ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER

被引:102
作者
Bernasconi, Riccardo [1 ]
Molinari, Maurizio [1 ,2 ]
机构
[1] Inst Res Biomed, CH-6500 Bellinzona, Switzerland
[2] Ecole Polytech Fed Lausanne, Sch Life Sci, CH-1015 Lausanne, Switzerland
基金
瑞士国家科学基金会;
关键词
RETICULUM-ASSOCIATED DEGRADATION; UNFOLDED PROTEIN RESPONSE; UBIQUITIN LIGASE COMPLEX; ENDOPLASMIC-RETICULUM; QUALITY-CONTROL; MANNOSIDASE-I; MUTANT ALPHA-1-ANTITRYPSIN; GLYCOPROTEIN DEGRADATION; MISFOLDED PROTEINS; EDEM1;
D O I
10.1016/j.ceb.2010.10.002
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The endoplasmic reticulum (ER) is the site of maturation for secretory and membrane proteins in eukaryotic cells. Unsuccessful folding attempts are eventually interrupted and most folding-defective polypeptides are dislocated across the ER membrane and degraded by cytosolic proteasomes in a complex series of events collectively defined as ER-associated degradation (ERAD). Uncontrolled ERAD activity might prematurely interrupt ongoing folding programs. At steady state, this is prevented by ERAD tuning, that is, the removal of select ERAD regulators from the ER and their degradation by proteasomes and by endo-lysosomal proteases. In Coronaviruses infected cells, the formation of LC3-I coated vesicles containing ERAD regulators cleared from the ER lumen is co-opted to anchor viral replication and transcription complexes to ER-derived membranes.
引用
收藏
页码:176 / 183
页数:8
相关论文
共 67 条
[41]   Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins [J].
Oliver, JD ;
vanderWal, FJ ;
Bulleid, NJ ;
High, S .
SCIENCE, 1997, 275 (5296) :86-88
[42]   The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin [J].
Pearse, Bradley R. ;
Tamura, Taku ;
Sunryd, Johan C. ;
Grabowski, Gregory A. ;
Kaufman, Randal J. ;
Hebert, Daniel N. .
JOURNAL OF CELL BIOLOGY, 2010, 189 (05) :829-841
[43]   The role of autophagy in α-1-antitrypsin deficiency:: A specific cellular response in genetic diseases associated with aggregation-prone proteins [J].
Perlmutter, David H. .
AUTOPHAGY, 2006, 2 (04) :258-263
[44]   Defining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation [J].
Quan, Erin M. ;
Kamiya, Yukiko ;
Kamiya, Dailki ;
Denic, Vladimir ;
Weibezahn, Jimena ;
Kato, Koichi ;
Weissman, Jonathan S. .
MOLECULAR CELL, 2008, 32 (06) :870-877
[45]   Coronaviruses Hijack the LC3-I-Positive EDEMosomes, ER-Derived Vesicles Exporting Short-Lived ERAD Regulators, for Replication [J].
Reggiori, Fulvio ;
Monastyrska, Iryna ;
Verheije, Monique H. ;
Cali, Tito ;
Ulasli, Mustafa ;
Bianchi, Siro ;
Bernasconi, Riccardo ;
de Haan, Cornelis A. M. ;
Molinari, Maurizio .
CELL HOST & MICROBE, 2010, 7 (06) :500-508
[46]   Regulation of basal cellular physiology by the homeostatic unfolded protein response [J].
Rutkowski, D. Thomas ;
Hegde, Ramanujan S. .
JOURNAL OF CELL BIOLOGY, 2010, 189 (05) :783-794
[47]   Rapid degradation of a large fraction of newly synthesized proteins by proteasomes [J].
Schubert, U ;
Antón, LC ;
Gibbs, J ;
Norbury, CC ;
Yewdell, JW ;
Bennink, JR .
NATURE, 2000, 404 (6779) :770-774
[48]   Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency [J].
Schulz, Benjamin L. ;
Stirnimann, Christian U. ;
Grimshaw, John P. A. ;
Brozzo, Maurice S. ;
Fritsch, Fabienne ;
Mohorko, Elisabeth ;
Capitani, Guido ;
Glockshuber, Rudi ;
Gruetter, Markus G. ;
Aebi, Markus .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2009, 106 (27) :11061-11066
[49]   Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle [J].
Soldà, T ;
Garbi, N ;
Hämmerling, GJ ;
Molinari, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (10) :6219-6226
[50]   Substrate-specific requirements for UGT1-dependent release from calnexin [J].
Solda, Tatiana ;
Galli, Carmela ;
Kaufman, Randal J. ;
Molinari, Maurizio .
MOLECULAR CELL, 2007, 27 (02) :238-249