您的账号已在其他设备登录,您当前账号已强迫下线,
如非您本人操作,建议您在会员中心进行密码修改

确定
收藏 | 浏览39

The phosphorylation and dephosphorylation of proteins are crucial in the regulation of protein activity and stability in various signaling pathways. In this study, we identified an ABA repressor, Arabidopsis Ying Yang 1 (AtYY1) as a potential target of casein kinase II (CKII). AtYY1 physically interacts with two regulatory subunits of CKII, CKB3, and CKB4. Moreover, AtYY1 can be phosphorylated by CKII in vitro, and the S284 site is the major CKII phosphorylation site. Further analyses indicated that S284 phosphorylation can enhance the transcriptional activity and protein stability of AtYY1 and hence strengthen the effect of AtYY1 as a negative regulator in the ABA response. Our study provides novel insights into the regulatory mechanism of AtYY1 mediated by CKII phosphorylation.

作者:Xiu-Yun, Wu;Tian, Li

来源:Frontiers in plant science 2017 年 8卷

知识库介绍

临床诊疗知识库该平台旨在解决临床医护人员在学习、工作中对医学信息的需求,方便快速、便捷的获取实用的医学信息,辅助临床决策参考。该库包含疾病、药品、检查、指南规范、病例文献及循证文献等多种丰富权威的临床资源。

详细介绍
热门关注
免责声明:本知识库提供的有关内容等信息仅供学习参考,不代替医生的诊断和医嘱。

收藏
| 浏览:39
作者:
Xiu-Yun, Wu;Tian, Li
来源:
Frontiers in plant science 2017 年 8卷
标签:
ABA response AtYY1 casein kinase II phosphorylation site protein stability transcriptional activity
The phosphorylation and dephosphorylation of proteins are crucial in the regulation of protein activity and stability in various signaling pathways. In this study, we identified an ABA repressor, Arabidopsis Ying Yang 1 (AtYY1) as a potential target of casein kinase II (CKII). AtYY1 physically interacts with two regulatory subunits of CKII, CKB3, and CKB4. Moreover, AtYY1 can be phosphorylated by CKII in vitro, and the S284 site is the major CKII phosphorylation site. Further analyses indicated that S284 phosphorylation can enhance the transcriptional activity and protein stability of AtYY1 and hence strengthen the effect of AtYY1 as a negative regulator in the ABA response. Our study provides novel insights into the regulatory mechanism of AtYY1 mediated by CKII phosphorylation.