The TGN/EE SNARE protein SYP61 and the ubiquitin ligase ATL31 cooperatively regulate plant responses to carbon/nitrogen conditions in Arabidopsis. Hasegawa, Y., Huarancca Reyes, T., Uemura, T., Baral, A., Fujimaki, A., Luo, Y., Morita, Y., Saeki, Y., Maekawa, S., Yasuda, S., Mukuta, K., Fukao, Y., Tanaka, K., Nakano, A., Takagi, J., Bhalerao, R. P, Yamaguchi, J., & Sato, T. The Plant Cell, 34(4):1354–1374, April, 2022. ![The TGN/EE SNARE protein SYP61 and the ubiquitin ligase ATL31 cooperatively regulate plant responses to carbon/nitrogen conditions in Arabidopsis [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{hasegawa_tgnee_2022,
title = {The {TGN}/{EE} {SNARE} protein {SYP61} and the ubiquitin ligase {ATL31} cooperatively regulate plant responses to carbon/nitrogen conditions in {Arabidopsis}},
volume = {34},
issn = {1040-4651},
url = {https://doi.org/10.1093/plcell/koac014},
doi = {10.1093/plcell/koac014},
abstract = {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.},
number = {4},
urldate = {2022-04-08},
journal = {The Plant Cell},
author = {Hasegawa, Yoko and Huarancca Reyes, Thais and Uemura, Tomohiro and Baral, Anirban and Fujimaki, Akari and Luo, Yongming and Morita, Yoshie and Saeki, Yasushi and Maekawa, Shugo and Yasuda, Shigetaka and Mukuta, Koki and Fukao, Yoichiro and Tanaka, Keiji and Nakano, Akihiko and Takagi, Junpei and Bhalerao, Rishikesh P and Yamaguchi, Junji and Sato, Takeo},
month = apr,
year = {2022},
pages = {1354--1374},
}
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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.","number":"4","urldate":"2022-04-08","journal":"The Plant Cell","author":[{"propositions":[],"lastnames":["Hasegawa"],"firstnames":["Yoko"],"suffixes":[]},{"propositions":[],"lastnames":["Huarancca","Reyes"],"firstnames":["Thais"],"suffixes":[]},{"propositions":[],"lastnames":["Uemura"],"firstnames":["Tomohiro"],"suffixes":[]},{"propositions":[],"lastnames":["Baral"],"firstnames":["Anirban"],"suffixes":[]},{"propositions":[],"lastnames":["Fujimaki"],"firstnames":["Akari"],"suffixes":[]},{"propositions":[],"lastnames":["Luo"],"firstnames":["Yongming"],"suffixes":[]},{"propositions":[],"lastnames":["Morita"],"firstnames":["Yoshie"],"suffixes":[]},{"propositions":[],"lastnames":["Saeki"],"firstnames":["Yasushi"],"suffixes":[]},{"propositions":[],"lastnames":["Maekawa"],"firstnames":["Shugo"],"suffixes":[]},{"propositions":[],"lastnames":["Yasuda"],"firstnames":["Shigetaka"],"suffixes":[]},{"propositions":[],"lastnames":["Mukuta"],"firstnames":["Koki"],"suffixes":[]},{"propositions":[],"lastnames":["Fukao"],"firstnames":["Yoichiro"],"suffixes":[]},{"propositions":[],"lastnames":["Tanaka"],"firstnames":["Keiji"],"suffixes":[]},{"propositions":[],"lastnames":["Nakano"],"firstnames":["Akihiko"],"suffixes":[]},{"propositions":[],"lastnames":["Takagi"],"firstnames":["Junpei"],"suffixes":[]},{"propositions":[],"lastnames":["Bhalerao"],"firstnames":["Rishikesh","P"],"suffixes":[]},{"propositions":[],"lastnames":["Yamaguchi"],"firstnames":["Junji"],"suffixes":[]},{"propositions":[],"lastnames":["Sato"],"firstnames":["Takeo"],"suffixes":[]}],"month":"April","year":"2022","pages":"1354–1374","bibtex":"@article{hasegawa_tgnee_2022,\n\ttitle = {The {TGN}/{EE} {SNARE} protein {SYP61} and the ubiquitin ligase {ATL31} cooperatively regulate plant responses to carbon/nitrogen conditions in {Arabidopsis}},\n\tvolume = {34},\n\tissn = {1040-4651},\n\turl = {https://doi.org/10.1093/plcell/koac014},\n\tdoi = {10.1093/plcell/koac014},\n\tabstract = {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. 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