메뉴 건너뛰기




Volumn 18, Issue 12, 1999, Pages 3282-3292

Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: Identification of a nucleoside diphosphatase in the endoplasmic reticulum

Author keywords

Endoplasmic reticulum; Nucleoside diphosphatase; Reglucosylation; UDP; UMP

Indexed keywords

CELL ENZYME; COCARBOXYLASE; DIVALENT CATION; GLUCOSYLTRANSFERASE; GLYCOPROTEIN; GUANOSINE DIPHOSPHATE; INOSINE DIPHOSPHATE; NUCLEOSIDE DIPHOSPHATASE; URIDINE DIPHOSPHATE; URIDINE PHOSPHATE;

EID: 0033564879     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.12.3282     Document Type: Article
Times cited : (79)

References (44)
  • 1
    • 0026505331 scopus 로고
    • Topography of glycosylation reactions in the endoplasmic reticulum
    • Abeijon, C. and Hirschberg, C.B. (1992) Topography of glycosylation reactions in the endoplasmic reticulum. Trends Biochem. Sci., 17, 32-36.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 32-36
    • Abeijon, C.1    Hirschberg, C.B.2
  • 2
    • 0027327079 scopus 로고
    • Guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae
    • Abeijon, C., Yanagisawa, K., Mandon, E.C., Hausler, A., Moremen, K., Hirschberg, C.B. and Robbins, P.W. (1993) Guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae. J. Cell Biol., 122, 307-323.
    • (1993) J. Cell Biol. , vol.122 , pp. 307-323
    • Abeijon, C.1    Yanagisawa, K.2    Mandon, E.C.3    Hausler, A.4    Moremen, K.5    Hirschberg, C.B.6    Robbins, P.W.7
  • 3
    • 0344595562 scopus 로고
    • The properties of Golgi-associated nucleoside diphosphatase and thiamine pyrophosphatase: 1. Cytochemical analysis
    • Allen, J. (1963a) The properties of Golgi-associated nucleoside diphosphatase and thiamine pyrophosphatase: 1. Cytochemical analysis. J. Histochem. Cytochem., 11, 529-541.
    • (1963) J. Histochem. Cytochem. , vol.11 , pp. 529-541
    • Allen, J.1
  • 4
    • 0344595562 scopus 로고
    • The properties of Golgi-associated nucleoside diphosphatase and thiamine pyrophosphatase: 2. Electrophoretic separation and identification
    • Allen, J. (1963b) The properties of Golgi-associated nucleoside diphosphatase and thiamine pyrophosphatase: 2. Electrophoretic separation and identification. J. Histochem. Cytochem., 11, 542-552.
    • (1963) J. Histochem. Cytochem. , vol.11 , pp. 542-552
    • Allen, J.1
  • 5
    • 0344595561 scopus 로고
    • A cytochemical study of Golgi-associated thiamine pyrophosphatase in the epididymis of the mouse
    • Allen, J. and Slater, J. (1961) A cytochemical study of Golgi-associated thiamine pyrophosphatase in the epididymis of the mouse. J. Histochem. Cytochem., 9, 418-423.
    • (1961) J. Histochem. Cytochem. , vol.9 , pp. 418-423
    • Allen, J.1    Slater, J.2
  • 6
    • 0026527418 scopus 로고
    • S-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin
    • Arber, S., Krause, K.H. and Caroni, P. (1992) s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin. J. Cell Biol., 116, 113-125.
    • (1992) J. Cell Biol. , vol.116 , pp. 113-125
    • Arber, S.1    Krause, K.H.2    Caroni, P.3
  • 7
    • 0030835887 scopus 로고    scopus 로고
    • Mitotic phosphorylation of Rab4 prevents binding to a specific receptor on endosome membranes
    • Ayad, N., Hull, M. and Mellman, I. (1997) Mitotic phosphorylation of Rab4 prevents binding to a specific receptor on endosome membranes. EMBO J., 16, 4497-4507.
    • (1997) EMBO J. , vol.16 , pp. 4497-4507
    • Ayad, N.1    Hull, M.2    Mellman, I.3
  • 8
    • 0028014382 scopus 로고
    • The Golgi guanosine diphosphatase is required for transport of GDP-mannose into the lumen of Saccharomyces cerevisiae Golgi vesicles
    • Berninsone, P., Miret, J.J. and Hirschberg, C.B. (1994) The Golgi guanosine diphosphatase is required for transport of GDP-mannose into the lumen of Saccharomyces cerevisiae Golgi vesicles. J. Biol. Chem., 269, 207-211.
    • (1994) J. Biol. Chem. , vol.269 , pp. 207-211
    • Berninsone, P.1    Miret, J.J.2    Hirschberg, C.B.3
  • 9
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. (1981) Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem., 256, 1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 10
    • 0020356675 scopus 로고
    • Orientation and role of nucleoside diphosphatase and 5′-nucleotidase in Golgi vesicles from rat liver
    • Brandan, E. and Fleischer, B. (1982) Orientation and role of nucleoside diphosphatase and 5′-nucleotidase in Golgi vesicles from rat liver. Biochemistry, 21, 4640-4645.
    • (1982) Biochemistry , vol.21 , pp. 4640-4645
    • Brandan, E.1    Fleischer, B.2
  • 11
    • 0033548479 scopus 로고    scopus 로고
    • Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells
    • Cannon, K. and Helenuis, A. (1999) Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells. J. Biol. Chem., 274, 7537-7544.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7537-7544
    • Cannon, K.1    Helenuis, A.2
  • 12
    • 15644364846 scopus 로고    scopus 로고
    • cDNA cloning and chromosomal mapping of a mouse gene with homology to NTPases
    • Chadwick, B.P., Williamson, J., Sheer, D. and Frischauf, A. (1998) cDNA cloning and chromosomal mapping of a mouse gene with homology to NTPases. Mamm. Genome, 9, 162-164.
    • (1998) Mamm. Genome , vol.9 , pp. 162-164
    • Chadwick, B.P.1    Williamson, J.2    Sheer, D.3    Frischauf, A.4
  • 13
    • 0015077598 scopus 로고
    • Isolation of a Golgi apparatus-rich fraction from rat liver
    • Cheetham, R., Morre, D., Pannek, C. and Friend, D.S. (1971) Isolation of a Golgi apparatus-rich fraction from rat liver. J. Cell Biol., 49, 899-905.
    • (1971) J. Cell Biol. , vol.49 , pp. 899-905
    • Cheetham, R.1    Morre, D.2    Pannek, C.3    Friend, D.S.4
  • 14
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • Chen, P.S., Toribara, T.I. and Warner, H. (1956) Microdetermination of phosphorus. Anal. Chem., 28, 1756-1758.
    • (1956) Anal. Chem. , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.I.2    Warner, H.3
  • 15
    • 0028150802 scopus 로고
    • Purification to homogeneity of UDP-glucose:Glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae
    • 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 from Saccharomyces cerevisiae. J. Biol. Chem., 269, 30701-30706.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30701-30706
    • Fernandez, F.S.1    Trombetta, S.E.2    Hellman, U.3    Parodi, A.J.4
  • 16
    • 0014495094 scopus 로고
    • Cytochemical staining of multivesicular body and Golgi vesicles
    • Friend, D.S. (1969) Cytochemical staining of multivesicular body and Golgi vesicles. J. Cell Biol., 41, 269-279.
    • (1969) J. Cell Biol. , vol.41 , pp. 269-279
    • Friend, D.S.1
  • 17
    • 0029058132 scopus 로고
    • Microsomal triglyceride transfer protein: A protein complex required for the assembly of lipoprotein particles
    • Gordon, D., Wetterau, J. and Gregg, R. (1995) Microsomal triglyceride transfer protein: a protein complex required for the assembly of lipoprotein particles. Trends Cell Biol., 5, 317-321.
    • (1995) Trends Cell Biol. , vol.5 , pp. 317-321
    • Gordon, D.1    Wetterau, J.2    Gregg, R.3
  • 18
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment and Golgi apparatus
    • Hammond, C. and Helenius, A. (1994) Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment and Golgi apparatus. J. Cell Biol., 126, 41-52.
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 19
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming and calnexin in glycoprotein folding and quality control
    • 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. USA, 91, 913-917.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 20
    • 0030034867 scopus 로고    scopus 로고
    • Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)
    • Handa, M. and Guidotti, G. (1996) Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum). Biochem. Biophys. Res. Commun., 218, 916-923.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 916-923
    • Handa, M.1    Guidotti, G.2
  • 21
    • 0023763078 scopus 로고
    • A membrane transporter mediates access of uridine 5′-diphosphoglucuronic acid from the cytosol into the endoplasmic reticulum of rat hepatocytes: Implications for glucuronidation reactions
    • Hauser, S., Ziurys, J. and Gollan, J. (1988) A membrane transporter mediates access of uridine 5′-diphosphoglucuronic acid from the cytosol into the endoplasmic reticulum of rat hepatocytes: implications for glucuronidation reactions. Biochim. Biophys. Acta, 967, 149-157.
    • (1988) Biochim. Biophys. Acta , vol.967 , pp. 149-157
    • Hauser, S.1    Ziurys, J.2    Gollan, J.3
  • 23
    • 0028983813 scopus 로고
    • Improvement of an 'in-gel' digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman, U., Wernstedt, C., Góñez, J. and Heldin, C. (1995) Improvement of an 'in-gel' digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal. Biochem., 224, 451-455.
    • (1995) Anal. Biochem. , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Góñez, J.3    Heldin, C.4
  • 24
    • 0023068345 scopus 로고
    • Topography of glycosylation reactions in the rough endoplasmic reticulum and Golgi apparatus
    • Hirschberg, C.B. and Snider, M.D. (1987) Topography of glycosylation reactions in the rough endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem., 56, 63-87.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 63-87
    • Hirschberg, C.B.1    Snider, M.D.2
  • 25
    • 0030019538 scopus 로고    scopus 로고
    • Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea
    • Hsieh, H.L., Tong, C.G., Thomas, C. and Roux, S.J. (1996) Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea. Plant Mol. Biol., 30, 135-147.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 135-147
    • Hsieh, H.L.1    Tong, C.G.2    Thomas, C.3    Roux, S.J.4
  • 26
    • 0024449727 scopus 로고
    • Application of the fast protein liquid chromatographic system and MonoQ HR5/5 anion exchanger to the separation of nucleotides
    • Kremmer, T., Paulik, E. and Boldizar, M. (1989) Application of the fast protein liquid chromatographic system and MonoQ HR5/5 anion exchanger to the separation of nucleotides. J. Chromatogr., 493, 45-52.
    • (1989) J. Chromatogr. , vol.493 , pp. 45-52
    • Kremmer, T.1    Paulik, E.2    Boldizar, M.3
  • 27
    • 0017707459 scopus 로고
    • The role of nucleoside diphosphatase in a uridine nucleotide cycle associated with lactose synthesis in rat mammary gland Golgi apparatus
    • Kuhn, N. and White, A. (1977) The role of nucleoside diphosphatase in a uridine nucleotide cycle associated with lactose synthesis in rat mammary gland Golgi apparatus. Biochem. J., 168, 423-433.
    • (1977) Biochem. J. , vol.168 , pp. 423-433
    • Kuhn, N.1    White, A.2
  • 28
    • 0015523026 scopus 로고
    • Studies on microsomal nucleoside diphosphatase of rat hepatocytes. Purification, intramembranous localization and turnover
    • Kuriyama, Y. (1972) Studies on microsomal nucleoside diphosphatase of rat hepatocytes. Purification, intramembranous localization and turnover. J. Biol., Chem., 247, 2979-2988.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2979-2988
    • Kuriyama, Y.1
  • 29
    • 0032568833 scopus 로고    scopus 로고
    • Molecular cloning of the chicken oviduct ecto-ATP-diphosphohydrolase
    • Nagy, A.K., Knowles, A.F. and Nagami, G.T. (1998) Molecular cloning of the chicken oviduct ecto-ATP-diphosphohydrolase. J. Biol. Chem., 273, 16043-16049.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16043-16049
    • Nagy, A.K.1    Knowles, A.F.2    Nagami, G.T.3
  • 30
    • 10244232330 scopus 로고
    • Nucleosidediphosphatase activity in the Golgi apparatus and its usefulness for cytological studies
    • Novikoff, A. and Goldfischer, S. (1961) Nucleosidediphosphatase activity in the Golgi apparatus and its usefulness for cytological studies. Proc. Natl Acad. Sci. USA, 47, 802-810.
    • (1961) Proc. Natl Acad. Sci. USA , vol.47 , pp. 802-810
    • Novikoff, A.1    Goldfischer, S.2
  • 31
    • 0019082015 scopus 로고
    • Purification and characterization of nucleoside diphosphatase from rat-liver microsomes. Evidence for metalloenzyme and glycoprotein
    • Ohkubo, I., Ishibashi, T., Taniguchi, N. and Makita, A. (1980) Purification and characterization of nucleoside diphosphatase from rat-liver microsomes. Evidence for metalloenzyme and glycoprotein. Eur. J. Biochem., 112, 111-118.
    • (1980) Eur. J. Biochem. , vol.112 , pp. 111-118
    • Ohkubo, I.1    Ishibashi, T.2    Taniguchi, N.3    Makita, A.4
  • 32
    • 0020957538 scopus 로고
    • Transient glucosylation of protein bound Man9GlcNac2, Man8GlcNac2 and Man7GlcNac2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins
    • Parodi, A.J., Mendelzon, D.H. and Lederkremer, G.H. (1983) Transient glucosylation of protein bound Man9GlcNac2, Man8GlcNac2 and Man7GlcNac2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins. J. Biol. Chem., 258, 8260-8265.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8260-8265
    • Parodi, A.J.1    Mendelzon, D.H.2    Lederkremer, G.H.3
  • 33
    • 0022854037 scopus 로고
    • Topography of glycosylation reactions in the rough endoplasmic reticulum membrane
    • Pérez, M. and Hirschberg, C.B. (1986) Topography of glycosylation reactions in the rough endoplasmic reticulum membrane. J. Biol. Chem., 261, 6822-6830.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6822-6830
    • Pérez, M.1    Hirschberg, C.B.2
  • 34
    • 0023303619 scopus 로고
    • Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllyla, R., Huhtala, M.L., Koivu, J. and Kivirikko, K.I. (1987) Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J., 6, 643-649.
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllyla, R.4    Huhtala, M.L.5    Koivu, J.6    Kivirikko, K.I.7
  • 35
    • 0022252944 scopus 로고
    • Purification and characterization of a guanosine diphosphatase activity from calf liver microsomal salt wash proteins
    • RayChaudhuri, P., Ghosh, S. and Maitra, U. (1985) Purification and characterization of a guanosine diphosphatase activity from calf liver microsomal salt wash proteins. J. Biol. Chem., 260, 8306-8311.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8306-8311
    • RayChaudhuri, P.1    Ghosh, S.2    Maitra, U.3
  • 36
    • 0023931086 scopus 로고
    • Thiamine pyrophosphatase (nucleoside diphosphatase) in the Golgi apparatus is distinct from microsomal nucleoside diphosphatase
    • Sano, S., Matsda, Y. and Nakagawa, H. (1988) Thiamine pyrophosphatase (nucleoside diphosphatase) in the Golgi apparatus is distinct from microsomal nucleoside diphosphatase. J. Biochem., 103, 678-681.
    • (1988) J. Biochem. , vol.103 , pp. 678-681
    • Sano, S.1    Matsda, Y.2    Nakagawa, H.3
  • 37
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
    • Sousa, M.C., Ferrero, G.M. and Parodi, A.J. (1992) Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry, 31, 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero, G.M.2    Parodi, A.J.3
  • 38
    • 0029910144 scopus 로고    scopus 로고
    • Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals and a tightly bound non-catalytic HDEL-containing subunit
    • 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 non-catalytic HDEL-containing subunit. J. Biol. Chem., 271, 27509-27516.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27509-27516
    • Trombetta, E.S.1    Simons, J.F.2    Helenius, A.3
  • 39
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:Glycoprotein glucosyltransferase
    • Trombetta, S.E. and Parodi, A.J. (1992) Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose: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
  • 40
    • 0026101730 scopus 로고
    • The UDP-Glc:Glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum
    • Trombetta, S.E., Ganan, S.A. and Parodi, A.J. (1991) The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum. Glycobiology, 1, 155-161.
    • (1991) Glycobiology , vol.1 , pp. 155-161
    • Trombetta, S.E.1    Ganan, S.A.2    Parodi, A.J.3
  • 41
    • 0031041169 scopus 로고    scopus 로고
    • Reglucosylation of N-linked glycans is critical for calnexin assembly with T cell receptor (TCR) α proteins but not TCRβ proteins
    • Van Leeuwen, J.E. and Kearse, K.P. (1997) Reglucosylation of N-linked glycans is critical for calnexin assembly with T cell receptor (TCR) α proteins but not TCRβ proteins. J. Biol. Chem., 272, 4179-4186.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4179-4186
    • Van Leeuwen, J.E.1    Kearse, K.P.2
  • 42
    • 0023695419 scopus 로고
    • Carrier-mediated translocation of uridine diphosphate glucose into the lumen of endoplasmic reticulum-derived vesicles from rat liver
    • Vanstapel, F. and Blanckaert, N. (1988) Carrier-mediated translocation of uridine diphosphate glucose into the lumen of endoplasmic reticulum-derived vesicles from rat liver. J. Clin. Invest., 82, 1113-1122.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1113-1122
    • Vanstapel, F.1    Blanckaert, N.2
  • 43
    • 0030815129 scopus 로고    scopus 로고
    • Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin
    • Wada, I., Kai, M., Imai, S., Sakane, F. and Kanoh, H. (1997) Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin. EMBO J., 16, 5420-5432.
    • (1997) EMBO J. , vol.16 , pp. 5420-5432
    • Wada, I.1    Kai, M.2    Imai, S.3    Sakane, F.4    Kanoh, H.5
  • 44
    • 0032079546 scopus 로고    scopus 로고
    • Golgi localization and functional expression of human uridine diphosphatase
    • Wang, T. and Guidotti, G. (1998) Golgi localization and functional expression of human uridine diphosphatase. J. Biol. Chem., 273, 11392-11399.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11392-11399
    • Wang, T.1    Guidotti, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.