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Updated: Jun 14, 2026
07:35
Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
DHHC20: a human palmitoyl acyltransferase that causes cellular transformation
Jeremiah M Draper1, Charles D Smith
1Department of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, South Carolina, USA.
Molecular Membrane Biology
|March 26, 2010
Summary
This study identifies DHHC20 as a human enzyme crucial for palmitoylation of N-terminal myristoylated proteins. Overexpression of DHHC20 promotes cancer-like cellular changes and is linked to various tumor types.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Palmitoylation is vital for cancer-associated protein function.
- Palmitoyl acyltransferase (PAT) enzymes are potential anticancer drug targets.
- Human PATs with N-terminal myristoylation activity require characterization.
Purpose of the Study:
- Identify and characterize a human PAT enzyme.
- Investigate DHHC20's role in protein palmitoylation and cellular transformation.
- Determine DHHC20's expression patterns in human tissues and tumors.
Main Methods:
- Stable transfection of NIH/3t3 cells with wild-type DHHC20 and a DHHS20 mutant.
- Assay of palmitoylation activity using N-terminal and C-terminal peptide mimics.
- Analysis of cellular transformation phenotypes (soft agar colony formation, growth inhibition, proliferation).
- Quantitative PCR for DHHC20 expression in human tissues and tumors.
Main Results:
- Overexpression of wild-type DHHC20 increased N-terminal palmitoylation activity.
- DHHC20 overexpression induced cellular transformation phenotypes.
- DHHC20 is overexpressed in ovarian, breast, and prostate tumors.
- DHHC20 exhibits tissue-specific expression.
Conclusions:
- DHHC20 is a human N-terminal-myristoyl-directed PAT.
- DHHC20 plays a role in cellular transformation.
- DHHC20 may be a potential therapeutic target in cancer.
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