BiP binding keeps ATF6 at bay

被引:63
作者
Sommer, T [1 ]
Jarosch, E [1 ]
机构
[1] Max Delbruck Ctr Mol Med, D-13092 Berlin, Germany
关键词
D O I
10.1016/S1534-5807(02)00210-1
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
A study by Shen et al. in this issue of Developmental Cell shows that transport to the Golgi complex and subsequent proteolytic activation of the stress-regulated transcription factor ATF6 is initiated by the dissociation of the ER chaperone BiP from ATF6. This demonstrates that BiP is a key element in sensing the folding capacity within the ER and provides mechanistic insights on how the activation of membrane-bound transcription factors can be regulated.
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页码:1 / 2
页数:2
相关论文
共 8 条
[1]   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
[2]   The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor [J].
Brown, MS ;
Goldstein, JL .
CELL, 1997, 89 (03) :331-340
[3]   IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA [J].
Calfon, M ;
Zeng, HQ ;
Urano, F ;
Till, JH ;
Hubbard, SR ;
Harding, HP ;
Clark, SG ;
Ron, D .
NATURE, 2002, 415 (6867) :92-96
[4]   The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi [J].
Chen, X ;
Shen, J ;
Prywes, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (15) :13045-13052
[5]   The unfolding tale of the unfolded protein response [J].
Ma, YJ ;
Hendershot, LM .
CELL, 2001, 107 (07) :827-830
[6]   Tripartite management of unfolded proteins in the endoplasmic reticulum [J].
Mori, K .
CELL, 2000, 101 (05) :451-454
[7]   ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals [J].
Shen, JS ;
Chen, X ;
Hendershot, L ;
Prywes, R .
DEVELOPMENTAL CELL, 2002, 3 (01) :99-111
[8]   ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs [J].
Ye, J ;
Rawson, RB ;
Komuro, R ;
Chen, X ;
Davé, UP ;
Prywes, R ;
Brown, MS ;
Goldstein, JL .
MOLECULAR CELL, 2000, 6 (06) :1355-1364