The plant unique ESCRT component FREE1 regulates autophagosome closure

Yonglun Zeng, Baiying Li, Shuxian Huang, Hongbo Li, Wenhan Cao, Yixuan Chen, Guoyong Liu, Zhenping Li, Chao Yang, Lei Feng, Jiayang Gao, Sze Wan Lo, Jierui Zhao, Jinbo Shen, Yan Guo, Caiji Gao, Yasin Dagdas and Liwen Jiang ()
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Yonglun Zeng: The Chinese University of Hong Kong
Baiying Li: The Chinese University of Hong Kong
Shuxian Huang: The Chinese University of Hong Kong
Hongbo Li: South China Normal University
Wenhan Cao: The Chinese University of Hong Kong
Yixuan Chen: The Chinese University of Hong Kong
Guoyong Liu: China Agricultural University
Zhenping Li: The Chinese University of Hong Kong
Chao Yang: South China Normal University
Lei Feng: The Chinese University of Hong Kong
Jiayang Gao: The Chinese University of Hong Kong
Sze Wan Lo: The Chinese University of Hong Kong
Jierui Zhao: Doctoral School of the University at Vienna and Medical University of Vienna
Jinbo Shen: Zhejiang A&F University
Yan Guo: China Agricultural University
Caiji Gao: South China Normal University
Yasin Dagdas: Austrian Academy of Sciences, Vienna BioCenter
Liwen Jiang: The Chinese University of Hong Kong

Nature Communications, 2023, vol. 14, issue 1, 1-17

Abstract: Abstract The energy sensor AMP-activated protein kinase (AMPK) can activate autophagy when cellular energy production becomes compromised. However, the degree to which nutrient sensing impinges on the autophagosome closure remains unknown. Here, we provide the mechanism underlying a plant unique protein FREE1, upon autophagy-induced SnRK1α1-mediated phosphorylation, functions as a linkage between ATG conjugation system and ESCRT machinery to regulate the autophagosome closure upon nutrient deprivation. Using high-resolution microscopy, 3D-electron tomography, and protease protection assay, we showed that unclosed autophagosomes accumulated in free1 mutants. Proteomic, cellular and biochemical analysis revealed the mechanistic connection between FREE1 and the ATG conjugation system/ESCRT-III complex in regulating autophagosome closure. Mass spectrometry analysis showed that the evolutionary conserved plant energy sensor SnRK1α1 phosphorylates FREE1 and recruits it to the autophagosomes to promote closure. Mutagenesis of the phosphorylation site on FREE1 caused the autophagosome closure failure. Our findings unveil how cellular energy sensing pathways regulate autophagosome closure to maintain cellular homeostasis.

Date: 2023
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DOI: 10.1038/s41467-023-37185-6

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