Hepatology 24: 1504-1516, 1996.
34. Van Leyen, K., R. Duvoisin, H. Engelhardt, and M. Wiedmann. A function for lipoxygenase in programmed organelle degradation. Nature 395: 392-396, 1998.
35. Walter, P., and G. Blobel. Signal recognition particle: a ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties. Methods Enzymol. 96: 84-93, 1983.
36. Ward, C. L., S. Omura, and R. R. Kopito. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83: 121-127, 1995.
37. Werner, E. D., J. L. Brodsky, and A. A. McCracken. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc. Natl. Acad. Sci. USA 93: 13797-13801, 1996.
38. Wiertz, E. J. H. J., D. Tortorella, M. Bogyo, J. Yu, W. Mothes, and T. R. Jones. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384: 432-438, 1996.
39. 1-antitrypsin deficiency. Proc. Natl. Acad. Sci. USA 91: 9014-9018, 1994.
40. Yang, M., S. Omura, J. S. Bonifacino, and A. M. Weissman. Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J. Exp. Med. 187: 835-846, 1998.
41. Yu, H., G. Kaung, S. Kobayashi, and R. R. Kopito. Cytosolic degradation of T-cell receptor αchains by the proteasome. J. Biol. Chem. 272: 20800-20804, 1997.
42. Zhou, M., E. A. Fisher, and H. N. Ginsberg. Regulated co-translational ubiquitination of apolipoprotein B100. A new paradigm for proteasomal degradation of a secretory protein. J. Biol. Chem. 273: 24649-24653, 1998.