Persulfidation of ATG18a regulates autophagy under ER stress inArabidopsis

• DOI: 10.1073/pnas.2023604118
• Publication Date: 2021-05-11T19:45:35Z
• Authors: Angeles Aroca; Inmaculada Yruela; Cecilia Gotor; Diane C. Bassham
• Keywords: Models, Molecular; autophagy; persulfidation; Protein Conformation; hydrogen sulfide; Arabidopsis; Autophagy-Related Proteins; Sulfides; 03 medical and health sciences; Gene Expression Regulation, Plant; Autophagy; Protein Interaction Domains and Motifs; Cysteine; Hydrogen Sulfide; Phospholipids; 0303 health sciences; Binding Sites; Arabidopsis Proteins; Autophagosomes; ATG18a; Endoplasmic Reticulum Stress; Persulfidation; persulfidation.; ER stress; Protein Processing, Post-Translational; Protein Binding; Signal Transduction

Significance Endoplasmic reticulum (ER) stress is a condition triggered by adverse environmental conditions, which in plants include extreme heat, pathogen infection, and drought. These stresses can have devastating effect on agricultural productivity, the appropriate responses of to are therefore critical. Autophagy macromolecular degradation pathway that activated response stress, including ER but mechanism it regulated still unclear. Here, we describe modification, persulfidation, key autophagy protein ATG18a affects its binding membranes controls activity. This tight regulation allows control tradeoff between growth tolerance.