The TGN/EE SNARE protein SYP61 and the ubiquitin ligase ATL31 cooperatively regulate plant responses to carbon/nitrogen conditions in Arabidopsis

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...

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Published in:	The Plant cell Vol. 34; no. 4; pp. 1354 - 1374
Main Authors:	Hasegawa, Yoko, Huarancca Reyes, Thais, Uemura, Tomohiro, Baral, Anirban, Fujimaki, Akari, Luo, Yongming, Morita, Yoshie, Saeki, Yasushi, Maekawa, Shugo, Yasuda, Shigetaka, Mukuta, Koki, Fukao, Yoichiro, Tanaka, Keiji, Nakano, Akihiko, Takagi, Junpei, Bhalerao, Rishikesh P, Yamaguchi, Junji, Sato, Takeo
Format:	Journal Article
Language:	English
Published:	England Oxford University Press 29-03-2022
Subjects:	Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Carbon - metabolism Cell Biology Cellbiologi Nitrogen - metabolism SNARE Proteins - metabolism trans-Golgi Network - metabolism Ubiquitin - metabolism Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism
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Summary:	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 thaliana trans-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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Senior author. These authors contributed equally (Y.H., T.H.R.). Present address: Department of Life Science, College of Science, Rikkyo University, Toshima-ku, Tokyo 171-8501, Japan. Present address: Graduate School of Science and Technology, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan. Present address: Department of Agriculture, Food and Environment, University of Pisa, Pisa 56124, Italy.
ISSN:	1040-4651 1532-298X 1532-298X
DOI:	10.1093/plcell/koac014