The thioesterase APT1 is a bidirectional-adjustment redox sensor

Tuo Ji, Lihua Zheng, Jiale Wu, Mei Duan, Qianwen Liu, Peng Liu, Chen Shen, Jinling Liu, Qinyi Ye, Jiangqi Wen, Jiangli Dong () and Tao Wang ()
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Tuo Ji: China Agricultural University
Lihua Zheng: China Agricultural University
Jiale Wu: China Agricultural University
Mei Duan: China Agricultural University
Qianwen Liu: China Agricultural University
Peng Liu: China Agricultural University
Chen Shen: China Agricultural University
Jinling Liu: China Agricultural University
Qinyi Ye: China Agricultural University
Jiangqi Wen: Oklahoma State University
Jiangli Dong: China Agricultural University
Tao Wang: China Agricultural University

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: Abstract The adjustment of cellular redox homeostasis is essential in when responding to environmental perturbations, and the mechanism by which cells distinguish between normal and oxidized states through sensors is also important. In this study, we found that acyl-protein thioesterase 1 (APT1) is a redox sensor. Under normal physiological conditions, APT1 exists as a monomer through S-glutathionylation at C20, C22 and C37, which inhibits its enzymatic activity. Under oxidative conditions, APT1 senses the oxidative signal and is tetramerized, which makes it functional. Tetrameric APT1 depalmitoylates S-acetylated NAC (NACsa), and NACsa relocates to the nucleus, increases the cellular glutathione/oxidized glutathione (GSH/GSSG) ratio through the upregulation of glyoxalase I expression, and resists oxidative stress. When oxidative stress is alleviated, APT1 is found in monomeric form. Here, we describe a mechanism through which APT1 mediates a fine-tuned and balanced intracellular redox system in plant defence responses to biotic and abiotic stresses and provide insights into the design of stress-resistant crops.

Date: 2023
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DOI: 10.1038/s41467-023-38464-y

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