Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?

被引:125
作者
High, S [1 ]
Lecomte, FJL [1 ]
Russell, SJ [1 ]
Abell, BM [1 ]
Oliver, JD [1 ]
机构
[1] Univ Manchester, Sch Biol Sci, Manchester M13 9PT, Lancs, England
关键词
endoplasmic reticulum; glycoprotein; protein folding; molecular chaperone; calnexin; ERp57;
D O I
10.1016/S0014-5793(00)01666-5
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 a major site of protein synthesis and its inside, or lumen, is a major site of protein folding, The lumen of the ER contains many folding factors and molecular chaperones, which facilitate protein folding by increasing both the rate and the efficiency of this process. Amongst the many ER folding factors, there are three components that specifically modulate the folding glycoproteins bearing N-linked carbohydrate side chains. These components are calnexin, calreticulin and ERp57, and this review focuses on the molecular basis for their capacity to influence glycoprotein folding. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:38 / 41
页数:4
相关论文
共 32 条
[1]   Calnexin and calreticulin bind to enzymically active tissue-type plasminogen activator during biosynthesis and are not required for folding to the native conformation [J].
Allen, S ;
Bulleid, NJ .
BIOCHEMICAL JOURNAL, 1997, 328 :113-119
[2]   CDNA CLONING AND BACULOVIRUS EXPRESSION OF THE HUMAN LIVER ENDOPLASMIC-RETICULUM P58 - CHARACTERIZATION AS A PROTEIN DISULFIDE-ISOMERASE ISOFORM, BUT NOT AS A PROTEASE OR A CARNITINE ACYLTRANSFERASE [J].
BOURDI, M ;
DEMADY, D ;
MARTIN, JL ;
JABBOUR, SK ;
MARTIN, BM ;
GEORGE, JW ;
POHL, LR .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1995, 323 (02) :397-403
[3]   Ca2+ regulation of interactions between endoplasmic reticulum chaperones [J].
Corbett, EF ;
Oikawa, K ;
Francois, P ;
Tessier, DC ;
Kay, C ;
Bergeron, JJM ;
Thomas, DY ;
Krause, KH ;
Michalak, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (10) :6203-6211
[4]   Setting the standards: Quality control in the secretory pathway [J].
Ellgaard, L ;
Molinari, M ;
Helenius, A .
SCIENCE, 1999, 286 (5446) :1882-1888
[5]   The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins [J].
Elliott, JG ;
Oliver, JD ;
High, S .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (21) :13849-13855
[6]   The protein disulphide-isomerase family:: unravelling a string of folds [J].
Ferrari, DM ;
Söling, HD .
BIOCHEMICAL JOURNAL, 1999, 339 :1-10
[7]   Protein folding - Linking catalysts to chemistry [J].
Freedman, R .
NATURE, 1999, 402 (6757) :27-+
[8]   PROTEIN DISULFIDE-ISOMERASE - BUILDING BRIDGES IN PROTEIN-FOLDING [J].
FREEDMAN, RB ;
HIRST, TR ;
TUITE, MF .
TRENDS IN BIOCHEMICAL SCIENCES, 1994, 19 (08) :331-336
[9]   PROTEIN FOLDING IN THE CELL [J].
GETHING, MJ ;
SAMBROOK, J .
NATURE, 1992, 355 (6355) :33-45
[10]   Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase [J].
Gillece, P ;
Luz, JM ;
Lennarz, WJ ;
de la Cruz, FJ ;
Römisch, K .
JOURNAL OF CELL BIOLOGY, 1999, 147 (07) :1443-1456