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Updated: Feb 28, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
Structure and function of DHHC protein S-acyltransferases
Colin D Gottlieb1, Maurine E Linder2
1Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY, U.S.A.
DHHC proteins modify 10% of human proteins via fatty acylation. This review explores recent findings on the structure and function of these crucial enzymes, highlighting their role in cell membranes and human disease.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Approximately 10% of the human genome encodes proteins undergoing fatty acylation at cysteine residues.
- The DHHC protein family is primarily responsible for this modification, functioning on the cytoplasmic side of cell membranes.
- DHHC proteins are implicated in various human diseases, emphasizing their biomedical significance.
Purpose of the Study:
- To review recent advancements in understanding the structure and function of DHHC enzymes.
- To elucidate the molecular mechanisms governing DHHC protein activity.
- To highlight the importance of DHHC proteins in cellular processes and disease.
Main Methods:
- Literature review of recent studies on DHHC protein structure and function.
- Analysis of data from DHHC-deficient mouse models.
- Integration of findings on enzymatic mechanisms and cellular roles.
Main Results:
- Recent structural and functional insights into DHHC enzymes have been elucidated.
- The essential roles of DHHC proteins in cellular functions and their links to disease are increasingly understood.
- DHHC-deficient mouse models have provided critical data on protein function.
Conclusions:
- DHHC proteins are vital enzymes involved in protein fatty acylation with significant implications for human health.
- Further research into DHHC enzyme mechanisms is crucial for understanding their roles in disease and developing potential therapies.
- The review synthesizes current knowledge, providing a foundation for future investigations into DHHC protein biology.
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