The TGN/EE SNARE protein SYP61 and the ubiquitin ligase ATL31 cooperatively regulate plant responses to carbon/nitrogen conditions in Arabidopsis. Issue 4 (28th January 2022)
- Record Type:
- Journal Article
- Title:
- The TGN/EE SNARE protein SYP61 and the ubiquitin ligase ATL31 cooperatively regulate plant responses to carbon/nitrogen conditions in Arabidopsis. Issue 4 (28th January 2022)
- Main Title:
- The TGN/EE SNARE protein SYP61 and the ubiquitin ligase ATL31 cooperatively regulate plant responses to carbon/nitrogen conditions in Arabidopsis
- 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 - Abstract:
- 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. Abstract : 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 nitrogenAbstract: 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. Abstract : 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. … (more)
- Is Part Of:
- The Plant Cell. Volume 34:Issue 4(2022)
- Journal:
- The Plant Cell
- Issue:
- Volume 34:Issue 4(2022)
- Issue Display:
- Volume 34, Issue 4 (2022)
- Year:
- 2022
- Volume:
- 34
- Issue:
- 4
- Issue Sort Value:
- 2022-0034-0004-0000
- Page Start:
- 1354
- Page End:
- 1374
- Publication Date:
- 2022-01-28
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1093/plcell/koac014 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 26269.xml