气候变化领域集成服务门户(CCPortal): Nucleocytoplasmic trafficking and turnover mechanisms of BRASSINAZOLE RESISTANT1 in Arabidopsis thaliana

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DOI	10.1073/pnas.2101838118
	Nucleocytoplasmic trafficking and turnover mechanisms of BRASSINAZOLE RESISTANT1 in Arabidopsis thaliana
	Wang R.; Wang R.; Liu M.; Yuan W.; Zhao Z.; Liu X.; Peng Y.; Yang X.; Sun Y.; Tang W.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:33
英文摘要	Regulation of the nucleocytoplasmic trafficking of signaling components, especially transcription factors, is a key step of signal transduction in response to extracellular stimuli. In the brassinosteroid (BR) signal transduction pathway, transcription factors from the BRASSINAZOLE RESISTANT1 (BZR1) family are essential in mediating BR-regulated gene expression. The subcellular localization and transcriptional activity of BZR1 are tightly regulated by reversible protein phosphorylation; however, the underlying mechanism is not well understood. Here, we provide evidence that both BZR1 phosphorylation and dephosphorylation occur in the nucleus and that BR-regulated nuclear localization of BZR1 is independent from its interaction with, or dephosphorylation by, protein phosphatase 2A. Using a photoconvertible fluorescent protein, Kaede, as a living tag to distinguish newly synthesized BZR1 from existing BZR1, we demonstrated that BR treatment recruits cytosolic BZR1 to the nucleus, which could explain the fast responses of plants to BR. Additionally, we obtained evidence for two types of protein turnover mechanisms that regulate BZR1 abundance in plant cells: a BR- and 26S proteosome-independent constitutive degradation mechanism and a BR-activated 26S proteosome-dependent proteolytic mechanism. Finally, treating plant cells with inhibitors of 26S proteosome induces the nuclear localization and dephosphorylation of BZR1, even in the absence of BR signaling. Based on these results, we propose a model to explain how BR signaling regulates the nucleocytoplasmic trafficking and reversible phosphorylation of BZR1. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Brassinosteroid; BZR1; Nucleocytoplasmic trafficking; Signal transduction; Turnover
语种	英语
scopus关键词	brassinosteroid; phosphoprotein phosphatase 2A; proteasome; Arabidopsis protein; BZR1 protein, Arabidopsis; DNA binding protein; Arabidopsis thaliana; Article; controlled study; dephosphorylation; nonhuman; nucleocytoplasmic transport; plant cell; protein degradation; protein function; protein interaction; protein localization; protein metabolism; protein phosphorylation; signal transduction; Arabidopsis; gene expression regulation; genetics; metabolism; mutation; nucleocytoplasmic transport; physiology; seedling; transgenic plant; Active Transport, Cell Nucleus; Arabidopsis; Arabidopsis Proteins; DNA-Binding Proteins; Gene Expression Regulation, Plant; Mutation; Plants, Genetically Modified; Seedlings
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/251071
作者单位	Ministry of Education Key Laboratory of Molecular and Cellular Biology, Hebei Collaboration Innovation Center for Cell Signaling and Environmental Adaptation, Hebei Key Laboratory of Molecular and Cellular Biology, College of Life Sciences, Hebei Normal University, Shijiazhuang, 050024, China; Department of Bioscience and Bioengineering, Hebei University of Science and Technology, Shijiazhuang, 050000, China
推荐引用方式 GB/T 7714	Wang R.,Wang R.,Liu M.,et al. Nucleocytoplasmic trafficking and turnover mechanisms of BRASSINAZOLE RESISTANT1 in Arabidopsis thaliana[J],2021,118(33).
APA	Wang R..,Wang R..,Liu M..,Yuan W..,Zhao Z..,...&Tang W..(2021).Nucleocytoplasmic trafficking and turnover mechanisms of BRASSINAZOLE RESISTANT1 in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America,118(33).
MLA	Wang R.,et al."Nucleocytoplasmic trafficking and turnover mechanisms of BRASSINAZOLE RESISTANT1 in Arabidopsis thaliana".Proceedings of the National Academy of Sciences of the United States of America 118.33(2021).