ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase

被引:123
作者
Coe, Helen [1 ,2 ]
Michalak, Marek [1 ,2 ]
机构
[1] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada
[2] Univ Alberta, Dept Pediat, Edmonton, AB T6G 2H7, Canada
基金
加拿大健康研究院;
关键词
Endoplasmic reticulum; Oxidoreductase; STAT3; Protein folding; ERp57; PROTEIN DISULFIDE-ISOMERASE; GLUCOSE-REGULATED PROTEIN; MOLECULAR-CLONING; CRYSTAL-STRUCTURE; CALRETICULIN; CALNEXIN; CELLS; EXPRESSION; COMPLEXES; DOMAINS;
D O I
10.1016/j.biocel.2010.01.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
ERp57 is a 58-kDa thiol oxidoreductase and a member of the protein disulfide isomerase (PDI)-like family. ERp57 is highly similar to other PDI family members in terms of amino acid sequence and structural/functional domain organization; however, It possesses some distinctive structural features that dictate its unique functions in the cell This protein plays an important role in endoplasmic reticulum quality control of newly synthesized glycoproteins, is critical in major histocompatability complex (MHC) class I assembly and regulates gene expression. Studies on ERp57-deficient mice indicate that the protein is critical during embryonic development The protein has been implicated in human pathologies including cancer and Alzheimer's disease. (C) 2010 Elsevier Ltd. All rights reserved
引用
收藏
页码:796 / 799
页数:4
相关论文
共 27 条
[1]
MOLECULAR-CLONING AND COMPLETE AMINO-ACID-SEQUENCE OF FORM-I PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE-C [J].
BENNETT, CF ;
BALCAREK, JM ;
VARRICHIO, A ;
CROOKE, ST .
NATURE, 1988, 334 (6179) :268-270
[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]
Coe H., 2009, J BIOL CHEM
[4]
Nuclear localization and DNA interaction of protein disulfide isomerase ERp57 in mammalian cells [J].
Coppari, S ;
Altieri, F ;
Ferraro, A ;
Chichiarelli, S ;
Eufemi, M ;
Turano, C .
JOURNAL OF CELLULAR BIOCHEMISTRY, 2002, 85 (02) :325-333
[5]
Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer [J].
Dong, Gang ;
Wearsch, Pamela A. ;
Peaper, David R. ;
Cresswell, Peter ;
Reinisch, Karin M. .
IMMUNITY, 2009, 30 (01) :21-32
[6]
In cerebrospinal fluid ER chaperones ERp57 and calreticulin bind β-amyloid [J].
Erickson, RR ;
Dunning, LM ;
Olson, DA ;
Cohen, SJ ;
Davis, AT ;
Wood, WG ;
Kratzke, RA ;
Holtzman, JL .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2005, 332 (01) :50-57
[7]
ERp57 is present in STAT3-DNA complexes [J].
Eufemi, M ;
Coppari, S ;
Altieri, F ;
Grillo, C ;
Ferraro, A ;
Turano, C .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2004, 323 (04) :1306-1312
[8]
Frickel E.M., 2004, J BIOL CHEM
[9]
Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57 [J].
Garbi, N ;
Tanaka, S ;
Momburg, F ;
Hämmerling, GJ .
NATURE IMMUNOLOGY, 2006, 7 (01) :93-102
[10]
Association of the chaperone (GRP58/ER-60/ERp57) with membrane glucose-regulated protein 58 stat3 in cytosol and plasma complexes [J].
Guo, GG ;
Patel, K ;
Kumar, V ;
Shah, M ;
Fried, VA ;
Etlinger, JD ;
Sehgal, PB .
JOURNAL OF INTERFERON AND CYTOKINE RESEARCH, 2002, 22 (05) :555-563