期刊
FRONTIERS IN PLANT SCIENCE
卷 9, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fpls.2018.00139
关键词
E3 ubiquitin-ligase; plant cell nucleus; post-translational modification; 26S proteasome; transcription factor
资金
- AgreenSkills fellowship within the EU Marie-Curie COFUND People Program [267196]
- Alfonso Martin Escudero Foundation
- French Laboratory of Excellence project TULIP [ANR-10-LABX-41, ANR-11-IDEX-0002-02]
Ubiquitination, the reversible protein conjugation with ubiquitin (Ub), is a post-translational modification that enables rapid and specific cellular responses to stimuli without requirement of de novo protein synthesis. Although ubiquitination also displays non-proteolytic functions, it often acts as a signal for selective protein degradation through the ubiquitin-proteasome system (UPS). In plants, it has become increasingly apparent that the UPS is a central regulator of many key cellular and physiological processes, including responses to biotic and abiotic stresses. In the nucleus, protein regulation via the UPS orchestrates gene expression, genome maintenance, and signal transduction. Here, we focus on E3 Ub-ligase proteins as major components of the ubiquitination cascade that confer specificity of substrate recognition. We provide an overview on how they contribute to nuclear proteome plasticity during plant responses to environmental stress signals.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据