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dc.creatorLaureano Marín, Ana Maríaes
dc.creatorAroca Aguilar, Ángeleses
dc.creatorPérez Pérez, Maria Estheres
dc.creatorYruela Guerrero, Inmaculadaes
dc.creatorJurado Flores, Anaes
dc.creatorMoreno González, María Inmaculadaes
dc.creatorCrespo González, José Luises
dc.creatorRomero González, Luis Carloses
dc.creatorGotor Martínez, Ceciliaes
dc.date.accessioned2021-10-04T15:33:08Z
dc.date.available2021-10-04T15:33:08Z
dc.date.issued2020
dc.identifier.citationLaureano Marín, A.M., Aroca Aguilar, Á., Pérez Pérez, M.E., Yruela Guerrero, I., Jurado Flores, A., Moreno González, M.I.,...,Gotor Martínez, C. (2020). Abscisic acid-triggered persulfidation of the cys protease ATG4 mediates regulation of autophagy by sulfide. Plant Cell, 32 (12), 3902-3920.
dc.identifier.issn1040-4651es
dc.identifier.issn1532-298Xes
dc.identifier.urihttps://hdl.handle.net/11441/126444
dc.description.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.es
dc.description.sponsorshipMinisterio de Economía y Competitividad BFU2015-68216-P, PGC2018-099048- B-I00, BIO2015-74432-JIN, PID2019- 110080GB-I00, BIO2016-76633-P, PID2019- 109785GB-I00es
dc.description.sponsorshipJunta de Andalucía P18-RT-3154es
dc.description.sponsorshipMarie Skłodowska-Curie 834120es
dc.description.sponsorshipGobierno de Aragón E35_17Res
dc.formatapplication/pdfes
dc.format.extent19 p.es
dc.language.isoenges
dc.publisherAmerican Society of Plant Biologistses
dc.relation.ispartofPlant Cell, 32 (12), 3902-3920.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleAbscisic acid-triggered persulfidation of the cys protease ATG4 mediates regulation of autophagy by sulfidees
dc.typeinfo:eu-repo/semantics/articlees
dcterms.identifierhttps://ror.org/03yxnpp24
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Bioquímica y Biología Moleculares
dc.relation.projectIDBFU2015-68216-Pes
dc.relation.projectIDPGC2018-099048- B-I00es
dc.relation.projectIDBIO2015-74432-JINes
dc.relation.projectIDPID2019- 110080GB-I00es
dc.relation.projectIDBIO2016-76633-Pes
dc.relation.projectIDPID2019- 109785GB-I00es
dc.relation.projectIDP18-RT-3154es
dc.relation.projectID834120es
dc.relation.projectIDE35_17Res
dc.relation.publisherversionhttps://doi.org/10.1105/tpc.20.00766es
dc.identifier.doi10.1105/tpc.20.00766es
dc.journaltitlePlant Celles
dc.publication.volumen32es
dc.publication.issue12es
dc.publication.initialPage3902es
dc.publication.endPage3920es

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