气候变化领域集成服务门户(CCPortal): Persulfidation of ATG18a regulates autophagy under ER stress in Arabidopsis

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DOI	10.1073/pnas.2023604118
	Persulfidation of ATG18a regulates autophagy under ER stress in Arabidopsis
	Aroca A.; Yruela I.; Gotor C.; Bassham D.C.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:20
英文摘要	Hydrogen sulfide (H2S) is an endogenously generated gaseous signaling molecule, which recently has been implicated in autophagy regulation in both plants and mammals through persulfidation of specific targets. Persulfidation has been suggested as the molecular mechanism through which sulfide regulates autophagy in plant cells. ATG18a is a core autophagy component that is required for bulk autophagy and also for reticulophagy during endoplasmic reticulum (ER) stress. In this research,we revealed the role of sulfide in plant ER stress responses as a negative regulator of autophagy. We demonstrate that sulfide regulates ATG18a phospholipid-binding activity by reversible persulfidation at Cys103, and that this modification activates ATG18a binding capacity to specific phospholipids in a reversible manner. Our findings strongly suggest that persulfidation of ATG18a at C103 regulates autophagy under ER stress, and that the impairment of persulfidation affects both the number and size of autophagosomes. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	ATG18a; Autophagy; ER stress; Hydrogen sulfide; Persulfidation
语种	英语
scopus关键词	ATG18a protein; cys 103; phospholipid binding protein; unclassified drug; Arabidopsis protein; ATG18a protein, Arabidopsis; autophagy related protein; cysteine; hydrogen sulfide; persulfides; phospholipid; protein binding; sulfide; Arabidopsis; Article; autophagosome; autophagy (cellular); biogenesis; controlled study; endoplasmic reticulum stress; nonhuman; persulfidation; physiological stress; priority journal; static electricity; translational protein modification; autophagy; binding site; chemistry; gene expression regulation; genetics; metabolism; molecular model; protein conformation; protein domain; protein processing; signal transduction; Arabidopsis; Arabidopsis Proteins; Autophagosomes; Autophagy; Autophagy-Related Proteins; Binding Sites; Cysteine; Endoplasmic Reticulum Stress; Gene Expression Regulation, Plant; Hydrogen Sulfide; Models, Molecular; Phospholipids; Protein Binding; Protein Conformation; Protein Interaction Domains and Motifs; Protein Processing, Post-Translational; Signal Transduction; Sulfides
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/251183
作者单位	Department of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50011, United States; Institute of Plant Biochemistry and Photosynthesis, Consejo Superior de Investigaciones Científicas, University of Seville, Seville, 41029, Spain; Consejo Superior de Investigaciones Científicas, Estación Experimental de Aula Dei, Zaragoza, 50059, Spain; Group of Biochemistry, Biophysics and Computational Biology, Consejo Superior de Investigaciones Científicas, University of Zaragoza, Zaragoza, 50009, Spain
推荐引用方式 GB/T 7714	Aroca A.,Yruela I.,Gotor C.,et al. Persulfidation of ATG18a regulates autophagy under ER stress in Arabidopsis[J],2021,118(20).
APA	Aroca A.,Yruela I.,Gotor C.,&Bassham D.C..(2021).Persulfidation of ATG18a regulates autophagy under ER stress in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America,118(20).
MLA	Aroca A.,et al."Persulfidation of ATG18a regulates autophagy under ER stress in Arabidopsis".Proceedings of the National Academy of Sciences of the United States of America 118.20(2021).