Intracellular processing of α1-antitrypsin

Proceedings of the American Thoracic Society

Volumn 7, Issue 6, 2010, Pages 376-380

  Sifers, Richard N ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

Autophagy; Biosynthetic quality control; Endoplasmic reticulum; Glycoproteins; Proteolysis

Indexed keywords

ALPHA 1 ANTITRYPSIN;

CHRONIC OBSTRUCTIVE LUNG DISEASE; ENDOPLASMIC RETICULUM; HUMAN; LIVER DISEASE; METABOLISM; REVIEW; SIGNAL TRANSDUCTION;

ALPHA 1-ANTITRYPSIN; ENDOPLASMIC RETICULUM; HUMANS; LIVER DISEASES; PULMONARY DISEASE, CHRONIC OBSTRUCTIVE; SIGNAL TRANSDUCTION;

EID: 79952634721     PISSN: 15463222     EISSN: 19435665     Source Type: Journal    
DOI: 10.1513/pats.201001-011AW     Document Type: Conference Paper

References (52)

1. Molinari M. N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 2007;3:313-320.
2. Balch WE, Morimoto RI, Dillin A, Kelly JW. Adapting proteostasis for disease intervention. Science 2008;319:916-919.
3. Lomas DA, Evans DLI, Finch JT, Carrell RW. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature 1992;357:605-607.
4. Carrell RW, Lomas DA. Alpha1-antitrypsin deficiency-a model for conformational diseases. N Engl J Med 2002;346:45-53.
5. Lomas DA, Mahadeva R. Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy. J Clin Invest 2002;110:1585-1590.
6. Sifers RN. Heritable a1-antitrypsin deficiency. In: Zander DS, Popper HH, Jagirdar J, Haque AK, Cagle PT, Barrios R, editors. Molecular pathology of lung disease. New York, NY: Springer; 1998. pp. 541-548.
7. Perlmutter DH, Pierce JA. The alpha 1-antitrypsin gene and emphysema. Am J Physiol 1989;257:L147-L162.
8. Ellgaard L, Helenius A. ER quality control: towards an understanding at the molecular level. Curr Opin Cell Biol 2001;13:431-437.
9. Sifers RN, Finegold MJ, Woo SLC. Molecular biology and genetics of alpha 1-antitrypsin deficiency. Semin Liver Dis 1992;12:301-310.
10. Fewell SW, Travers KJ, Weissman JS, Brodsky JL. The action of molecular chaperones in the early secretory pathway. Annu Rev Genet 2001;35:149-191.
11. Gething MJ, Sambrook J. Protein folding in the cell. Nature 1992;355:33-45.
12. Plemper RK, Wolf DH. Endoplasmic reticulum degradation: reverse protein transport and its end in the proteasome. Mol Biol Rep 1999; 26:125-130.
13. Sifers RN, Brashears-Macatee S, Kidd VJ, Muensch H, Woo SLC. A frameshift mutation results in a truncated alpha1-antitrypsin that is retained within the rough endoplasmic reticulum. J Biol Chem 1989; 263:7330-7335.
14. Ellgaard L, Molinari M, Helenius A. Setting the standards: quality control in the secretory pathway. Science 1999;286:1882-1888.
15. Cabral CM, Liu Y, Sifers RN. Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem Sci 2001;26:619-624.
16. Cabral CM, Liu Y, Moremen KW, Sifers RN. Organizational diversity among distinct glycoprotein ER-associated degradation programs. Mol Biol Cell 2002;13:2639-2650.
17. Trombetta SE, Ganan S, Parodi AJ. The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum. Glycobiology 1991;1:155-161.
18. Sousa MC, Ferro-Garcia MA, Parodi AJ. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc: glycoprotein glucosyltransferase. Biochemistry 1992;31:97-105.
19. Klausner RD, Sitia R. Protein degradation in the endoplasmic reticulum. Cell 1990;62:611-614.
20. Bonifacino JS, Weissman AM. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu Rev Cell Dev Biol 1998;14:19-57.
21. Bernasconi R, Galli C, Calanca V, Nakajima T, Molinari M. Stringent requirement for HRD1, SEL1, and OS-9/XTP-3-B for disposal of ERAD-LS substrates. J Cell Biol 2010;188:223.
22. Gonzalez DS, Karaveg K, Vandersall-Nairn AS, Lal A, Moremen KW. Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis. J Biol Chem 1999;274:21375-21386.
23. Tremblay LO, Herscovics A. Cloning and expression of a specific human alpha1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. Glycobiology 1999;9:1073-1078.
24. Olivari S, Galli C, Alanen H, Ruddock L, Molinari M. A novel stressinduced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation. J Biol Chem 2005;280:2424-2428.
25. Gonzalez DS, Jordan IK. The alpha-mannosidases: phylogeny and adaptive diversification. Mol Biol Evol 2000;17:292-300.
26. Aebi M, Bernasconi R, Clerc S, Molinari M. N-glycan structures: recognition and processing in the ER. Trends Biochem Sci 2010;35:74.
27. Hosokawa N, Kamiya Y, Kato K. The role of MRH domain-containing lectins in ERAD. Glycobiology 2010;20:651-660.
28. Clerc S, Hirsch C, Oggier DM, Deprez P, Jakob C, Sommer T, Aebi M. Hrtm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. Biochem Biophys Res Commun 2006;349:1278.
29. Wu Y, Swulius MT, Moremen KW, Sifers RN. Elucidation of the molecular logic by which misfolded alpha1-antitrypsin is preferentially selected for intracellular degradation. Proc Natl Acad Sci USA 2003;100:8229-8234.
30. Wu Y, Termine DJ, Swulius MT, Moremen KW, Sifers RN. Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis. J Biol Chem 2007;282:4841-4849.
31. Cali T, Vanoni O, Molinari M. The endoplasmic reticulum crossroads for newly synthesized polypeptide chains. Prog Mol Biol Transl Sci 2008;83:135.
32. Reggiori F, Monastyrska I, Verheije MH, Cali T, Ulasli M, Bianchi S, Bernasconi R, de Haan CA, Molinari M. Coronoviruses hijack the LC3-I-positive EDEMsomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication. Cell Host Microbe 2010;7:500-508.
33. Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007;8:519-529.
34. Travers KJ, Patil CK, Wodicka L, Lockhardt DJ, Weissman JS, Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 2000;101:249-258.
35. Yoshida H, Matsui T, Hosokawa N, Kaufman RJ, Nagata K, Mori K. A time-dependent phase shift in the mammalian unfolded protein response. Dev Cell 2003;4:265-271.
36. Banerjee S, Vishwanath P, Cui J, Kelleher DJ, Gilmore R, Robbins PW, Samuelson J. The evolution of N-glycan-dependent endoplasmic reticulum quality control factors for glycoprotein folding and degradation. Proc Natl Acad Sci USA 2007;104:11676-11681.
37. Hosokawa N, Wada I, Hasegawa K, Yorihuzi T, Tremblay LO, Herscovics A, Nagata K. A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation. EMBO Rep 2001;2:415-422.
38. Mast SW, Diekman K, Davis AW, Karaveg K, Sifers RN, Moremen KW. Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins. Glycobiology 2005;15:421-436.
39. Termine DJ, Moremen KW, Sifers RN. The mammalian UPR boosts glycoprotein ERAD by suppressing the proteolytic down-regulation of ER mannosidase I. J Cell Sci 2009;122:976-984.
40. Rutkowski DT, Kaufman RJ. That which does not kill me makes me stronger: adapting to chronic ER stress. Trends Biochem Sci 2007;32: 469-476.
41. Le A, Ferrell GA, Dishon DS, Le Q-Q, Sifers RN. Soluble aggregates of the human PI Z alpha1-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis. J Biol Chem 1992;267:1072-1080.
42. Qu D, Teckman JH, Omura S, Perlmutter DH. Degradation of a mutant secretory protein, alpha1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J Biol Chem 1996;271:22791-22795.
43. Teckman JH, Perlmutter DH. The endoplasmic reticulum degradation pathway for mutant secretory proteins alpha1-antitrypsin Z and S is distinct from that for an unassembled membrane protein. J Biol Chem 1996;271:13215-13220.
44. YuMH, Lee KN, Kim J. The Z type variation of human alpha 1-antitrypsin causes a protein folding defect. Nat Struct Biol 1995;2:363-367.
45. Lawless MW, Greene CM, Mulgrew A, Taggart CC, O'Neill SJ, McElvaney NG. Activation of endoplasmic reticulum-specific stress responses associated with the conformational disease Z alpha 1-antitrypsin deficiency. J Immunol 2004;172:5722-5726.
46. Hidvegi T, Schmidt BZ, Hale P, Perlmutter DH. Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and-12, NFkappaB, and BAP31 but not the unfolded protein response. J Biol Chem 2005;280:39002-39015.
47. Graham KS, Le A, Sifers RN. Accumulation of the insoluble PiZ variant of human alpha 1-antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP. J Biol Chem 1990;265:20463-20468.
48. Lindblad D, Blomenkamp K, Teckman J. Alpha-1-antitrypsin mutant Z protein content in individual hepatocytes correlates with cell death in a mouse model. Hepatology 2007;46:1228-1235.
49. Teckman JH, Perlmutter DH. Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response. Am J Physiol Gastrointest Liver Physiol 2000;279:G961-G974.
50. Teckman JH, An JK, Blomenkamp K, Schmidt B, Perlmutter DH. Mitochondrial autophagy and injury in the liver in alpha1-antitrypsin deficiency. Am J Physiol Gastrointest Liver Physiol 2004;286:G851-G862.
51. Volpert D, Molleston JP, Perlmutter DH. Alpha1-antitrypsin deficiency-associated liver disease progresses slowly in some children. J Pediatr Gastroenterol Nutr 2000;31:258-263.
52. Pan S, Huang L, McPherson J, Muzny D, Rouhani F, Brantly M, Gibbs R, Sifers RN. Single nucleotide polymorphism-mediated translational suppression of endoplasmic reticulum mannosidase I modifies the onset of end-stage liver disease in alpha1-antitrypsin deficiency. Hepatology 2009;50:275-281.