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Autophagy Volume 18, 2022 - Issue 8
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Autophagic Punctum

Regulation of oxidative stress-induced autophagy by ATG9A ubiquitination

Yi-Ting Wanga Institute of Biological Chemistry Academia Sinica, Taipei, Taiwan;b Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, TaiwanORCID Iconhttps://orcid.org/0000-0001-5996-6932View further author information
ORCID Icon &
Guang-Chao Chena Institute of Biological Chemistry Academia Sinica, Taipei, Taiwan;b Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, TaiwanCorrespondence[email protected]
ORCID Iconhttps://orcid.org/0000-0002-4980-4718View further author information
ORCID Icon
Pages 2008-2010 | Received 15 Mar 2022, Accepted 30 Mar 2022, Published online: 12 Apr 2022

Figures & data

Figure 1. Scheme depicting the mechanisms of ATG9A ubiquitination in oxidative stress induced-autophagy. TNFAIP3/A20 interacts with ATG9A under normal conditions. Upon oxidative stress, TRAF6 mediates ATG9A ubiquitination, thereby enhancing ATG9A-BECN1 interaction, BECN1-PIK3C3/VPS34-UVRAG complex assembly, PIK3C3/VPS34 activation, autophagosome formation, and endocytic trafficking. Ablation of TRAF6 or ATG9A, or expression of TNFAIP3/A20 or ATG9A ubiquitination mutant impairs BECN1-PIK3C3/VPS34-UVRAG complex assembly and PIK3C3/VPS34 activity.

Figure 1. Scheme depicting the mechanisms of ATG9A ubiquitination in oxidative stress induced-autophagy. TNFAIP3/A20 interacts with ATG9A under normal conditions. Upon oxidative stress, TRAF6 mediates ATG9A ubiquitination, thereby enhancing ATG9A-BECN1 interaction, BECN1-PIK3C3/VPS34-UVRAG complex assembly, PIK3C3/VPS34 activation, autophagosome formation, and endocytic trafficking. Ablation of TRAF6 or ATG9A, or expression of TNFAIP3/A20 or ATG9A ubiquitination mutant impairs BECN1-PIK3C3/VPS34-UVRAG complex assembly and PIK3C3/VPS34 activity.

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