ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses

The conjugation of ATG8 (autophagy-related 8) proteins to the lipid phosphatidylethanolamine (PE) is the result of the coordinated and highly regulated action of several ATG core proteins, including ATG4 proteases and the E1 (ATG7)- and E2 (ATG3)- activating enzymes. Although it has been stablished...

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Bibliographic Details
Published in:Autophagy reports 2024-12, Vol.3 (1)
Main Authors: Mallén-Ponce, Manuel J., Pérez-Pérez, María Esther
Format: Article
Language:English
Subjects:
ATG3
ATG8 lipidation
Chlamydomonas
redox
ROS
stress
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Summary:The conjugation of ATG8 (autophagy-related 8) proteins to the lipid phosphatidylethanolamine (PE) is the result of the coordinated and highly regulated action of several ATG core proteins, including ATG4 proteases and the E1 (ATG7)- and E2 (ATG3)- activating enzymes. Although it has been stablished that ROS signaling plays an important role in autophagy activation, the molecular mechanisms underlying the redox control of ATG proteins remain largely unclear. We have recently shown that ATG3 activity in Chlamydomonas reinhardtii is subjected to reversible redox regulation to ensure ATG8 lipidation and autophagy progression under ROS-linked stress conditions.Abbreviations: ATG, Autophagy-related; Cys, Cysteine; DTTred, Reduced Dithiothreitol; MM(PEG24), Methyl Polyethylene Glycol Maleimide; NEM: N-ethylmaleimide; PE, Phosphatidylethanolamine; ROS, Reactive Oxygen Species; TOR, Target Of Rapamycin; Trx, Thioredoxin; WT, Wild Type
ISSN:2769-4127
2769-4127
DOI:10.1080/27694127.2023.2300622