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Abscisic Acid-Triggered Persulfidation of Cysteine Protease ATG4 Mediates Regulation of Autophagy by Sulfide

AuthorsLaureano-Marín, Ana M. CSIC ORCID; Aroca, Ángeles CSIC ORCID; Pérez-Pérez, M. Esther; Yruela Guerrero, Inmaculada CSIC ORCID ; Jurado-Flores, Ana; Moreno, Inmaculada CSIC ORCID; Crespo, José L. CSIC ORCID ; Romero, Luis C. CSIC ORCID CVN ; Gotor, Cecilia CSIC ORCID
Issue DateOct-2020
PublisherAmerican Society of Plant Biologists
CitationLaureano-Marín AM , Aroca A, Pérez-Pérez ME, Yruela I, Jurado-Flores A, Moreno I, Crespo JL, Romero LC, Gotor C. Abscisic Acid-Triggered Persulfidation of Cysteine Protease ATG4 Mediates Regulation of Autophagy by Sulfide. Plant Cell 32 (12): 3902-3920 (2020)
AbstractHydrogen sulfide is a signaling molecule that regulates essential processes in plants, such as autophagy. In Arabidopsis (Arabidopsis thaliana), hydrogen sulfide negatively regulates autophagy independently of reactive oxygen species via an unknown mechanism. Comparative and quantitative proteomic analysis was used to detect abscisic acid-triggered persulfidation that reveals a main role in the control of autophagy mediated by the autophagy-related (ATG) Cys protease AtATG4a. This protease undergoes specific persulfidation of Cys170 that is a part of the characteristic catalytic Cys-His-Asp triad of Cys proteases. Regulation of the ATG4 activity by persulfidation was tested in a heterologous assay using the Chlamydomonas reinhardtii CrATG8 protein as a substrate. Sulfide significantly and reversibly inactivates AtATG4a. The biological significance of the reversible inhibition of the ATG4 by sulfide is supported by the results obtained in Arabidopsis leaves under basal and autophagy-activating conditions. A significant increase in the overall ATG4 proteolytic activity in Arabidopsis was detected under nitrogen starvation and osmotic stress and can be inhibited by sulfide. Therefore, the data strongly suggest that the negative regulation of autophagy by sulfide is mediated by specific persulfidation of the ATG4 protease.
Description48 Pags.- 10 Figs. The definitive version, with suppl mat., is available at: http://www.plantcell.org/
Publisher version (URL)https://doi.org/10.1105/tpc.20.00766
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