Arabidopsis SINAT Proteins Control Autophagy by Mediating Ubiquitylation and Degradation of ATG13.
Hua Qi,Juan Li,Juan Li,Fan-Nv Xia,Jin-Yu Chen,Xue Lei,Mu-Qian Han,Li-Juan Xie,Qing-Ming Zhou,Shi Xiao +9 more
TLDR
It is demonstrated that the SINAT family proteins facilitate ATG13 ubiquitylation and stability and thus regulate autophagy, and under starvation conditions, ATG1 promoted TRAF1a protein stability in vivo, suggesting feedback regulation of autophileagy.Abstract:
In eukaryotes, autophagy maintains cellular homeostasis by recycling cytoplasmic components. The autophagy-related proteins (ATGs) ATG1 and ATG13 form a protein kinase complex that regulates autophagosome formation; however, mechanisms regulating ATG1 and ATG13 remain poorly understood. Here, we show that, under different nutrient conditions, the RING-type E3 ligases SEVEN IN ABSENTIA OF ARABIDOPSIS THALIANA1 (SINAT1), SINAT2, and SINAT6 control ATG1 and ATG13 stability and autophagy dynamics by modulating ATG13 ubiquitylation in Arabidopsis (Arabidopsis thaliana). During prolonged starvation and recovery, ATG1 and ATG13 were degraded through the 26S proteasome pathway. TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR1a (TRAF1a) and TRAF1b interacted in planta with ATG13a and ATG13b and required SINAT1 and SINAT2 to ubiquitylate and degrade ATG13s in vivo. Moreover, lysines K607 and K609 of ATG13a protein contributed to K48-linked ubiquitylation and destabilization, and suppression of autophagy. Under starvation conditions, SINAT6 competitively interacted with ATG13 and induced autophagosome biogenesis. Furthermore, under starvation conditions, ATG1 promoted TRAF1a protein stability in vivo, suggesting feedback regulation of autophagy. Consistent with ATGs functioning in autophagy, the atg1a atg1b atg1c triple knockout mutants exhibited premature leaf senescence, hypersensitivity to nutrient starvation, and reduction in TRAF1a stability. Therefore, these findings demonstrate that SINAT family proteins facilitate ATG13 ubiquitylation and stability and thus regulate autophagy.read more
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Protein Quality Control in Plant Organelles: Current Progress and Future Perspectives.
TL;DR: Recent progress in understanding of protein quality control in the ER, chloroplasts, and mitochondria in plants is summarized, with a focus on the common mechanisms shared in these organelles during protein homeostasis.
Journal ArticleDOI
Autophagy in plants: Physiological roles and post‐translational regulation
Hua Qi,Fan-Nv Xia,Shi Xiao +2 more
TL;DR: An overview of the physiological roles and post-translational regulation of autophagy in plants is provided and it is demonstrated that, similar to non-plant systems, the modulation of core proteins in the plant Autophagy machinery by post- translational modifications is widely involved in the initiation and progression of autophileagy.
Journal ArticleDOI
SINAT E3 Ubiquitin Ligases Mediate FREE1 and VPS23A Degradation to Modulate Abscisic Acid Signaling
Fan-Nv Xia,Baiquan Zeng,Hui-Shan Liu,Hua Qi,Li-Juan Xie,Lu-Jun Yu,Qin-Fang Chen,Jian-Feng Li,Yue-Qin Chen,Liwen Jiang,Shi Xiao +10 more
TL;DR: The SINAT E3 ubiquitin ligases regulate ABA signaling by modulating the protein stability of ESCRT components FREE1 and VPS23A by regulating the stabilities of FYVE DOMAIN PROTEin required for endosomal sorting and VACUOLAR PROTEIN SORTING23A.
Journal ArticleDOI
Interplay between the Ubiquitin Proteasome System and Ubiquitin-Mediated Autophagy in Plants.
TL;DR: The components of the UPS, such as the 26S proteasome, can be degraded via autophagy, and conversely, ATGs can be degradation by the UPS), indicating cross regulation between the two pathways.
Journal ArticleDOI
The F-box E3 ubiquitin ligase BAF1 mediates the degradation of the brassinosteroid-activated transcription factor BES1 through selective autophagy in Arabidopsis.
Ping Wang,Trevor M. Nolan,Natalie M. Clark,Hao Jiang,Christian Montes-Serey,Hongqing Guo,Diane C. Bassham,Justin W. Walley,Yanhai Yin +8 more
TL;DR: In this paper, an F-box family E3 ubiquitin ligase named BRI1-ASSOCIATED F-BOX1 (BAF1) was identified in Arabidopsis thaliana.
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