Functions and pathologies of BiP and its interaction partners

被引:167
作者
Dudek, J. [1 ]
Benedix, J. [1 ]
Cappel, S. [1 ]
Greiner, M. [1 ]
Jalal, C. [1 ]
Mueller, L. [1 ]
Zimmermann, R. [1 ]
机构
[1] Univ Saarland, D-66421 Homburg, Germany
关键词
BiP; ERj proteins; nucleotide exchange factors; unfolded protein response; haemolytic uraemic syndrome; Marinesco-Sjogren syndrome; polycystic liver disease; Wolcott-Rallison syndrome; MARINESCO-SJOGREN-SYNDROME; ENDOPLASMIC-RETICULUM STRESS; CHAIN BINDING-PROTEIN; ESCHERICHIA-COLI DNAJ; NUCLEOTIDE EXCHANGE FACTOR; WOLCOTT-RALLISON-SYNDROME; POLYCYSTIC LIVER-DISEASE; DOG PANCREAS MICROSOMES; MOLECULAR CHAPERONE; ER STRESS;
D O I
10.1007/s00018-009-8745-y
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 involved in a variety of essential and interconnected processes in human cells, including protein biogenesis, signal transduction, and calcium homeostasis. The central player in all these processes is the ER-lumenal polypeptide chain binding protein BiP that acts as a molecular chaperone. BiP belongs to the heat shock protein 70 (Hsp70) family and crucially depends on a number of interaction partners, including co-chaperones, nucleotide exchange factors, and signaling molecules. In the course of the last five years, several diseases have been linked to BiP and its interaction partners, such as a group of infectious diseases that are caused by Shigella toxin producing E. coli. Furthermore, the inherited diseases Marinesco-Sjogren syndrome, autosomal dominant polycystic liver disease, Wolcott-Rallison syndrome, and several cancer types can be considered BiP-related diseases. This review summarizes the physiological and pathophysiological characteristics of BiP and its interaction partners.
引用
收藏
页码:1556 / 1569
页数:14
相关论文
共 147 条
[1]   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
[2]  
[Anonymous], 2003, J BIOL SCI
[3]   The gene disrupted in Marinesco-Sjogren syndrome encodes SIL1, an HSPA5 cochaperone [J].
Anttonen, AK ;
Mahjneh, I ;
Hämäläinen, RH ;
Lagier-Tourenne, C ;
Kopra, O ;
Waris, L ;
Anttonen, M ;
Joensuu, T ;
Kalimo, H ;
Paetau, A ;
Tranebjaerg, L ;
Chaigne, D ;
Koenig, M ;
Eeg-Olofsson, O ;
Udd, B ;
Somer, M ;
Somer, H ;
Lehesjoki, AE .
NATURE GENETICS, 2005, 37 (12) :1309-1311
[4]   Novel SIL1 mutations and exclusion of functional candidate genes in Marinesco-Sjogren syndrome [J].
Anttonen, Anna-Kaisa ;
Siintola, Eija ;
Tranebjaerg, Lisbeth ;
Iwata, Nobue K. ;
Bijlsma, Emilia K. ;
Meguro, Hiroyuki ;
Ichikawa, Yaeko ;
Goto, Jun ;
Kopra, Outi ;
Lehesjoki, Anna-Elina .
EUROPEAN JOURNAL OF HUMAN GENETICS, 2008, 16 (08) :961-969
[5]   Visiting the ER: The endoplasmic reticulum as a target for therapeutics in traffic related diseases [J].
Aridor, Meir .
ADVANCED DRUG DELIVERY REVIEWS, 2007, 59 (08) :759-781
[6]   Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response [J].
Bertolotti, A ;
Zhang, YH ;
Hendershot, LM ;
Harding, HP ;
Ron, D .
NATURE CELL BIOLOGY, 2000, 2 (06) :326-332
[7]   Characterization of pancreatic ERj3p, ahomolog of yeast DnaJ-like protein Scj1p [J].
Bies, C ;
Blum, R ;
Dudek, J ;
Nastainczyk, W ;
Oberhauser, S ;
Jung, M ;
Zimmermann, R .
BIOLOGICAL CHEMISTRY, 2004, 385 (05) :389-395
[8]   A Scj1p homolog and folding catalysts present in dog pancreas microsomes [J].
Bies, C ;
Guth, S ;
Janoschek, K ;
Nastainczyk, W ;
Volkmer, J ;
Zimmermann, R .
BIOLOGICAL CHEMISTRY, 1999, 380 (10) :1175-1182
[9]   ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane [J].
Blau, M ;
Mullapudi, S ;
Becker, T ;
Dudek, J ;
Zimmermann, R ;
Penczek, PA ;
Beckmann, R .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2005, 12 (11) :1015-1016
[10]   TRANSFER OF PROTEINS ACROSS MEMBRANES .1. PRESENCE OF PROTEOLYTICALLY PROCESSED AND UNPROCESSED NASCENT IMMUNOGLOBULIN LIGHT-CHAINS ON MEMBRANE-BOUND RIBOSOMES OF MURINE MYELOMA [J].
BLOBEL, G ;
DOBBERSTEIN, B .
JOURNAL OF CELL BIOLOGY, 1975, 67 (03) :835-851