Ufmylation reconciles salt stress-induced unfolded protein responses via ER-phagy in Arabidopsis

Author:

Li Baiying1ORCID,Niu Fangfang1ORCID,Zeng Yonglun1,Tse Man Kei1,Deng Cesi1,Hong Liu1ORCID,Gao Shengyu1ORCID,Lo Sze Wan1ORCID,Cao Wenhan1ORCID,Huang Shuxian1,Dagdas Yasin2ORCID,Jiang Liwen134

Affiliation:

1. School of Life Sciences, Centre for Cell & Developmental Biology and State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, Hong Kong, China

2. Gregor Mendel Institute of Molecular Plant Biology, Austrian Academy of Sciences, Vienna BioCenter 1030 Vienna, Austria

3. Institute of Plant Molecular Biology and Agricultural Biotechnology, The Chinese University of Hong Kong, Shatin, Hong Kong, China

4. The Chinese University of Hong Kong Shenzhen Research Institute, Shenzhen 518057, China

Abstract

In plants, the endomembrane system is tightly regulated in response to environmental stresses for maintaining cellular homeostasis. Autophagosomes, the double membrane organelles forming upon nutrient deprivation or stress induction, degrade bulky cytosolic materials for nutrient turnover. Though abiotic stresses have been reported to induce plant autophagy, few receptors or regulators for selective autophagy have been characterized for specific stresses. Here, we have applied immunoprecipitation followed by tandem mass spectrometry using the autophagosome marker protein ATG8 as bait and have identified the E3 ligase of the ufmylation system Ufl1 as a bona fide ATG8 interactor under salt stress. Notably, core components in the ufmylation cascade, Ufl1 and Ufm1, interact with the autophagy kinase complexes proteins ATG1 and ATG6. Cellular and genetic analysis showed that Ufl1 is important for endoplasmic reticulum (ER)-phagy under persisting salt stress. Loss-of-function mutants of Ufl1 display a salt stress hypersensitive phenotype and abnormal ER morphology. Prolonged ER stress responses are detected in ufl1 mutants that phenocopy the autophagy dysfunction atg5 mutants. Consistently, expression of ufmylation cascade components is up-regulated by salt stress. Taken together, our study demonstrates the role of ufmylation in regulating ER homeostasis under salt stress through ER-phagy.

Funder

National Natural Science Foundation of China

Research Grants Council, University Grants Committee

Chinese University of Hong Kong

CAS-Croucher Funding Scheme for Joint Laboratories

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

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