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Volumn 22, Issue 11, 2011, Pages 1810-1823

Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GLUCOSIDASE AB; ALPHA MANNOSIDASE; CALNEXIN; CALRETICULIN; GLUCOSIDASE II ALPHA; GLUCOSIDASE IIBETA; GLYCAN; GLYCAN DERIVATIVE; GLYCOPROTEIN; MANNOSE; N GLYCAN MANNOSE; UNCLASSIFIED DRUG;

EID: 79957596037     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E11-01-0019     Document Type: Article
Times cited : (42)

References (48)
  • 2
    • 0034008736 scopus 로고    scopus 로고
    • Two distinct domains of the β-subunit of glucosidase II interact with the catalytic α-subunit
    • Arendt CW, Ostergaard HL (2000). Two distinct domains of the β subunit of glucosidase II interact with the catalytic α-subunit. Glycobiology 10, 487-492. (Pubitemid 30216090)
    • (2000) Glycobiology , vol.10 , Issue.5 , pp. 487-492
    • Arendt, C.W.1    Ostergaard, H.L.2
  • 3
    • 0031818471 scopus 로고    scopus 로고
    • Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe
    • DOI 10.1002/(SICI)1097-0061(199807)14:10<943::AID-YEA292>3.0.CO;2-Y
    • Bähler J, Wu JQ, Longtine MS, Shah NG, McKenzie A 3rd, Steever AB, Wach A, Philippsen P, Pringle JR (1998). Heterologous modules for ef- ficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe. Yeast 14, 943-951. (Pubitemid 28328000)
    • (1998) Yeast , vol.14 , Issue.10 , pp. 943-951
    • Bahler, J.1    Wu, J.-Q.2    Longtine, M.S.3    Shah, N.G.4    McKenzie III, A.5    Steever, A.B.6    Wach, A.7    Philippsen, P.8    Pringle, J.R.9
  • 4
    • 0035478934 scopus 로고    scopus 로고
    • Dissecting glycoprotein quality control in the secretory pathway
    • DOI 10.1016/S0968-0004(01)01942-9, PII S0968000401019429
    • Cabral CM, Liu Y, Sifers RN (2001). Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem Sci 26, 619-624. (Pubitemid 32925192)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.10 , pp. 619-624
    • Cabral, C.M.1    Liu, Y.2    Sifers, R.N.3
  • 5
    • 36249022072 scopus 로고    scopus 로고
    • How sugars convey information on protein conformation in the endoplasmic reticulum
    • Caramelo JJ, Parodi AJ (2007). How sugars convey information on protein conformation in the endoplasmic reticulum. Sem Cell Dev Biol 18, 10221-10225.
    • (2007) Sem Cell Dev Biol , vol.18 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 6
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out of calnexin and calreticulin cycles
    • Caramelo JJ, Parodi AJ (2008). Getting in and out of calnexin and calreticulin cycles. J Biol Chem 283, 10221-10225.
    • (2008) J Biol Chem , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 7
    • 77952583769 scopus 로고    scopus 로고
    • UDP-Glc:glycoprotein glucosyltransferase- glucosidase II, the ying-yang of the ER quality control
    • D'Alessio C, Caramelo JJ, Parodi AJ (2010). UDP-Glc:glycoprotein glucosyltransferase- glucosidase II, the ying-yang of the ER quality control. Semin Cell Dev Biol 21, 491-499.
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 491-499
    • D'Alessio, C.1    Caramelo, J.J.2    Parodi, A.J.3
  • 8
    • 0038187312 scopus 로고    scopus 로고
    • Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding
    • D'Alessio C, Fernández F, Trombetta ES, Parodi AJ (1999). Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding. J Biol Chem 274, 25899-25905.
    • (1999) J Biol Chem , vol.274 , pp. 25899-25905
    • D'Alessio, C.1    Fernández, F.2    Trombetta, E.S.3    Parodi, A.J.4
  • 9
    • 0037928841 scopus 로고    scopus 로고
    • Nucleoside diphosphatase and glycosyltransferase activities can localize to different subcellular compartments in Schizosaccharomyces pombe
    • DOI 10.1074/jbc.M300892200
    • D'Alessio C, Trombetta ES, Parodi AJ (2003). Nucleoside diphosphatase and glycosyltransferase activities can localize to different subcellular compartments in Schizosaccharomyces pombe. J Biol Chem 278, 22379-22387. (Pubitemid 36830288)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.25 , pp. 22379-22387
    • D'Alessio, C.1    Trombetta, E.S.2    Parodi, A.J.3
  • 10
    • 0023655783 scopus 로고
    • Synthesis of dolichol derivatives in trypanosomatids. Characterization of enzymatic patterns
    • De la Canal L, Parodi AJ (1987). Synthesis of dolichol derivatives in trypanosomatids. Characterization of enzymatic patterns. J Biol Chem 262, 11128-11133.
    • (1987) J Biol Chem , vol.262 , pp. 11128-11133
    • De La Canal, L.1    Parodi, A.J.2
  • 11
    • 0032476580 scopus 로고    scopus 로고
    • The UDP-Glc: Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress
    • Fanchiotti S, Fernández F, D'Alessio C, Parodi AJ (1998). The UDP-Glc: glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress. J Cell Biol 143, 625-635.
    • (1998) J Cell Biol , vol.143 , pp. 625-635
    • Fanchiotti, S.1    Fernández, F.2    D'Alessio, C.3    Parodi, A.J.4
  • 12
    • 0032531734 scopus 로고    scopus 로고
    • A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase
    • Fernández F, D'Alessio C, Fanchiotti S, Parodi AJ (1998). A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J 17, 5877-5886.
    • (1998) EMBO J , vol.17 , pp. 5877-5886
    • Fernández, F.1    D'Alessio, C.2    Fanchiotti, S.3    Parodi, A.J.4
  • 13
    • 0028150802 scopus 로고
    • Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae
    • Fernández FS, Trombetta SE, Hellman U, Parodi AJ (1994). Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae. J Biol Chem 269, 30701-30706. (Pubitemid 24376560)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.48 , pp. 30701-30706
    • Fernandez, F.S.1    Trombetta, S.E.2    Hellman, U.3    Parodi, A.J.4
  • 15
    • 0019332339 scopus 로고
    • Substrate specificities of rat liver microsomal glucosidases which process glycoproteins
    • Grinna LS, Robbins PW (1980). Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J Biol Chem 255, 2255-2258.
    • (1980) J Biol Chem , vol.255 , pp. 2255-2258
    • Grinna, L.S.1    Robbins, P.W.2
  • 16
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases automomous plasmids for transformation of Escherichia coli
    • DOI 10.1016/0378-1119(87)90131-4
    • Hoffman CS, Winston F (1987). A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57, 267-272. (Pubitemid 18007116)
    • (1987) Gene , vol.57 , Issue.2-3 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 17
    • 67650535999 scopus 로고    scopus 로고
    • Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
    • Hosokawa N, Kamiya Y, Kamiya D, Kato K, Nagata K (2009). Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J Biol Chem 284, 17061-17068.
    • (2009) J Biol Chem , vol.284 , pp. 17061-17068
    • Hosokawa, N.1    Kamiya, Y.2    Kamiya, D.3    Kato, K.4    Nagata, K.5
  • 19
    • 0033619113 scopus 로고    scopus 로고
    • High-efficiency gene targeting in Schizosaccharomyces pombe using a modular, PCR-based approach with long tracts of flanking homology
    • Krawchuk MD, Wahls WP (1999). High-efficiency gene targeting in Schizosaccharomyces pombe using a modular, PCR-based approach with long tracts of flanking homology. Yeast 15, 1419-1427.
    • (1999) Yeast , vol.15 , pp. 1419-1427
    • Krawchuk, M.D.1    Wahls, W.P.2
  • 20
    • 0029085605 scopus 로고
    • Retention of the glucose unit added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum
    • Labriola CA, Cazzulo JJ, Parodi AJ (1995). Retention of the glucose unit added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum. J Cell Biol 130, 771-779.
    • (1995) J Cell Biol , vol.130 , pp. 771-779
    • Labriola, C.A.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 21
    • 33746112995 scopus 로고    scopus 로고
    • ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe
    • Erratum in: Nat Biotechnol, 24, 1033
    • Matsuyama A et al. (2006). ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe. Nat Biotechnol 24, 841-847. Erratum in: Nat Biotechnol, 24, 1033.
    • (2006) Nat Biotechnol , vol.24 , pp. 841-847
    • Matsuyama, A.1
  • 22
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno S, Klar A, Nurse P (1991). Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol 194, 795-823.
    • (1991) Methods Enzymol , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 23
    • 26244466799 scopus 로고    scopus 로고
    • Characterization of Schizosaccharomyces pombe ER α-mannosidase. A re-evaluation of the role of the enzyme on ER-associated degradation
    • Movsichoff F, Castro OA, Parodi AJ (2005). Characterization of Schizosaccharomyces pombe ER α-mannosidase. A re-evaluation of the role of the enzyme on ER-associated degradation. Mol Biol Cell 16, 4714-4724.
    • (2005) Mol Biol Cell , vol.16 , pp. 4714-4724
    • Movsichoff, F.1    Castro, O.A.2    Parodi, A.J.3
  • 24
    • 0035838410 scopus 로고    scopus 로고
    • The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins
    • Munro S (2001). The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins. Curr Biol 11, 499-501.
    • (2001) Curr Biol , vol.11 , pp. 499-501
    • Munro, S.1
  • 25
    • 0027282621 scopus 로고
    • N-glycosylation in trypanosomatid protozoa
    • Parodi AJ (1993). N-glycosylation in trypanosomatid protozoa. Glycobiology 3, 193-199.
    • (1993) Glycobiology , vol.3 , pp. 193-199
    • Parodi, A.J.1
  • 26
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi AJ (2000). Protein glucosylation and its role in protein folding. Annu Rev Biochem 69, 69-95.
    • (2000) Annu Rev Biochem , vol.69 , pp. 69-95
    • Parodi, A.J.1
  • 30
  • 34
    • 21644445829 scopus 로고    scopus 로고
    • New drug-resistant cassettes for gene disruption and epitope tagging in Schizosaccharomyces pombe
    • DOI 10.1002/yea.1233
    • Sato M, Dhut S, Toda T (2005). New drug-resistant cassettes for gene disruption and epitope tagging in Schizosaccharomyces pombe. Yeast 22, 583-591. (Pubitemid 40932159)
    • (2005) Yeast , vol.22 , Issue.7 , pp. 583-591
    • Sato, M.1    Dhut, S.2    Toda, T.3
  • 35
    • 78650250452 scopus 로고    scopus 로고
    • Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation
    • Satoh T, Chen Y, Hu D, Hanashima S, Yamamoto K, Yamaguchi Y (2010). Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation. Mol Cell 22, 905-916.
    • (2010) Mol Cell , vol.22 , pp. 905-916
    • Satoh, T.1    Chen, Y.2    Hu, D.3    Hanashima, S.4    Yamamoto, K.5    Yamaguchi, Y.6
  • 36
    • 0022474909 scopus 로고
    • Characterization of calf liver glucosidase I and its inhibition by basic sugar analogs
    • Schweden J, Borgmann C, Legler G, Bause E (1986). Characterization of calf liver glucosidase I and its inhibition by basic sugar analogs. Arch Biochem Biophys 248, 335-340. (Pubitemid 16045610)
    • (1986) Archives of Biochemistry and Biophysics , vol.248 , Issue.1 , pp. 335-340
    • Schweden, J.1    Borgmann, C.2    Legler, G.3    Bause, E.4
  • 37
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDPGlc: Glycoprotein glucosyltransferase
    • Sousa M, Ferrero-García MA, Parodi AJ (1992). Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDPGlc: glycoprotein glucosyltransferase. Biochemistry 31, 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.1    Ferrero-García, M.A.2    Parodi, A.J.3
  • 39
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • DOI 10.1074/jbc.271.19.11588
    • Spiro RG, Zhu Q, Bhoyroo V, 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. (Pubitemid 26156006)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.19 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Soling, H.-D.4
  • 41
    • 33845969527 scopus 로고    scopus 로고
    • Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans
    • DOI 10.1074/jbc.M605457200
    • Totani K, Ihara Y, Matsuo I, Ito Y (2006). Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans. J Biol Chem 281, 31502-31508. (Pubitemid 46041415)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31502-31508
    • Totani, K.1    Ihara, Y.2    Matsuo, I.3    Ito, Y.4
  • 42
    • 39049105287 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on glycoprotein processing enzymes
    • DOI 10.1021/ja077570k
    • Totani K, Ihara Y, Matsuo I, Ito Y (2008). Effects of macromolecular crowding on glycoprotein processing enzymes. J Am Chem Soc 130, 2101-2107. (Pubitemid 351238661)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.6 , pp. 2101-2107
    • Totani, K.1    Ihara, Y.2    Matsuo, I.3    Ito, Y.4
  • 43
    • 0024468302 scopus 로고
    • Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes
    • Trombetta ES, Bosch M, Parodi AJ (1989). Glucosylation of glycoproteins by mammalian, plant, fungal and trypanosomatid protozoa microsomal membranes. Biochemistry 28, 8108-8116. (Pubitemid 19252890)
    • (1989) Biochemistry , vol.28 , Issue.20 , pp. 8108-8116
    • Trombetta, S.E.1    Bosch, M.2    Parodi, A.J.3
  • 44
    • 0029910144 scopus 로고    scopus 로고
    • Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL- Containing subunit
    • DOI 10.1074/jbc.271.44.27509
    • Trombetta ES, Simons JF, 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. (Pubitemid 26367313)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.44 , pp. 27509-27516
    • Trombetta, E.S.1    Simons, J.F.2    Helenius, A.3
  • 45
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-Glc:glycoprotein glucosyltransferase
    • Trombetta SE, Parodi AJ (1992). Purification to apparent homogeneity and partial characterization of rat liver UDP-Glc:glycoprotein glucosyltransferase. J Biol Chem 267, 9236-9240.
    • (1992) J Biol Chem , vol.267 , pp. 9236-9240
    • Trombetta, S.E.1    Parodi, A.J.2
  • 46
    • 33646591932 scopus 로고    scopus 로고
    • Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum
    • DOI 10.1074/jbc.M510455200
    • Wilkinson BM, Purswani J, Stirling CJ (2006). Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum. J Biol Chem 281, 6325-6333. (Pubitemid 43847564)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6325-6333
    • Wilkinson, B.M.1    Purswani, J.2    Stirling, C.J.3
  • 47
    • 0008443072 scopus 로고
    • Tetrahymena pyriformis cells are deficient in all mannose-P-dolichol- dependent mannosyltransferases but not in mannose-P-dolichol synthesis
    • Yagodnik C, de la Canal L, Parodi AJ (1987). Tetrahymena pyriformis cells are deficient in all mannose-P-dolichol-dependent mannosyltransferases but not in mannose-P-dolichol synthesis. Biochemistry 26, 5937-5943.
    • (1987) Biochemistry , vol.26 , pp. 5937-5943
    • Yagodnik, C.1    De La Canal, L.2    Parodi, A.J.3
  • 48
    • 0032126962 scopus 로고    scopus 로고
    • Purification to homogeneity and properties of plant glucosidase i
    • DOI 10.1006/abbi.1998.0717
    • Zeng Y-C, Elbein AD (1998). Purification to homogeneity and properties of plant glucosidase I. Arch Biochem Biophys 355, 26-34. (Pubitemid 28371148)
    • (1998) Archives of Biochemistry and Biophysics , vol.355 , Issue.1 , pp. 26-34
    • Zeng, Y.-C.1    Elbein, A.D.2


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