The viral F-box protein P0 induces an ER-derived autophagy degradation pathway for the clearance of membrane-bound AGO1

التفاصيل البيبلوغرافية
العنوان: The viral F-box protein P0 induces an ER-derived autophagy degradation pathway for the clearance of membrane-bound AGO1
المؤلفون: Gad Galili, Julia De Cilia, Marieke Dubois, Maxime Lecorbeiller, Benoît Derrien, Hervé Vaucheret, Véronique Ziegler-Graff, Pascal Genschik, Esther Izquierdo, Esther Lechner, Simon Michaeli, Jian Wu, Thibaut Hacquard, Nathalie Bouteiller, Corrado Viotti, Marion Clavel
المساهمون: Unité Propre de Recherche 2357, Institution de Biologie Moléculaire des Plantes, Department of Plant and Environmental Sciences [Copenhagen], Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), VIBUGent Center for Plant Systems Biology, NA SCRIPT, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie moléculaire des plantes (IBMP), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Weizmann Institute of Science [Rehovot, Israël], Universiteit Gent = Ghent University [Belgium] (UGENT), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)
المصدر: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (45), pp.22872-22883. ⟨10.1073/pnas.1912222116⟩
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
بيانات النشر: HAL CCSD, 2019.
سنة النشر: 2019
مصطلحات موضوعية: 0106 biological sciences, autophagy, [SDV]Life Sciences [q-bio], ATG5, BIOGENESIS, INHIBITION, Arabidopsis, Plant Biology, Vacuole, Endoplasmic Reticulum, 01 natural sciences, F-box protein, MECHANISMS, SMALL RNAS, 03 medical and health sciences, Viral Proteins, ARGONAUTE COMPLEXES, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, TRAFFICKING, SELECTIVE AUTOPHAGY, 030304 developmental biology, Plant Proteins, 0303 health sciences, Multidisciplinary, biology, SILENCING SUPPRESSOR, Chemistry, Endoplasmic reticulum, Autophagy, fungi, 26S PROTEASOME, Membrane Proteins, Biology and Life Sciences, Biological Sciences, Cell biology, RNA silencing, Proteasome, Argonaute Proteins, Proteolysis, Vacuoles, biology.protein, Biogenesis, 010606 plant biology & botany
الوصف: Significance The viral suppressor of RNA silencing P0 is known to target plant antiviral ARGONAUTE (AGO) proteins for degradation via an autophagy-related process. Here we utilized P0 to gain insight into the cellular degradation dynamics of AGO1, the major plant effector of RNA silencing. We revealed that P0 targets endoplasmic reticulum (ER)-associated AGO1 by inducing the formation of ER-related bodies that are delivered to the vacuole with both P0 and AGO1 as cargos. This process involves ATG8-interacting proteins 1 and 2 (ATI1 and ATI2) that interact with AGO1 and negatively regulate its transgene-silencing activity. Together, our results reveal a layer of ER-bound AGO1 posttranslational regulation that is manipulated by P0 to subvert plant antiviral defense.
RNA silencing is a major antiviral defense mechanism in plants and invertebrates. Plant ARGONAUTE1 (AGO1) is pivotal in RNA silencing, and hence is a major target for counteracting viral suppressors of RNA-silencing proteins (VSRs). P0 from Turnip yellows virus (TuYV) is a VSR that was previously shown to trigger AGO1 degradation via an autophagy-like process. However, the identity of host proteins involved and the cellular site at which AGO1 and P0 interact were unknown. Here we report that P0 and AGO1 associate on the endoplasmic reticulum (ER), resulting in their loading into ER-associated vesicles that are mobilized to the vacuole in an ATG5- and ATG7-dependent manner. We further identified ATG8-Interacting proteins 1 and 2 (ATI1 and ATI2) as proteins that associate with P0 and interact with AGO1 on the ER up to the vacuole. Notably, ATI1 and ATI2 belong to an endogenous degradation pathway of ER-associated AGO1 that is significantly induced following P0 expression. Accordingly, ATI1 and ATI2 deficiency causes a significant increase in posttranscriptional gene silencing (PTGS) activity. Collectively, we identify ATI1 and ATI2 as components of an ER-associated AGO1 turnover and proper PTGS maintenance and further show how the VSR P0 manipulates this pathway.
وصف الملف: application/pdf
اللغة: English
تدمد: 0027-8424
1091-6490
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d50d07cd03b74ec44ef1d909fc95b31Test
https://hal.archives-ouvertes.fr/hal-02349952Test
حقوق: OPEN
رقم الانضمام: edsair.doi.dedup.....6d50d07cd03b74ec44ef1d909fc95b31
قاعدة البيانات: OpenAIRE