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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Main Authors: 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
Format: Article
Language:English
Published: Nature Publishing Group 2017-08-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-017-08577-8
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spelling doaj-6992c0ebf240486fa7c47bdd6f4fefa62020-12-08T02:45:06ZengNature Publishing GroupScientific Reports2045-23222017-08-017111410.1038/s41598-017-08577-8Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell deathArpaporn Sutipatanasomboon0Stefanie Herberth1Ellen G. Alwood2Heidrun Häweker3Britta Müller4Mojgan Shahriari5Anke Y. Zienert6Birger Marin7Silke Robatzek8Gerrit J. K. Praefcke9Kathryn R. Ayscough10Martin Hülskamp11Swen Schellmann12Botanik III, Biocenter, Universtiy of CologneBotanik III, Biocenter, Universtiy of CologneDepartment of Biomedical Science, The University of SheffieldThe Sainsbury Laboratory, Norwich Research ParkBotanik III, Biocenter, Universtiy of CologneBotanik III, Biocenter, Universtiy of CologneInstitut für Genetik, Universtiy of CologneBotanik I, Biocenter, Universtiy of CologneThe Sainsbury Laboratory, Norwich Research ParkInstitut für Genetik, Universtiy of CologneDepartment of Biomedical Science, The University of SheffieldBotanik III, Biocenter, Universtiy of CologneBotanik III, Biocenter, Universtiy of CologneAbstract 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.https://doi.org/10.1038/s41598-017-08577-8
collection DOAJ
language English
format Article
sources DOAJ
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
spellingShingle 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
Scientific Reports
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 Publishing Group
series Scientific Reports
issn 2045-2322
publishDate 2017-08-01
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.
url https://doi.org/10.1038/s41598-017-08577-8
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