Endoplasmic reticulum glucosidase II is inhibited by its end products

Biochemistry

Volumn 47, Issue 41, 2008, Pages 10970-10980

  Bosis, Eran ^a   Nachliel, Esther ^a   Cohen, Tamar ^a   Takeda, Yoichi ^b   Ito, Yukishige ^b   Bar Nun, Shoshana ^a   Gutman, Menachem ^a  

^a TEL AVIV UNIVERSITY   (Israel)

^b INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CUSTOMER SATISFACTION; ELECTRIC RESISTANCE; GLYCOPROTEINS; PROTEINS; QUALITY ASSURANCE; QUALITY FUNCTION DEPLOYMENT; TOTAL QUALITY MANAGEMENT;

CALRETICULIN; END PRODUCTS; ENDOPLASMIC RETICULUM; GLUCOSIDASE; QUALITY CONTROL SYSTEMS;

CONTROL SYSTEMS;

ALPHA GLUCOSIDASE AB; CALNEXIN; CALRETICULIN; GLUCOSIDASE; GLYCAN DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; ENDOPLASMIC RETICULUM; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME MECHANISM; PRIORITY JOURNAL; SIMULATION;

ALGORITHMS; ALPHA-GLUCOSIDASES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ENDOPLASMIC RETICULUM; GLYCOSYLATION; HYDROLYSIS; KINETICS;

EID: 53749094428     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801545d     Document Type: Article

References (47)

1. Osborne, A. R., Rapoport, T. A., and van den Berg, B. (2005) Protein translocation by the Sec61/SecY channel. Annu. Rev. Cell Dev. Biol. 21, 529-550.
2. Ellgaard, L., and Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4, 181-191.
3. 2) substrate. J. Biol. Chem. 275, 24348-24356.
4. Totani, K., Ihara, Y., Matsuo, I., Koshino, H., and Ito, Y. (2005) Synthetic substrates for an endoplasmic reticulum protein-folding sensor, UDP-glucose:glycoprotein glucosyltransferase. Angew. Chem., Int. Ed. Engl. 44, 7950-7954.
5. Kapoor, M., Srinivas, H., Kandiah, E., Gemma, E., Ellgaard, L., Oscarson, S., Helenius, A., and Surolia, A. (2003) Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone. J. Biol. Chem. 278, 6194-6200.
6. Williams, D. B. (2006) Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J. Cell Sci. 119, 615-623.
7. Parodi, A. J. (2000) Protein glucosylation and its role in protein folding. Annu. Rev. Biochem. 69, 69-93.
8. Helenius, A. (1994) How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5, 253-265.
9. Grinna, L. S., and Robbins, P. W. (1980) Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 255, 2255-2258.
10. Sousa, M. C., Fenero-Garcia, M. A., and Parodi, A. J. (1992) Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 31, 97-105.
11. Helenius, A., and Aebi, M. (2001) Intracellular functions of N-linked glycans. Science 291, 2364-2369.
12. Moremen, K. W., and Molinari, M. (2006) N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality control. Curr. Opin. Struct. Biol. 16, 592-599.
13. Lederkremer, G. Z., and Glickman, M. H. (2005) A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins. Trends Biochem. Sci. 30, 297-303.
14. Cabrai, C. M., Liu, Y., and Sifers, R. N. (2001) Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem. Sci. 26, 619-624.
15. Totani, K., Ihara, Y., Matsuo, I., and Ito, Y. (2006) Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans. J. Biol. Chem. 281, 31502-31508.
16. Moscovitch, D., Noivirt, O., Mezer, A., Nachliel, E., Mark, T., Gutman, M., and Fibich, G. (2004) Determination of a unique solution to parallel proton transfer reactions using the genetic algorithm. Biophys. J. 87, 47-57.
17. Trombetta, E. S., Simons, J. F., and Helenius, A. (1996) Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem. 271, 27509-27516.
18. Penny, J. E. T., and Lindfield, G. R. (1995) Numerical methods using MATLAB, Ellis Horwood, New York.
19. Gutman, M., and Nachliel, E. (1997) Time-resolved dynamics of proton transfer in proteinous systems. Annu. Rev. Phys. Chem. 48, 329-356.
20. Alonso, J. M., Santa-Cecilia, A., and Calvo, P. (1991) Glucosidase II from rat liver microsomes. Kinetic model for binding and hydrolysis. Biochem. J. 278 (Part 3), 721-727.
21. Alonso, J. M., Santa-Cecilia, A., and Calvo, P. (1993) Effect of bromoconduritol on glucosidase II from rat liver. A new kinetic model for the binding and hydrolysis of the substrate. Eur. J. Biochem. 215, 37-42.
22. Pelletier, M. F., Marcil, A., Sevigny, G., Jakob, C. A., Tessier, D. C., Chevet, E., Menard, R., Bergeron, J. J., and Thomas, D. Y. (2000) The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology 10, 815-827.
23. Ito, Y., Hagihara, S., Matsuo, I., and Totani, K. (2005) Structural approaches to the study of oligosaccharides in glycoprotein quality control. Curr. Opin. Struct. Biol. 15, 481-489.
24. Spiro, R. G., Zhu, Q., Bhoyroo, V., and Soling, H. D. (1996) Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol. Chem. 271, 11588-11594.
25. Houck, C., Joines, J., and Kay, M. A. (1995) A Genetic Algorithm for Function Optimization: A Matlab Implementation. NCSU-1E TR 95-09.
26. Mezer, A., Ashery, U., Gutman, M., Project, E., Bosis, E., Fibich, G., and Nachliel, E. (2006) Systematic search for the rate constants that control the exocytotic process from chromaffin cells by a genetic algorithm. Biochim. Biophys. Acta 1763, 345-355.
27. Hammond, C., Braakman, I., and Helenius, A. (1994) Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. U.S.A. 91, 913-917.
28. Schrag, J. D., Procopio, D. O., Cygler, M., Thomas, D. Y., and Bergeron, J. J. (2003) Lectin control of protein folding and sorting in the secretory pathway. Trends Biochem. Sci. 28, 49-57.
29. Zapun, A., Petrescu, S. M., Rudd, P. M., Dwek, R. A., Thomas, D. Y., and Bergeron, J. J. (1997) Conformation-independent binding of monoglucosylated ribonuclease B to calnexin. Cell 88, 29-38.
30. Petrescu, A. J., Butters, T. D., Reinkensmeier, G., Petrescu, S., Platt, F. M., Dwek, R. A., and Wormald, M. R. (1997) The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding. EMBO J. 16, 4302-4310.
31. Kornfeld, S., Li, E., and Tabas, I. (1978) The synthesis of complex-type oligosaccharides. II. Characterization of the processing intermediates in the synthesis of the complex oligosaccharide units of the vesicular stomatitis virus G protein. J. Biol. Chem. 253, 7771-7778.
32. 2 species in the MI8-5 CHO cell line. Eur. J. Biochem. 271, 398-404.
33. 2. J. Biol. Chem. 278, 34119-34124.
34. Hosokawa, N., Tremblay, L. O., You, Z., Herscovics, A., Wada, I., and Nagata, K. (2003) Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I. J. Biol. Chem. 278, 26287-26294.
35. Kitzmuller, C., Caprini, A., Moore, S. E., Frenoy, J. P., Schwaiger, E., Kellermann, O., Ivessa, N. E., and Ermonval, M. (2003) Processing of N-linked glycans during endoplasmic-reticulum-associated degradation of a short-lived variant of ribophorin I. Biochem. J. 376, 687-696.
36. Ermonval, M., Kitzmuller, C., Mir, A. M., Cacan, R., and Ivessa, N. E. (2001) N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation. Glycobiology 11, 565-576.
37. Olivari, S., Cali, T., Salo, K. E., Paganetti, P., Ruddock, L. W., and Molinari, M. (2006) EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation. Biochem. Biophys. Res. Commun. 349, 1278-1284.
38. Molinari, M. (2007) N-glycan structure dictates extension of protein folding or onset of disposal. Nat. Chem. Biol. 3, 313-320.
39. Schrag, J. D., Bergeron, J. J., Li, Y., Borisova, S., Hahn, M., Thomas, D. Y., and Cygler, M. (2001) The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8, 633-644.
40. Solda, T., Galli, C., Kaufman, R. J., and Molinari, M. (2007) Substrate-specific requirements for UGT1-dependent release from calnexin. Mol. Cell 27, 238-249.
41. Molinari, M., Galli, C., Vanoni, O., Arnold, S. M., and Kaufman, R. J. (2005) Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Mol. Cell 20, 503-512.
42. Fernandez, F. S., Trombetta, S. E., Hellman, U., and Parodi, A. J. (1994) Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme for Saccharomyces cerevisiae. J. Biol. Chem. 269, 30701-30706.
43. Vanoni, O., Paganetti, P., and Molinari, M. (2008) Consequences of individual N-glycan deletions and of proteasomal inhibition on secretion of active BACE. Mol. Biol. Cell (in press).
44. Totani, K., Ihara, Y., Matsuo, I., and Ito, Y. (2008) Effects of macromolecular crowding on glycoprotein processing enzymes. J. Am. Chem. Soc. 130, 2101-2107.
45. Bischoff, J., Liscum, L., and Kornfeld, R. (1986) The use of 1-deoxymannojirimycin to evaluate the role of various alpha-mannosidases in oligosaccharide processing in intact cells. J. Biol. Chem. 261, 4766-4774.
46. Caramelo, J. J., and Parodi, A. J. (2008) Getting in and out from calnexin/calreticulin cycles. J. Biol. Chem. 283, 10221-10225.
47. Weng, S., and Spiro, R. G. (1993) Demonstration that a kifunensine-resistant alpha-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells. J. Biol. Chem. 268, 25656-25663.