UPR Signal Activation by Luminal Sensor Domains

被引：43

作者：

Carrara, Marta ^{[1
]}

Prischi, Filippo ^{[1
]}

Ali, Maruf M. U. ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Dept Life Sci, Struct Biol Ctr, London SW7 2AZ, England

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2013年 / 14卷 / 03期

关键词：

unfolded protein response; ER-stress; signaling; UNFOLDED-PROTEIN RESPONSE; ENDOPLASMIC-RETICULUM STRESS; GLUCOSE-REGULATED PROTEINS; ER-STRESS; QUALITY-CONTROL; IRE1; BIP; BINDING; KINASE; DISSOCIATION;

D O I：

10.3390/ijms14036454

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：

The unfolded protein response (UPR) is a cell-signaling system that detects the accumulation of unfolded protein within the endoplasmic reticulum (ER) and initiates a number of cellular responses to restore ER homeostasis. The presence of unfolded protein is detected by the ER-luminal sensor domains of the three UPR-transducer proteins IRE1, PERK, and ATF6, which then propagate the signal to the cytosol. In this review, we discuss the various mechanisms of action that have been proposed on how the sensor domains detect the presence of unfolded protein to activate downstream UPR signaling.

引用

页码：6454 / 6466

页数：13

共 44 条

[1]

Messenger RNA targeting to endoplasmic reticulum stress signalling sites [J].