The endoplasmic reticulum: integration of protein folding, quality control, signaling and degradation

被引:107
作者
Chevet, E [1 ]
Cameron, PH
Pelletier, MF
Thomas, DY
Bergeron, JJM
机构
[1] McGill Univ, Dept Anat & Cell Biol, Montreal, PQ H3A 2B2, Canada
[2] McGill Univ, Dept Biochem, Montreal, PQ H3A 2B2, Canada
关键词
D O I
10.1016/S0959-440X(00)00168-8
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
The endoplasmic reticulum is the entry point into the secretory pathway. To acquire a correct conformation, secretory proteins encounter the endoplasmic reticulum molecular machines of folding, quality control, signaling and disposal, which function as an integrated mechanism. The creation of such a molecular network, spatially regulated, suggests how the endoplasmic reticulum promotes the release of correctly folded secretory proteins.
引用
收藏
页码:120 / 124
页数:5
相关论文
共 47 条
  • [1] Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    Bertolotti, A
    Zhang, YH
    Hendershot, LM
    Harding, HP
    Ron, D
    [J]. NATURE CELL BIOLOGY, 2000, 2 (06) : 326 - 332
  • [2] Role of Cue1p in ubiquitination and degradation at the ER surface
    Biederer, T
    Volkwein, C
    Sommer, T
    [J]. SCIENCE, 1997, 278 (5344) : 1806 - 1809
  • [3] The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
    Brodsky, JL
    Werner, ED
    Dubas, ME
    Goeckeler, JL
    Kruse, KB
    McCracken, AA
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (06) : 3453 - 3460
  • [4] Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    Brown, MS
    Ye, J
    Rawson, RB
    Goldstein, JL
    [J]. CELL, 2000, 100 (04) : 391 - 398
  • [5] Processing by endoplasmic reticulum mannosidases partitions a secretion-impaired glycoprotein into distinct disposal pathways
    Cabral, CM
    Choudhury, P
    Liu, Y
    Sifers, RN
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (32) : 25015 - 25022
  • [6] Degradation of proteins from the ER of S-cerevisiae requires an intact unfolded protein response pathway
    Casagrande, R
    Stern, P
    Diehn, M
    Shamu, C
    Osario, M
    Zúñiga, M
    Brown, PO
    Ploegh, H
    [J]. MOLECULAR CELL, 2000, 5 (04) : 729 - 735
  • [7] Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes
    Chevet, E
    Wong, HN
    Gerber, D
    Cochet, C
    Fazel, A
    Cameron, PH
    Gushue, JN
    Thomas, DY
    Bergeron, JJM
    [J]. EMBO JOURNAL, 1999, 18 (13) : 3655 - 3666
  • [8] Calnexin family members as modulators of genetic diseases
    Chevet, E
    Jakob, CA
    Thomas, DY
    Bergeron, JJM
    [J]. SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY, 1999, 10 (05) : 473 - 480
  • [9] Setting the standards: Quality control in the secretory pathway
    Ellgaard, L
    Molinari, M
    Helenius, A
    [J]. SCIENCE, 1999, 286 (5446) : 1882 - 1888
  • [10] A regulatory link between ER-associated protein degradation and the unfolded-protein response.
    Friedlander, R
    Jarosch, E
    Urban, J
    Volkwein, C
    Sommer, T
    [J]. NATURE CELL BIOLOGY, 2000, 2 (07) : 379 - 384