Folding upon phosphorylation: translational regulation by a disorder-to-order transition

被引：9

作者：

Metskas, Lauren Ann ^{[1
,2
]}

Rhoades, Elizabeth ^{[1
,2
]}

机构：

[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA

[2] Yale Univ, Integrated Grad Program Phys & Engn Biol, New Haven, CT 06520 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2015年 / 40卷 / 05期

关键词：

intrinsically disordered proteins; translation; phosphorylation; PROTEIN; SWITCH;

D O I：

10.1016/j.tibs.2015.02.007

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：

4E binding proteins (4E-BPs) play an important role in the regulation of translation by binding to eukaryotic translation initiation factor 4E (eIF4E) and inhibiting assembly of the eIF4F complex. While phosphorylation of 4E-BPs is known to disrupt their binding to eIF4E, the mechanism by which this occurs has been unclear. In a recent study, Forman-Kay and coworkers demonstrate that this mechanism is primarily structure-based: phosphorylation of 4E-BPs results in a disorder-to-order transition, bringing them from their binding-competent disordered state to a folded state incompatible with eIF4E binding.

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收藏

页码：243 / 244

页数：2

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