Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol

被引:52
作者
Christis, Chantal [1 ]
Lubsen, Nicolette H. [2 ]
Braakman, Ineke [1 ]
机构
[1] Univ Utrecht, Bijvoet Ctr Biomol Res, Fac Sci, NL-3584 CH Utrecht, Netherlands
[2] Radboud Univ Nijmegen, NL-6525 ED Nijmegen, Netherlands
基金
英国医学研究理事会;
关键词
chaperone; disulfide bond formation; endoplasmic reticulum; ERAD; glycosylation; lectin; oligomerization; protein folding; quality control; unfolded protein response;
D O I
10.1111/j.1742-4658.2008.06590.x
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
A correct three-dimensional structure is a prerequisite for protein functionality, and therefore for life. Thus, it is not surprising that our cells are packed with proteins that assist protein folding, the process in which the native three-dimensional structure is formed. In general, plasma membrane and secreted proteins, as well as those residing in compartments along the endocytic and exocytic pathways, fold and oligomerize in the endoplasmic reticulum. The proteins residing in the endoplasmic reticulum are specialized in the folding of this subset of proteins, which renders this compartment a protein-folding factory. This review focuses on protein folding in the endoplasmic reticulum, and discusses the challenge of oligomer formation in the endoplasmic reticulum as well as the cytosol.
引用
收藏
页码:4700 / 4727
页数:28
相关论文
共 281 条
  • [1] XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks
    Acosta-Alvear, Diego
    Zhou, Yiming
    Blais, Alexandre
    Tsikitis, Mary
    Lents, Nathan H.
    Arias, Carolina
    Lennon, Christen J.
    Kluger, Yuval
    Dynlacht, Brian David
    [J]. MOLECULAR CELL, 2007, 27 (01) : 53 - 66
  • [2] Protein targeting to endoplasmic reticulum by dilysine signals involves direct retention in addition to retrieval
    Andersson, H
    Kappeler, F
    Hauri, HP
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (21) : 15080 - 15084
  • [3] ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
    Anelli, T
    Alessio, M
    Mezghrani, A
    Simmen, T
    Talamo, F
    Bachi, A
    Sitia, R
    [J]. EMBO JOURNAL, 2002, 21 (04) : 835 - 844
  • [4] Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44
    Anelli, T
    Alessio, M
    Bachi, A
    Bergamelli, L
    Bertoli, G
    Camerini, S
    Mezghrani, A
    Ruffato, E
    Simmen, T
    Sitia, R
    [J]. EMBO JOURNAL, 2003, 22 (19) : 5015 - 5022
  • [5] Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis
    Anelli, Tiziana
    Ceppi, Stefania
    Bergamelli, Leda
    Cortini, Margherita
    Masciarelli, Silvia
    Valetti, Caterina
    Sitia, Roberto
    [J]. EMBO JOURNAL, 2007, 26 (19) : 4177 - 4188
  • [6] KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF REDUCED POLYPEPTIDE CHAIN
    ANFINSEN, CB
    HABER, E
    SELA, M
    WHITE, FH
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1961, 47 (09) : 1309 - +
  • [7] Luteinizing hormone receptor ectodomain splice variant misroutes the full-length receptor into a subcompartment of the endoplasmic reticulum
    Apaja, PM
    Tuusa, JT
    Pietilä, EM
    Rajaniemi, HJ
    Petäjä-Repo, UE
    [J]. MOLECULAR BIOLOGY OF THE CELL, 2006, 17 (05) : 2243 - 2255
  • [8] GRP94, an ER chaperone with protein and peptide binding properties
    Argon, Y
    Simen, BB
    [J]. SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY, 1999, 10 (05) : 495 - 505
  • [9] BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP
    Awad, Walid
    Estrada, Isaac
    Shen, Ying
    Hendershot, Linda M.
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (04) : 1164 - 1169
  • [10] COPII-dependent transport from the endoplasmic reticulum
    Barlowe, C
    [J]. CURRENT OPINION IN CELL BIOLOGY, 2002, 14 (04) : 417 - 422