Putting the brakes on the unfolded protein response

被引：5

作者：

Sicheri, Frank ^{[1
]}

Silverman, Robert H. ^{[2
]}

机构：

[1] Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Program Syst Biol, Toronto, ON M5G 1X5, Canada

[2] Cleveland Clin, Dept Canc Biol, Lerner Res Inst, Cleveland, OH 44195 USA

来源：

JOURNAL OF CELL BIOLOGY | 2011年 / 193卷 / 01期

关键词：

ENDOPLASMIC-RETICULUM; TRANSMEMBRANE PROTEIN; KINASE-ACTIVITY; RNASE-L; IRE1P; NUCLEUS; ER;

D O I：

10.1083/jcb.201101105

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The unfolded protein response is an ancient cellular pathway for rapidly responding to endoplasmic reticulum stress. Two studies in this issue (Rubio et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201007077 and Chawla et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201008071) provide insight into how the unfolded protein response is tamped down to restore normal endoplasmic reticulum function. Although both papers implicate the Ire1 kinase domain as the key effector of the off-switch mechanism, alternate models for how this is achieved are proposed.

引用

页码：17 / 19

页数：3

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