Degradation of the antiviral component ARGONAUTE1 by the autophagy pathway

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DERRIEN, Benoît, Nicolas BAUMBERGER, Mikhail SCHEPETILNIKOV, Corrado VIOTTI, Julia DE CILLIA, Veronique ZIEGLER-GRAFF, Erika ISONO, Karin SCHUMACHER, Pascal GENSCHIK, 2012. Degradation of the antiviral component ARGONAUTE1 by the autophagy pathway. In: Proceedings of the National Academy of Sciences of the United States of America (PNAS). 109(39), pp. 15942-15946. ISSN 0027-8424. eISSN 1091-6490

@article{Derrien2012-09-25Degra-38629, title={Degradation of the antiviral component ARGONAUTE1 by the autophagy pathway}, year={2012}, doi={10.1073/pnas.1209487109}, number={39}, volume={109}, issn={0027-8424}, journal={Proceedings of the National Academy of Sciences of the United States of America (PNAS)}, pages={15942--15946}, author={Derrien, Benoît and Baumberger, Nicolas and Schepetilnikov, Mikhail and Viotti, Corrado and De Cillia, Julia and Ziegler-Graff, Veronique and Isono, Erika and Schumacher, Karin and Genschik, Pascal} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/38629"> <dc:contributor>Schepetilnikov, Mikhail</dc:contributor> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38629"/> <dc:contributor>Isono, Erika</dc:contributor> <dc:contributor>Derrien, Benoît</dc:contributor> <dc:creator>Viotti, Corrado</dc:creator> <dcterms:abstract xml:lang="eng">Posttranscriptional gene silencing (PTGS) mediated by siRNAs is an evolutionarily conserved antiviral defense mechanism in higher plants and invertebrates. In this mechanism, viral-derived siRNAs are incorporated into the RNA-induced silencing complex (RISC) to guide degradation of the corresponding viral RNAs. In Arabidopsis, a key component of RISC is ARGONAUTE1 (AGO1), which not only binds to siRNAs but also carries the RNA slicer activity. At present little is known about posttranslational mechanisms regulating AGO1 turnover. Here we report that the viral suppressor of RNA silencing protein P0 triggers AGO1 degradation by the autophagy pathway. Using a P0-inducible transgenic line, we observed that AGO1 degradation is blocked by inhibition of autophagy. The engineering of a functional AGO1 fluorescent reporter protein further indicated that AGO1 colocalizes with autophagy-related (ATG) protein 8a (ATG8a) positive bodies when degradation is impaired. Moreover, this pathway also degrades AGO1 in a nonviral context, especially when the production of miRNAs is impaired. Our results demonstrate that a selective process such as ubiquitylation can lead to the degradation of a key regulatory protein such as AGO1 by a degradation process generally believed to be unspecific. We anticipate that this mechanism will not only lead to degradation of AGO1 but also of its associated proteins and eventually small RNAs.</dcterms:abstract> <dc:contributor>Ziegler-Graff, Veronique</dc:contributor> <dc:creator>Isono, Erika</dc:creator> <dc:creator>Derrien, Benoît</dc:creator> <dcterms:title>Degradation of the antiviral component ARGONAUTE1 by the autophagy pathway</dcterms:title> <dc:contributor>Genschik, Pascal</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-27T07:37:36Z</dcterms:available> <dc:creator>Baumberger, Nicolas</dc:creator> <dc:contributor>Baumberger, Nicolas</dc:contributor> <dc:creator>De Cillia, Julia</dc:creator> <dc:creator>Schumacher, Karin</dc:creator> <dc:language>eng</dc:language> <dc:creator>Schepetilnikov, Mikhail</dc:creator> <dc:creator>Ziegler-Graff, Veronique</dc:creator> <dc:creator>Genschik, Pascal</dc:creator> <dc:contributor>Schumacher, Karin</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-27T07:37:36Z</dc:date> <dcterms:issued>2012-09-25</dcterms:issued> <dc:contributor>Viotti, Corrado</dc:contributor> <dc:contributor>De Cillia, Julia</dc:contributor> </rdf:Description> </rdf:RDF>

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