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Li, Y and Qi, B (2017) Progress toward Understanding Protein S-acylation: Prospective in Plants. Frontiers in Plant Science, 8. ISSN 1664-462X
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Progress toward Understanding Protein S-acylation Prospective in Plants.pdf - Published Version Available under License Creative Commons Attribution. Download (1MB) | Preview |
Abstract
S-acylation, also known as S-palmitoylation or palmitoylation, is a reversible posttranslational lipid modification in which long chain fatty acid, usually the 16-carbon palmitate, covalently attaches to a cysteine residue(s) throughout the protein via a thioester bond. It is involved in an array of important biological processes during growth and development, reproduction and stress responses in plant. S-acylation is a ubiquitous mechanism in eukaryotes catalyzed by a family of enzymes called Protein S-Acyl Transferases (PATs). Since the discovery of the first PAT in yeast in 2002 research in S-acylation has accelerated in the mammalian system and followed by in plant. However, it is still a difficult field to study due to the large number of PATs and even larger number of putative S-acylated substrate proteins they modify in each genome. This is coupled with drawbacks in the techniques used to study S-acylation, leading to the slower progress in this field compared to protein phosphorylation, for example. In this review we will summarize the discoveries made so far based on knowledge learnt from the characterization of protein S-acyltransferases and the S-acylated proteins, the interaction mechanisms between PAT and its specific substrate protein(s) in yeast and mammals. Research in protein S-acylation and PATs in plants will also be covered although this area is currently less well studied in yeast and mammalian systems.
| Item Type: | Article |
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| Uncontrolled Keywords: | 0607 Plant Biology |
| Subjects: | R Medicine > RV Botanic, Thomsonian, and eclectic medicine |
| Divisions: | Pharmacy & Biomolecular Sciences |
| Publisher: | Frontiers Media |
| Related URLs: | |
| Date Deposited: | 08 Oct 2019 11:25 |
| Last Modified: | 04 Sep 2021 08:44 |
| DOI or ID number: | 10.3389/fpls.2017.00346 |
| URI: | https://researchonline.ljmu.ac.uk/id/eprint/11494 |
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