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Mechanism and function of DHHC S-acyltransferases
Maurine E Linder1, Benjamin C Jennings
1Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA. mel237@cornell.edu
Biochemical Society Transactions
|January 30, 2013
Summary
Protein S-palmitoylation, a key fatty acid modification, is increasingly identified in hundreds of proteins. This process, mediated by DHHC protein acyltransferases (PATs), impacts protein function and stability, offering therapeutic targets for diseases.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Protein S-palmitoylation is a reversible post-translational modification involving fatty acid attachment.
- Recent advances in proteomics have identified hundreds of new palmitoylation substrates.
- This modification influences protein membrane interactions, activity, trafficking, and stability.
Purpose of the Study:
- To review recent advancements in understanding protein S-palmitoylation.
- To discuss the mechanism, regulation, and substrate specificity of DHHC protein acyltransferases (PATs).
- To highlight the biomedical significance of PATs and their potential as therapeutic targets.
Main Methods:
- Review of recent scientific literature and proteomic studies.
- Analysis of the catalytic mechanism and regulatory pathways of PATs.
- Discussion of substrate identification and specificity.
Main Results:
- The number of identified palmitoylated proteins has significantly increased due to improved proteomic techniques.
- Protein S-palmitoylation plays crucial roles in various cellular processes.
- DHHC PATs, characterized by their catalytic DHHC domain, are central to this modification.
Conclusions:
- DHHC PATs are essential enzymes involved in protein S-palmitoylation.
- Dysregulation of PATs is linked to human diseases including intellectual disability, Huntington's disease, and cancer.
- DHHC PATs represent promising targets for future therapeutic interventions.
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