Free and N-linked oligomannosides as markers of the quality control of newly synthesized glycoproteins

被引:18
作者
Cacan, R [1 ]
Verbert, A [1 ]
机构
[1] Univ Sci & Technol Lille, Chim Biol Lab, CNRS, UMR 111, F-59655 Villeneuve Dascq, France
关键词
N-glycosylation; endoplasmic reticulum; cytosol; oligomannoside trafficking; quality control; protein degradation;
D O I
10.1006/bbrc.1999.0549
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
It appears increasingly evident that the oligomannoside type N-glycans play important roles in the fate of newly synthesized glycoproteins in the rough endoplasmic reticulum. The variety of protein-bound oligomannoside isomers are involved in the quality control of glycoprotein, in their transport into the Golgis and probably as a degradation signal. A prerequisite of the degradation in the cytosol by the proteasome pathway is the release of the glycans as free oligomannosides. These oligomannosides are further processed in the cytosol into a peculiar isomer of Man(5)GlcNAc(1) which enters into the lysosome to be further degraded into monosaccharides. In this review, we will illustrate how the different species of N-linked and free oligomannosides either are involved or are markers of the quality control and fate of newly synthesized glycoproteins. (C) 1999 Academic Press.
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页码:1 / 5
页数:5
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共 39 条
  • [1] ANUMULA KR, 1983, J BIOL CHEM, V258, P5274
  • [2] 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, JP
    MONSIGNY, M
    LEGRAND, A
    ROCHE, AC
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (08) : 3551 - 3553
  • [3] EFFECT OF SUBSTRATE STRUCTURE ON THE ACTIVITY OF MAN9-MANNOSIDASE FROM PIG-LIVER INVOLVED IN N-LINKED OLIGOSACCHARIDE PROCESSING
    BAUSE, E
    BREUER, W
    SCHWEDEN, J
    ROESER, R
    GEYER, R
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 208 (02): : 451 - 457
  • [4] Reversal of fortune for nascent proteins
    Bonifacino, JS
    [J]. NATURE, 1996, 384 (6608) : 405 - 406
  • [5] Free oligomannosides produced during the N-glycosylation process: Origin, intracellular trafficking and putative roles
    Cacan, R
    Verbert, A
    [J]. TRENDS IN GLYCOSCIENCE AND GLYCOTECHNOLOGY, 1997, 9 (49) : 365 - 377
  • [6] CACAN R, 1996, BIOCHEM J, V271, P11588
  • [7] Cytosolic deglycosylation process of newly synthesized glycoproteins generates oligomannosides possessing one GlcNAc residue at the reducing end
    Duvet, S
    Labiau, O
    Mir, AM
    Kmiécik, D
    Krag, SS
    Verbert, A
    Cacan, R
    [J]. BIOCHEMICAL JOURNAL, 1998, 335 : 389 - 396
  • [8] Ermonval M, 1997, J CELL SCI, V110, P323
  • [9] Oligomannosides or oligosaccharide-lipids as potential substrates for rat liver cytosolic alpha-D-mannosidase
    Grard, T
    Herman, V
    SaintPol, A
    Kmiecik, D
    Labiau, O
    Mir, AM
    Alonso, C
    Verbert, A
    Cacan, R
    Michalski, JC
    [J]. BIOCHEMICAL JOURNAL, 1996, 316 : 787 - 792
  • [10] ISOLATION OF CHINESE-HAMSTER OVARY CELL-LINES TEMPERATURE CONDITIONAL FOR THE CELL-SURFACE EXPRESSION OF INTEGRAL MEMBRANE-GLYCOPROTEINS
    HEARING, J
    HUNTER, E
    RODGERS, L
    GETHING, MJ
    SAMBROOK, J
    [J]. JOURNAL OF CELL BIOLOGY, 1989, 108 (02) : 339 - 353