Versatility of the endoplasmic reticulum protein folding factory

被引：166

作者：

van Anken, E ^{[1
]}

Braakman, I ^{[1
]}

机构：

[1] Univ Utrecht, Dept Cellular Prot Chem, Bijvoet Ctr, NL-3584 CH Utrecht, Netherlands

来源：

CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY | 2005年 / 40卷 / 04期

关键词：

chaperones; PDI; BiP; calnexin; EDEM; ERAD;

D O I：

10.1080/10409230591008161

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 (ER) is dedicated to import, folding and assembly of all proteins that travel along or reside in the secretory pathway of eukaryotic cells. Folding in the ER is special. For instance, newly synthesized proteins are N-glycosylated and by default form disulfide bonds in the ER, but not elsewhere in the cell. In this review, we discuss which features distinguish the ER as an efficient folding factory, how the ER monitors its output and how it disposes of folding failures.

引用

收藏

页码：191 / 228

页数：38

相关论文

共 450 条

[1] TOPOGRAPHY OF GLYCOSYLATION REACTIONS IN THE ENDOPLASMIC-RETICULUM [J].

ABEIJON, C ;

HIRSCHBERG, CB .

TRENDS IN BIOCHEMICAL SCIENCES, 1992, 17 (01) :32-36

[2] Tail-anchored and signal-anchored proteins utilize overlapping pathways during membrane insertion [J].

Abell, BM ;

Jung, M ;

Oliver, JD ;

Knight, BC ;

Tyedmers, J ;

Zimmermann, R ;

High, S .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (08) :5669-5678

[3] Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member [J].

Alanen, HI ;

Williamson, RA ;

Howard, MJ ;

Lappi, AK ;

Jäntti, HP ;

Rautio, SM ;

Kellokumpu, S ;

Ruddock, LW .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (31) :28912-28920

[4] The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum [J].

Alder, NN ;

Shen, Y ;

Brodsky, JL ;

Hendershot, LM ;

Johnson, AE .

JOURNAL OF CELL BIOLOGY, 2005, 168 (03) :389-399

[5] INTRACELLULAR FOLDING OF TISSUE-TYPE PLASMINOGEN-ACTIVATOR - EFFECTS OF DISULFIDE BOND FORMATION ON N-LINKED GLYCOSYLATION AND SECRETION [J].

ALLEN, S ;

NAIM, HY ;

BULLEID, NJ .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (09) :4797-4804

[6] ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family [J].

Anelli, T ;

Alessio, M ;

Mezghrani, A ;

Simmen, T ;

Talamo, F ;

Bachi, A ;

Sitia, R .

EMBO JOURNAL, 2002, 21 (04) :835-844

[7] Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44 [J].

Anelli, T ;

Alessio, M ;

Bachi, A ;

Bergamelli, L ;

Bertoli, G ;

Camerini, S ;

Mezghrani, A ;

Ruffato, E ;

Simmen, T ;

Sitia, R .

EMBO JOURNAL, 2003, 22 (19) :5015-5022

[8]

Anfinsen C B, 1975, Adv Protein Chem, V29, P205, DOI 10.1016/S0065-3233(08)60413-1

[9] The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules [J].

Antoniou, AN ;

Ford, S ;

Alphey, M ;

Osborne, A ;

Elliott, T ;

Powis, SJ .

EMBO JOURNAL, 2002, 21 (11) :2655-2663

[10] The lectin ERGIC-53 is a cargo transport receptor for glycoproteins [J].

Appenzeller, C ;

Andersson, H ;

Kappeler, F ;

Hauri, HP .

NATURE CELL BIOLOGY, 1999, 1 (06) :330-334

← 1 2 3 4 5 6 7 8 9 10 →