An ABHD17-like hydrolase screening system to identify de-S-acylation enzymes of protein substrates in plant cells. Issue 10 (2nd August 2021)
- Record Type:
- Journal Article
- Title:
- An ABHD17-like hydrolase screening system to identify de-S-acylation enzymes of protein substrates in plant cells. Issue 10 (2nd August 2021)
- Main Title:
- An ABHD17-like hydrolase screening system to identify de-S-acylation enzymes of protein substrates in plant cells
- Authors:
- Liu, Xiaoshi
Li, Min
Li, Yang
Chen, Zian
Zhuge, Chun
Ouyang, Youwei
Zhao, Yawen
Lin, Yuxin
Xie, Qi
Yang, Chengwei
Lai, Jianbin - Abstract:
- Abstract: Protein S-acylation is an important post-translational modification in eukaryotes, regulating the subcellular localization, trafficking, stability, and activity of substrate proteins. The dynamic regulation of this reversible modification is mediated inversely by protein S-acyltransferases and de-S-acylation enzymes, but the de-S-acylation mechanism remains unclear in plant cells. Here, we characterized a group of putative protein de-S-acylation enzymes in Arabidopsis thaliana, including 11 members of Alpha/Beta Hydrolase Domain-containing Protein 17-like acyl protein thioesterases (ABAPTs). A robust system was then established for the screening of de-S-acylation enzymes of protein substrates in plant cells, based on the effects of substrate localization and confirmed via the protein S-acylation levels. Using this system, the ABAPTs, which specifically reduced the S-acylation levels and disrupted the plasma membrane localization of five immunity-related proteins, were identified respectively in Arabidopsis. Further results indicated that the de-S-acylation of RPM1-Interacting Protein 4, which was mediated by ABAPT8, resulted in an increase of cell death in Arabidopsis and Nicotiana benthamiana, supporting the physiological role of the ABAPTs in plants. Collectively, our current work provides a powerful and reliable system to identify the pairs of plant protein substrates and de-S-acylation enzymes for further studies on the dynamic regulation of plant proteinAbstract: Protein S-acylation is an important post-translational modification in eukaryotes, regulating the subcellular localization, trafficking, stability, and activity of substrate proteins. The dynamic regulation of this reversible modification is mediated inversely by protein S-acyltransferases and de-S-acylation enzymes, but the de-S-acylation mechanism remains unclear in plant cells. Here, we characterized a group of putative protein de-S-acylation enzymes in Arabidopsis thaliana, including 11 members of Alpha/Beta Hydrolase Domain-containing Protein 17-like acyl protein thioesterases (ABAPTs). A robust system was then established for the screening of de-S-acylation enzymes of protein substrates in plant cells, based on the effects of substrate localization and confirmed via the protein S-acylation levels. Using this system, the ABAPTs, which specifically reduced the S-acylation levels and disrupted the plasma membrane localization of five immunity-related proteins, were identified respectively in Arabidopsis. Further results indicated that the de-S-acylation of RPM1-Interacting Protein 4, which was mediated by ABAPT8, resulted in an increase of cell death in Arabidopsis and Nicotiana benthamiana, supporting the physiological role of the ABAPTs in plants. Collectively, our current work provides a powerful and reliable system to identify the pairs of plant protein substrates and de-S-acylation enzymes for further studies on the dynamic regulation of plant protein S-acylation. Abstract : A robust screening system for ABHD17-like hydrolases was established to identify de-S-acylation enzymes of protein substrates in plant cells. … (more)
- Is Part Of:
- The Plant Cell. Volume 33:Issue 10(2021)
- Journal:
- The Plant Cell
- Issue:
- Volume 33:Issue 10(2021)
- Issue Display:
- Volume 33, Issue 10 (2021)
- Year:
- 2021
- Volume:
- 33
- Issue:
- 10
- Issue Sort Value:
- 2021-0033-0010-0000
- Page Start:
- 3235
- Page End:
- 3249
- Publication Date:
- 2021-08-02
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1093/plcell/koab199 ↗
- 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:
- 25857.xml