Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications

被引：402
作者：
Bah, Alaji [1 ,2 ]
Forman-Kay, Julie D. [1 ,2 ]
机构：
[1] Hosp Sick Children, Program Mol Struct & Funct, Toronto, ON M5G 0A4, Canada
[2] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2016年 / 291卷 / 13期
基金：
加拿大健康研究院;
关键词：
intrinsically disordered protein; post-translational modification (PTM); protein conformation; protein-DNA interaction; protein-protein interaction; regulation; GAMMA-CARBOXYGLUTAMIC ACID; ETS-1; DNA-BINDING; MOLECULAR RECOGNITION; STRUCTURAL DISORDER; INTERMOLECULAR INTERACTIONS; MULTISITE PHOSPHORYLATION; TRANSLATION INITIATION; UNSTRUCTURED PROTEINS; PHASE-TRANSITIONS; CRYSTAL-STRUCTURE;
D O I：
10.1074/jbc.R115.695056
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：
Post-translational modifications (PTMs) produce significant changes in the structural properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes. PTMs can induce a range of effects, from local stabilization or destabilization of transient secondary structure to global disorder-to-order transitions, potentially driving complete state changes between intrinsically disordered and folded states or dispersed monomeric and phase-separated states. Here, we discuss diverse biological processes that are dependent on PTM regulation of IDPs. We also present recent tools for generating homogenously modified IDPs for studies of PTM-mediated IDP regulatory mechanisms.
引用
收藏
页码：6696 / 6705
页数：10
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