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Progress toward Understanding Protein S-acylation: Prospective in Plants
Frontiers in Plant Science
|April 11, 2017
Summary
S-acylation, a lipid modification, attaches fatty acids to proteins. This review summarizes protein S-acyltransferases (PATs) and their substrates in yeast, mammals, and plants, despite study challenges.
Area of Science:
- Biochemistry and Molecular Biology
- Plant Science
- Cellular Biology
Background:
- S-acylation (palmitoylation) is a reversible lipid post-translational modification.
- It involves attaching palmitate to cysteine residues, impacting biological processes.
- Protein S-acyltransferases (PATs) catalyze this reaction in eukaryotes.
Purpose of the Study:
- To review current knowledge on S-acylation and PATs.
- To summarize findings from yeast and mammalian systems.
- To cover emerging research in plant S-acylation.
Main Methods:
- Literature review and synthesis of existing research.
- Characterization of protein S-acyltransferases (PATs).
- Analysis of S-acylated substrate proteins and their interactions.
Main Results:
- S-acylation is crucial for growth, development, reproduction, and stress responses.
- Research has advanced significantly in yeast and mammals since 2002.
- Plant S-acylation is less studied but gaining attention.
Conclusions:
- S-acylation is a vital and complex cellular process.
- Challenges in studying S-acylation include numerous PATs and substrates.
- Further research, especially in plants, is needed to fully understand this modification.