ERAD and how viruses exploit it

被引:57
作者
Byun, Hyewon
Gou, Yongqiang
Zook, Adam
Lozano, Mary M.
Dudley, Jaquelin P. [1 ,2 ]
机构
[1] Univ Texas Austin, Dept Mol Biosci, Ctr Infect Dis, Austin, TX 78712 USA
[2] Univ Texas Austin, Inst Cellular & Mol Biol, Austin, TX 78712 USA
来源
FRONTIERS IN MICROBIOLOGY | 2014年 / 5卷
关键词
ERAD; immune response; retrotranslocation; ubiquitination; proteasomal degradation; retrovirus; herpesvirus; polyomavirus; RETICULUM-ASSOCIATED DEGRADATION; PROTEIN DISULFIDE-ISOMERASE; MAMMALIAN ENDOPLASMIC-RETICULUM; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN LIGASE COMPLEX; SIGNAL PEPTIDE PEPTIDASE; HEPATITIS-B-VIRUS; CLASS-I MOLECULES; QUALITY-CONTROL; CHOLERA-TOXIN;
D O I
10.3389/fmicb.2014.00330
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Endoplasmic reticulum (ER)-associated degradation (ERAD) is a universally important process among eukaryotic cells. ERAD is necessary to preserve cell integrity since the accumulation of defective proteins results in diseases associated with neurological dysfunction, cancer, and infections. This process involves recognition of misfolded or misassembled proteins that have been translated in association with ER membranes. Recognition of ERAD substrates leads to their extraction through the ER membrane (retrotranslocation or dislocation), ubiquitination, and destruction by cytosolic proteasomes. This review focuses on ERAD and its components as well as how viruses use this process to promote their replication and to avoid the immune response.
引用
收藏
页数:16
相关论文
共 208 条
  • [1] p97 is in a complex with cholera toxin and influences the transport of cholera toxin and related toxins to the cytoplasm
    AbuJarour, RJ
    Dalal, S
    Hanson, PI
    Draper, RK
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (16) : 15865 - 15871
  • [2] N-glycan structures: recognition and processing in the ER
    Aebi, Markus
    Bernasconi, Riccardo
    Clerc, Simone
    Molinari, Maurizio
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 2010, 35 (02) : 74 - 82
  • [3] UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1α turnover
    Alexandru, Gabriela
    Graumann, Johannes
    Smith, Geoffrey T.
    Kolawa, Natalie J.
    Fang, Ruihua
    Deshaies, Raymond J.
    [J]. CELL, 2008, 134 (05) : 804 - 816
  • [4] INTRACELLULAR FOLDING OF TISSUE-TYPE PLASMINOGEN-ACTIVATOR - EFFECTS OF DISULFIDE BOND FORMATION ON N-LINKED GLYCOSYLATION AND SECRETION
    ALLEN, S
    NAIM, HY
    BULLEID, NJ
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (09) : 4797 - 4804
  • [5] Enhanced CD4 down-modulation by late stage HIV-1 nef alleles is associated with increased env incorporation and viral replication
    Argañaraz, ER
    Schindler, M
    Kirchhoff, F
    Cortes, MJ
    Lama, J
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (36) : 33912 - 33919
  • [6] Functional and genomic analyses of blocked protein O-mannosylation in baker's yeast
    Arroyo, Javier
    Hutzler, Johannes
    Bermejo, Clara
    Ragni, Enrico
    Garcia-Cantalejo, Jess
    Botias, Pedro
    Piberger, Heidi
    Schott, Andrea
    Belen Sanz, Ana
    Strahl, Sabine
    [J]. MOLECULAR MICROBIOLOGY, 2011, 79 (06) : 1529 - 1546
  • [7] A Network of Cytosolic Factors Targets SRP-Independent Proteins to the Endoplasmic Reticulum
    Ast, Tslil
    Cohen, Galit
    Schuldiner, Maya
    [J]. CELL, 2013, 152 (05) : 1134 - 1145
  • [8] Signal peptidase I: Cleaving the way to mature proteins
    Auclair, Sarah M.
    Bhanu, Meera K.
    Kendall, Debra A.
    [J]. PROTEIN SCIENCE, 2012, 21 (01) : 13 - 25
  • [9] Amino acid composition of α1/α2 domains and cytoplasmic tail of MHC class I molecules determine their susceptibility to human cytomegalovirus US11-mediated down-regulation
    Barel, MT
    Pizzato, N
    van Leeuwen, D
    Le Bouteiller, P
    Wiertz, EJHJ
    Lenfant, F
    [J]. EUROPEAN JOURNAL OF IMMUNOLOGY, 2003, 33 (06) : 1707 - 1716
  • [10] INTERACTIONS AMONG THE MAJOR AND MINOR COAT PROTEINS OF POLYOMAVIRUS
    BAROUCH, DH
    HARRISON, SC
    [J]. JOURNAL OF VIROLOGY, 1994, 68 (06) : 3982 - 3989