Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death

Abstract Cell death, autophagy and endosomal sorting contribute to many physiological, developmental and immunological processes in plants. They are mechanistically interconnected and interdependent, but the molecular basis of their mutual regulation has only begun to emerge in plants. Here, we desc...

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Autores principales: Arpaporn Sutipatanasomboon, Stefanie Herberth, Ellen G. Alwood, Heidrun Häweker, Britta Müller, Mojgan Shahriari, Anke Y. Zienert, Birger Marin, Silke Robatzek, Gerrit J. K. Praefcke, Kathryn R. Ayscough, Martin Hülskamp, Swen Schellmann
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Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/6992c0ebf240486fa7c47bdd6f4fefa6
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spelling oai:doaj.org-article:6992c0ebf240486fa7c47bdd6f4fefa62021-12-02T16:08:09ZDisruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death10.1038/s41598-017-08577-82045-2322https://doaj.org/article/6992c0ebf240486fa7c47bdd6f4fefa62017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08577-8https://doaj.org/toc/2045-2322Abstract Cell death, autophagy and endosomal sorting contribute to many physiological, developmental and immunological processes in plants. They are mechanistically interconnected and interdependent, but the molecular basis of their mutual regulation has only begun to emerge in plants. Here, we describe the identification and molecular characterization of CELL DEATH RELATED ENDOSOMAL FYVE/SYLF PROTEIN 1 (CFS1). The CFS1 protein interacts with the ENDOSOMAL SORTING COMPLEX REQUIRED FOR TRANSPORT I (ESCRT-I) component ELCH (ELC) and is localized at ESCRT-I-positive late endosomes likely through its PI3P and actin binding SH3YL1 Ysc84/Lsb4p Lsb3p plant FYVE (SYLF) domain. Mutant alleles of cfs1 exhibit auto-immune phenotypes including spontaneous lesions that show characteristics of hypersensitive response (HR). Autoimmunity in cfs1 is dependent on ENHANCED DISEASE SUSCEPTIBILITY 1 (EDS1)-mediated effector-triggered immunity (ETI) but independent from salicylic acid. Additionally, cfs1 mutants accumulate the autophagy markers ATG8 and NBR1 independently from EDS1. We hypothesize that CFS1 acts at the intersection of autophagosomes and endosomes and contributes to cellular homeostasis by mediating autophagosome turnover.Arpaporn SutipatanasomboonStefanie HerberthEllen G. AlwoodHeidrun HäwekerBritta MüllerMojgan ShahriariAnke Y. ZienertBirger MarinSilke RobatzekGerrit J. K. PraefckeKathryn R. AyscoughMartin HülskampSwen SchellmannNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Arpaporn Sutipatanasomboon
Stefanie Herberth
Ellen G. Alwood
Heidrun Häweker
Britta Müller
Mojgan Shahriari
Anke Y. Zienert
Birger Marin
Silke Robatzek
Gerrit J. K. Praefcke
Kathryn R. Ayscough
Martin Hülskamp
Swen Schellmann
Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death
description Abstract Cell death, autophagy and endosomal sorting contribute to many physiological, developmental and immunological processes in plants. They are mechanistically interconnected and interdependent, but the molecular basis of their mutual regulation has only begun to emerge in plants. Here, we describe the identification and molecular characterization of CELL DEATH RELATED ENDOSOMAL FYVE/SYLF PROTEIN 1 (CFS1). The CFS1 protein interacts with the ENDOSOMAL SORTING COMPLEX REQUIRED FOR TRANSPORT I (ESCRT-I) component ELCH (ELC) and is localized at ESCRT-I-positive late endosomes likely through its PI3P and actin binding SH3YL1 Ysc84/Lsb4p Lsb3p plant FYVE (SYLF) domain. Mutant alleles of cfs1 exhibit auto-immune phenotypes including spontaneous lesions that show characteristics of hypersensitive response (HR). Autoimmunity in cfs1 is dependent on ENHANCED DISEASE SUSCEPTIBILITY 1 (EDS1)-mediated effector-triggered immunity (ETI) but independent from salicylic acid. Additionally, cfs1 mutants accumulate the autophagy markers ATG8 and NBR1 independently from EDS1. We hypothesize that CFS1 acts at the intersection of autophagosomes and endosomes and contributes to cellular homeostasis by mediating autophagosome turnover.
format article
author Arpaporn Sutipatanasomboon
Stefanie Herberth
Ellen G. Alwood
Heidrun Häweker
Britta Müller
Mojgan Shahriari
Anke Y. Zienert
Birger Marin
Silke Robatzek
Gerrit J. K. Praefcke
Kathryn R. Ayscough
Martin Hülskamp
Swen Schellmann
author_facet Arpaporn Sutipatanasomboon
Stefanie Herberth
Ellen G. Alwood
Heidrun Häweker
Britta Müller
Mojgan Shahriari
Anke Y. Zienert
Birger Marin
Silke Robatzek
Gerrit J. K. Praefcke
Kathryn R. Ayscough
Martin Hülskamp
Swen Schellmann
author_sort Arpaporn Sutipatanasomboon
title Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death
title_short Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death
title_full Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death
title_fullStr Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death
title_full_unstemmed Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death
title_sort disruption of the plant-specific cfs1 gene impairs autophagosome turnover and triggers eds1-dependent cell death
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/6992c0ebf240486fa7c47bdd6f4fefa6
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