Intracellular functions of N-linked glycans

被引:1944
作者
Helenius, A
Aebi, M
机构
[1] Swiss Fed Inst Technol, Inst Biochem, CH-8092 Zurich, Switzerland
[2] Swiss Fed Inst Technol, Inst Microbiol, CH-8092 Zurich, Switzerland
关键词
D O I
10.1126/science.291.5512.2364
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
N-Linked oligosaccharides arise when blocks of 14 sugars are added cotranslationally to newly synthesized polypeptides in the endoplasmic reticulum (ER), These glycans are then subjected to extensive modification as the glycoproteins mature and move through the ER via the Golgi complex to their final destinations inside and outside the cell. in the ER and in the early secretory pathway, where the repertoire of oligosaccharide structures is still rather small, the glycans play a pivotal role in protein folding, oligomerization, quality control, sorting, and transport. They are used as universal "tags" that allow specific Lectins and modifying enzymes to establish order among the diversity of maturing glycoproteins. in the Golgi complex, the glycans acquire more complex structures and a new set of functions. The division of synthesis and processing between the ER and the Golgi complex represents an evolutionary adaptation that allows efficient exploitation of the potential of oligosaccharides.
引用
收藏
页码:2364 / 2369
页数:6
相关论文
共 84 条
  • [11] CHA Y, 1990, J BIOL CHEM, V265, P5008
  • [12] A novel disorder caused by defective biosynthesis of N-linked oligosaccharides due to glucosidase I deficiency
    De Praeter, CM
    Gerwig, GJ
    Bause, E
    Nuytinck, LK
    Vliegenthart, JFG
    Breuer, W
    Kamerling, JP
    Espeel, MF
    Martin, JJR
    De Paepe, AM
    Chan, NWC
    Dacremont, GA
    Van Coster, RN
    [J]. AMERICAN JOURNAL OF HUMAN GENETICS, 2000, 66 (06) : 1744 - 1756
  • [13] GLYCOSIDASE INHIBITORS - INHIBITORS OF N-LINKED OLIGOSACCHARIDE PROCESSING
    ELBEIN, AD
    [J]. FASEB JOURNAL, 1991, 5 (15) : 3055 - 3063
  • [14] Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment
    Ellgaard, L
    Riek, R
    Braun, D
    Herrmann, T
    Helenius, A
    Wüthrich, K
    [J]. FEBS LETTERS, 2001, 488 (1-2) : 69 - 73
  • [15] NMR structure of the calreticulin P-domain
    Ellgaard, L
    Riek, R
    Herrmann, T
    Güntert, P
    Braun, D
    Helenius, A
    Wüthrich, K
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (06) : 3133 - 3138
  • [16] FIELDER K, 1994, EMBO J, V13, P1729
  • [17] Füllekrug J, 1999, J CELL SCI, V112, P2813
  • [18] Why mammalian cell surface proteins are glycoproteins
    Gahmberg, CG
    Tolvanen, M
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1996, 21 (08) : 308 - 311
  • [19] SEQUENCE DIFFERENCES BETWEEN GLYCOSYLATED AND NONGLYCOSYLATED ASN-X-THR SER ACCEPTOR SITES - IMPLICATIONS FOR PROTEIN ENGINEERING
    GAVEL, Y
    VONHEIJNE, G
    [J]. PROTEIN ENGINEERING, 1990, 3 (05): : 433 - 442
  • [20] GRANGER BL, 1990, J BIOL CHEM, V265, P12036