메뉴 건너뛰기




Volumn 1473, Issue 1, 1999, Pages 137-146

Trafficking of oligomannosides released during N-glycosylation: A clearing mechanism of the rough endoplasmic reticulum

Author keywords

Cytosol; Endoplasmic reticulum; Lipid intermediates; N glycosylation; Oligomannoside trafficking

Indexed keywords

MANNOSIDE;

EID: 0032712592     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(99)00174-9     Document Type: Review
Times cited : (20)

References (40)
  • 1
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54:1985;631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 2
    • 0001709752 scopus 로고
    • Glycosyltransferases involved in the synthesis of N-glycan antennae
    • in: J. Montreuil, J.F.G. Vliegenthart, H.Schachter (Eds.), Elsevier, Amsterdam
    • H. Schachter, Glycosyltransferases involved in the synthesis of N-glycan antennae, in: J. Montreuil, J.F.G. Vliegenthart, H.Schachter (Eds.), Glycoproteins, Elsevier, Amsterdam, 1995, pp. 153-.
    • (1995) Glycoproteins , pp. 153
    • Schachter, H.1
  • 3
    • 0031315172 scopus 로고    scopus 로고
    • Free oligomannosides produced during the N-glycosylation process origin, intracellular trafficking and putative roles
    • Cacan R., Verbert A. Free oligomannosides produced during the N-glycosylation process origin, intracellular trafficking and putative roles. TIGG. 9:1997;365-377.
    • (1997) TIGG , vol.9 , pp. 365-377
    • Cacan, R.1    Verbert, A.2
  • 5
    • 0018946112 scopus 로고
    • Fate of oligosaccharide-lipid intermediates synthetised by resting rat-spleen lymphocytes
    • Cacan R., Hoflack B., Verbert A. Fate of oligosaccharide-lipid intermediates synthetised by resting rat-spleen lymphocytes. Eur. J. Biochem. 106:1980;473-479.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 473-479
    • Cacan, R.1    Hoflack, B.2    Verbert, A.3
  • 6
    • 0016254329 scopus 로고
    • The role of a dolichol-oligosaccharide as an intermediate in glycoprotein biosynthesis
    • Hsu A.F., Baynes J.W., Heath E.C. The role of a dolichol-oligosaccharide as an intermediate in glycoprotein biosynthesis. Proc. Natl. Acad. Sci. USA. 71:1974;2391-2395.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 2391-2395
    • Hsu, A.F.1    Baynes, J.W.2    Heath, E.C.3
  • 7
    • 0016685618 scopus 로고
    • The mannosylation of dolichol-diphosphate oligosaccharides in relation to the formation of oligosaccharides and glycoproteins in pig liver endoplasmic reticulum
    • Oliver G.J.A., Harrison J., Hemming F.W. The mannosylation of dolichol-diphosphate oligosaccharides in relation to the formation of oligosaccharides and glycoproteins in pig liver endoplasmic reticulum. Eur. J. Biochem. 58:1975;223-229.
    • (1975) Eur. J. Biochem. , vol.58 , pp. 223-229
    • Oliver, G.J.A.1    Harrison, J.2    Hemming, F.W.3
  • 8
    • 0018186610 scopus 로고
    • Study of nuclear mannosyl-transferase lipids intermediates
    • Richard M., Tytgat F., Louisot P. Study of nuclear mannosyl-transferase lipids intermediates. Biochimie. 60:1978;593-599.
    • (1978) Biochimie , vol.60 , pp. 593-599
    • Richard, M.1    Tytgat, F.2    Louisot, P.3
  • 9
    • 0019154119 scopus 로고
    • Enzymatic activities in cultured human lymphocytes that dephosphorylate dolichol pyrophosphate and dolichol phosphate
    • Wedgwood J.F., Strominger J.L. Enzymatic activities in cultured human lymphocytes that dephosphorylate dolichol pyrophosphate and dolichol phosphate. J. Biol. Chem. 255:1980;1120-1123.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1120-1123
    • Wedgwood, J.F.1    Strominger, J.L.2
  • 10
    • 0023821862 scopus 로고
    • Characterization of an oligosaccharide-pyrophosphodolichol pyrophosphatase in yeast.
    • Bélard M., Cacan R., Verbert A. Characterization of an oligosaccharide-pyrophosphodolichol pyrophosphatase in yeast. Biochem. J. 255:1988;235-242.
    • (1988) Biochem. J. , vol.255 , pp. 235-242
    • Bélard, M.1    Cacan, R.2    Verbert, A.3
  • 11
    • 0019483754 scopus 로고
    • Dolichol pathway in lymphocytes from rat spleen: Influence of the glucosylation on the cleavage of dolichol diphosphate oligosaccharides into phospho-oligosaccharides
    • Hoflack B., Cacan R., Verbert A. Dolichol pathway in lymphocytes from rat spleen: influence of the glucosylation on the cleavage of dolichol diphosphate oligosaccharides into phospho-oligosaccharides. Eur. J. Biochem. 117:1981;285-290.
    • (1981) Eur. J. Biochem. , vol.117 , pp. 285-290
    • Hoflack, B.1    Cacan, R.2    Verbert, A.3
  • 12
    • 0023655478 scopus 로고
    • A Catabolic pathway of oligosaccharide-diphosphodolichol: Study of the fate of the oligosaccharidic moiety in mouse splenocytes
    • Cacan R., Cecchelli R., Verbert A. A Catabolic pathway of oligosaccharide-diphosphodolichol: study of the fate of the oligosaccharidic moiety in mouse splenocytes. Eur. J. Biochem. 166:1987;469-474.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 469-474
    • Cacan, R.1    Cecchelli, R.2    Verbert, A.3
  • 13
    • 0019631138 scopus 로고
    • Transmembrane assembly of membrane and secretory glycoproteins
    • Hanover J.A., Lennarz J. Transmembrane assembly of membrane and secretory glycoproteins. Arch. Biochem. Biophys. 211:1981;1-19.
    • (1981) Arch. Biochem. Biophys. , vol.211 , pp. 1-19
    • Hanover, J.A.1    Lennarz, J.2
  • 14
    • 0020490406 scopus 로고
    • Transmembrane assembly of N-linked glycoproteins
    • Hanover J.A., Lennarz J. Transmembrane assembly of N-linked glycoproteins. J. Biol. Chem. 257:1982;2787-2794.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2787-2794
    • Hanover, J.A.1    Lennarz, J.2
  • 15
    • 0021015788 scopus 로고
    • Release of glucose-containing polymannose oligosaccharides during glycoprotein biosynthesis
    • Anumula K.R., Spiro R.G. Release of glucose-containing polymannose oligosaccharides during glycoprotein biosynthesis. J. Biol. Chem. 258:1983;15274-15282.
    • (1983) J. Biol. Chem. , vol.258 , pp. 15274-15282
    • Anumula, K.R.1    Spiro, R.G.2
  • 16
    • 0025762343 scopus 로고
    • Potential regulation of N-glycosylation precursor through oligosaccharide-lipid hydrolase action and glucosyltransferase-glucosidase shuttle
    • Spiro M.J., Spiro R.G. Potential regulation of N-glycosylation precursor through oligosaccharide-lipid hydrolase action and glucosyltransferase-glucosidase shuttle. J. Biol. Chem. 266:1991;5311-5317.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5311-5317
    • Spiro, M.J.1    Spiro, R.G.2
  • 17
    • 0028084472 scopus 로고
    • Release of oligomannoside-type glycans as a marker of the degradation of newly synthesized glycoprotein
    • Villers C., Cacan R., Mir A.-M., Labiau O., Verbert A. Release of oligomannoside-type glycans as a marker of the degradation of newly synthesized glycoprotein. Biochem. J. 298:1994;135-142.
    • (1994) Biochem. J. , vol.298 , pp. 135-142
    • Villers, C.1    Cacan, R.2    Mir, A.-M.3    Labiau, O.4    Verbert, A.5
  • 19
    • 0030033862 scopus 로고    scopus 로고
    • Occurrence of a cytosolic neutral chitobiase activity involved in oligomannoside degradation: A study with Madin-Darby Bovine Kidney (MDBK) cells
    • Cacan R., Dengremont C., Labiau O., Kmiécik D., Mir A.-M., Verbert A. Occurrence of a cytosolic neutral chitobiase activity involved in oligomannoside degradation: a study with Madin-Darby Bovine Kidney (MDBK) cells. Biochem. J. 313:1996;597-602.
    • (1996) Biochem. J. , vol.313 , pp. 597-602
    • Cacan, R.1    Dengremont, C.2    Labiau, O.3    Kmiécik, D.4    Mir, A.-M.5    Verbert, A.6
  • 20
    • 0032532358 scopus 로고    scopus 로고
    • Cytosolic deglycosylation process of newly synthesized glycoproteins generates oligomannosides possessing one GlcNAc residue at the reducing end
    • Duvet S., Labiau O., Mir A.-M., Kmiecik D., Krag S.S., Verbert A., Cacan R. Cytosolic deglycosylation process of newly synthesized glycoproteins generates oligomannosides possessing one GlcNAc residue at the reducing end. Biochem. J. 335:1998;389-396.
    • (1998) Biochem. J. , vol.335 , pp. 389-396
    • Duvet, S.1    Labiau, O.2    Mir, A.-M.3    Kmiecik, D.4    Krag, S.S.5    Verbert, A.6    Cacan, R.7
  • 21
    • 0028827570 scopus 로고
    • Endoplasmic reticulum to cytosol transport of free polymannose oligosaccharides in permeabilized HepG2 cells
    • Moore S.E.H., Bauvy C., Codogno P. Endoplasmic reticulum to cytosol transport of free polymannose oligosaccharides in permeabilized HepG2 cells. EMBO J. 14:1995;6034-6042.
    • (1995) EMBO J. , vol.14 , pp. 6034-6042
    • Moore, S.E.H.1    Bauvy, C.2    Codogno, P.3
  • 22
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz J., Donaldson J.G., Schweizer A., Berger E.G., Hauri H.P., Yuan L.C., Klausner R.D. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell. 60:1990;821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 23
    • 0025818182 scopus 로고
    • Effects of Brefeldin A on oligosaccharide processing
    • Chawla D., Hughes C.R. Effects of Brefeldin A on oligosaccharide processing. Biochem. J. 279:1991;159-165.
    • (1991) Biochem. J. , vol.279 , pp. 159-165
    • Chawla, D.1    Hughes, C.R.2
  • 25
    • 0021255868 scopus 로고
    • Transmembrane movement of oligosaccharide-lipids during glycoprotein synthesis
    • Snider M.D., Rogers O.C. Transmembrane movement of oligosaccharide-lipids during glycoprotein synthesis. Cell. 36:1984;753-761.
    • (1984) Cell , vol.36 , pp. 753-761
    • Snider, M.D.1    Rogers, O.C.2
  • 26
    • 0024456160 scopus 로고
    • Catabolic pathway of oligosaccharide-diphosphodolichol: Subcellular sites of the degradation of the oligomannoside moiety
    • Cacan R., Lepers A., Bélard M., Verbert A. Catabolic pathway of oligosaccharide-diphosphodolichol: subcellular sites of the degradation of the oligomannoside moiety. Eur. J. Biochem. 185:1989;173-179.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 173-179
    • Cacan, R.1    Lepers, A.2    Bélard, M.3    Verbert, A.4
  • 27
    • 0028335370 scopus 로고
    • Intracellular compartmentalization and degradation of free polymannose oligosaccharides released during glycoprotein biosynthesis
    • Moore S.E.H., Spiro R.G. Intracellular compartmentalization and degradation of free polymannose oligosaccharides released during glycoprotein biosynthesis. J. Biol. Chem. 269:1994;12715-12721.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12715-12721
    • Moore, S.E.H.1    Spiro, R.G.2
  • 28
    • 0031030663 scopus 로고    scopus 로고
    • Transfer of free polymannose type oligosaccharides from the cytosol to lysosomes in cultured human hepatocellular carcinoma HepG2 cells
    • Saint-Pol A., Bauvy C., Codogno P., Moore S.E.H. Transfer of free polymannose type oligosaccharides from the cytosol to lysosomes in cultured human hepatocellular carcinoma HepG2 cells. J. Cell. Biol. 136:1997;45-59.
    • (1997) J. Cell. Biol. , vol.136 , pp. 45-59
    • Saint-Pol, A.1    Bauvy, C.2    Codogno, P.3    Moore, S.E.H.4
  • 29
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz E.J.H.J., Jones T.R., Sun L., Bogyo M., Geuze H.J., Ploegh H.L. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell. 84:1996;769-779.
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 30
    • 0029828991 scopus 로고    scopus 로고
    • Sec 61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz E.J.H.J., Tortorella D., Bogyo M., Yu J., Mothes W., Jones T.R., Rapoport T.A., Ploegh H.L. Sec 61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature. 384:1996;432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.H.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 31
    • 0029852685 scopus 로고    scopus 로고
    • Reversal of fortune for nascent proteins
    • Bonifacino J.S. Reversal of fortune for nascent proteins. Nature. 384:1996;405-406.
    • (1996) Nature , vol.384 , pp. 405-406
    • Bonifacino, J.S.1
  • 32
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C.L., Omura S., Kopito R.R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell. 83:1995;121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 33
    • 0029788023 scopus 로고    scopus 로고
    • 1-antitrypsin Z in the endoplasmic reticulum requires proteasome activity
    • 1-antitrypsin Z in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 271:1996;22791-22795.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22791-22795
    • Qu, D.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 34
    • 0031051852 scopus 로고    scopus 로고
    • Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded into the proteasome
    • Hughes E.A., Hammond C., Cresswell P. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded into the proteasome. Proc. Natl. Acad. Sci. USA. 94:1997;1896-1901.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1896-1901
    • Hughes, E.A.1    Hammond, C.2    Cresswell, P.3
  • 35
    • 0028362217 scopus 로고
    • Purification and enzymatic propreties of petide-N-glycanase from C3H mouse-derived L-929 fibroblast cells, possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation
    • Suzuki T., Seko A., Kitajima K., Inoue Y., Inoue S. Purification and enzymatic propreties of petide-N-glycanase from C3H mouse-derived L-929 fibroblast cells, possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation. J. Biol. Chem. 269:1994;17611-17618.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17611-17618
    • Suzuki, T.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 36
    • 0018791725 scopus 로고
    • Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney
    • Pierce R.J., Spik G., Montreuil J. Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney. Biochem. J. 180:1979;673-676.
    • (1979) Biochem. J. , vol.180 , pp. 673-676
    • Pierce, R.J.1    Spik, G.2    Montreuil, J.3
  • 37
    • 0018841512 scopus 로고
    • Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver
    • Pierce R.J., Spik G., Montreuil J. Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver. Biochem. J. 185:1980;261-264.
    • (1980) Biochem. J. , vol.185 , pp. 261-264
    • Pierce, R.J.1    Spik, G.2    Montreuil, J.3
  • 38
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou W.J., Cameron P.H., Thomas D.Y., Bergeron J.J.M. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature. 364:1993;771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 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
    • Spiro R.G., Zhu Q., Bhoyroo V., Söling H.-D. 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. 271:1996;11588-11594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Söling, H.-D.4
  • 40
    • 0028926420 scopus 로고
    • ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60 an intracellular mannose-specific lectin of myelomonocytic cells
    • Arar C., Carpentier V., LeCaer J.-P., Monsigny M., Roche A.-C. ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60 an intracellular mannose-specific lectin of myelomonocytic cells. J. Biol. Chem. 270:1995;3551-3553.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3551-3553
    • Arar, C.1    Carpentier, V.2    Lecaer, J.-P.3    Monsigny, M.4    Roche, A.-C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.