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dc.contributor.authorLaureano-Marín, Ana M.es_ES
dc.contributor.authorAroca, Ángeleses_ES
dc.contributor.authorPérez-Pérez, M. Estheres_ES
dc.contributor.authorYruela Guerrero, Inmaculadaes_ES
dc.contributor.authorJurado-Flores, Anaes_ES
dc.contributor.authorMoreno, Inmaculadaes_ES
dc.contributor.authorCrespo, José L.es_ES
dc.contributor.authorRomero, Luis C.es_ES
dc.contributor.authorGotor, Ceciliaes_ES
dc.identifier.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)es_ES
dc.description48 Pags.- 10 Figs. The definitive version, with suppl mat., is available at: http://www.plantcell.org/es_ES
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_ES
dc.description.sponsorshipThis work was supported in part by the European Regional Development Fund through the Ministerio de Economía y Competitividad and the Agencia Estatal de Investigación (grant nos. BFU2015-68216-P and PGC2018-099048- B-I00 to J.L.C.; grant nos. BIO2015-74432-JIN and PID2019- 110080GB-I00 to M.E.P.-P.; grant nos. BIO2016-76633-P and PID2019- 109785GB-I00; and Junta de Andalucía grant no. P18-RT-3154 to C.G.)., the Marie Skłodowska-Curie Grant Agreement (grant no. 834120 to Á.A.), Government of Aragón-FEDER (grant no. E35_17R to I.Y.), and the Ministerio de Economia y Competitividad through the program of “Formación de Personal Investigador” (to A.M.L.-M. and A.J.-F.).es_ES
dc.publisherAmerican Society of Plant Biologistses_ES
dc.relationMICIU/ICTI2017-2020/PGC2018-099048- B-I00es_ES
dc.relationMICIU/ICTI2017-2020/PID2019- 110080GB-I00es_ES
dc.relationMICIU/ICTI2017-2020/PID2019- 109785GB-I00es_ES
dc.titleAbscisic Acid-Triggered Persulfidation of Cysteine Protease ATG4 Mediates Regulation of Autophagy by Sulfidees_ES
dc.description.peerreviewedPeer reviewedes_ES
dc.contributor.funderEuropean Commissiones_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.contributor.funderAgencia Estatal de Investigación (España)es_ES
dc.contributor.funderJunta de Andalucíaes_ES
dc.contributor.funderGobierno de Aragónes_ES
oprm.item.hasRevisionno ko 0 false*
dc.contributor.orcidYruela Guerrero, Inmaculada [0000-0003-3608-4720]es_ES
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