期刊
PLANT CELL
卷 34, 期 4, 页码 1354-1374出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/plcell/koac014
关键词
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资金
- Japan Society for the Promotion of Science (JSPS) [17J06430]
- MEXT
- Knut and Alice Wallenberg Foundation
- MEXT KAKENHI [JP18H05275, JP15H01167, JP21H02150, JP20K05949, JP21H05644, JP16H06280]
- JST (CREST) [JPMJCR20E5]
- Sumitomo Foundation
- NOASTEC foundation
- Hokkaido University
- Grants-in-Aid for Scientific Research [17J06430] Funding Source: KAKEN
This study identified the interaction between the trans-Golgi network/early endosome localized SNARE protein SYP61 and the transmembrane ubiquitin ligase ATL31 in Arabidopsis. It also revealed the critical role of SYP61 in plant responses to nutrient stress, as well as its ubiquitination under low carbon/high nitrogen conditions. These findings provide important insights into the ubiquitin signaling and membrane trafficking machinery in plants.
The TGN/EE SNARE protein SYP61 plays a critical role in plant carbon/nitrogen nutrient stress responses and is ubiquitinated in response to low carbon/high nitrogen conditions. Ubiquitination is a post-translational modification involving the reversible attachment of the small protein ubiquitin to a target protein. Ubiquitination is involved in numerous cellular processes, including the membrane trafficking of cargo proteins. However, the ubiquitination of the trafficking machinery components and their involvement in environmental responses are not well understood. Here, we report that the Arabidopsis thalianatrans-Golgi network/early endosome localized SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein SYP61 interacts with the transmembrane ubiquitin ligase ATL31, a key regulator of resistance to disrupted carbon (C)/nitrogen/(N)-nutrient conditions. SYP61 is a key component of membrane trafficking in Arabidopsis. The subcellular localization of ATL31 was disrupted in knockdown mutants of SYP61, and the insensitivity of ATL31-overexpressing plants to high C/low N-stress was repressed in these mutants, suggesting that SYP61 and ATL31 cooperatively function in plant responses to nutrient stress. SYP61 is ubiquitinated in plants, and its ubiquitination level is upregulated under low C/high N-nutrient conditions. These findings provide important insights into the ubiquitin signaling and membrane trafficking machinery in plants.
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