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The Drosophila protein palmitoylome: characterizing palmitoyl-thioesterases and DHHC palmitoyl-transferases.
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Who cites it
26 citing papers in PubMed, 59 citations in OpenAlex.
- Huntington's disease-associated ankyrin repeat palmitoyl transferases are rate-limiting factors in lysosome formation and fusion.PLoS genetics · 2025Article
- Bioinformatics and Expression Profiling of the DHHC-CRD S-Acyltransferases Reveal Their Roles in Growth and Stress Response in Woodland Strawberry (Plants (Basel, Switzerland) · 2025Article
- Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications.The Journal of cell biology · 2023Article
- Viruses in LaboratoryViruses · 2023Article
- Lost in traffic: consequences of altered palmitoylation in neurodegeneration.Frontiers in physiology · 2023Review
- Comparison of insect and human cytochrome b561 proteins: Insights into candidate ferric reductases in insects.PloS one · 2023Article
- Modelling the structure of Short Gastrulation and generation of a toolkit for studying its function in Drosophila.Biology open · 2022Article
- Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo.Nature communications · 2022Article
- Regulation of T cell function by protein S-acylation.Frontiers in physiology · 2022Review
- Article
- Substrate recruitment by zDHHC protein acyltransferases.Open biology · 2021Article
- Article
- Overexpression of PPT2 Represses the Clear Cell Renal Cell Carcinoma Progression by Reducing Epithelial-to-mesenchymal Transition.Journal of Cancer · 2020Article
- Drosophila ZDHHC8 palmitoylates scribble and Ras64B and controls growth and viability.PloS one · 2019Article
- Membrane targeting of inhibitory Smads through palmitoylation controls TGF-β/BMP signaling.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Protein S-palmitoylation in cellular differentiation.Biochemical Society transactions · 2017Review
- Progress toward Understanding Protein S-acylation: Prospective in Plants.Frontiers in plant science · 2017Review
- Identification of a Novel Sequence Motif Recognized by the Ankyrin Repeat Domain of zDHHC17/13 S-Acyltransferases.The Journal of biological chemistry · 2015Article
- A systematic analysis of protein palmitoylation in Caenorhabditis elegans.BMC genomics · 2014Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
Palmitoylation is the post-translational addition of a palmitate moiety to a cysteine residue through a covalent thioester bond. The addition and removal of this modification is controlled by both palmitoyl acyl-transferases and thioesterases. Using bioinformatic analysis, we identified 22 DHHC family palmitoyl acyl-transferase homologs in the Drosophila genome. We used in situ hybridization,RT-PCR, and published FlyAtlas microarray data to characterize the expression patterns of all 22 fly homologs. Our results indicate that all are expressed genes, but several, including CG1407, CG4676, CG5620, CG6017/dHIP14, CG6618, CG6627 and CG17257 appear to be enriched in neural tissues suggesting that they are important for neural function. Furthermore, we have found that several may be expressed in a sex-specific manner with adult male specific expression of CG4483 and CG17195. Using tagged versions of the DHHC genes, we demonstrate that fly DHHC proteins are primarily located in either the Golgi Apparatus or Endoplasmic Reticulum in S2 cells, except for CG1407, which was found on the plasma membrane. We also characterized the subcellular localization and expression of the three known thioesterases: Palmitoyl-protein Thioesterase 1 (Ppt1), Palmitoyl-protein Thioesterase 2 (Ppt2)and Acyl-protein Thioesterase 1 (APT1). Our results indicate that Ppt1 and Ppt2 are the major lysosomal thioesterases while APT1 is the likely cytoplasmic thioesterase. Finally, in vivo rescue experiments show that Ppt2 expression cannot rescue the neural inclusion phenotypes associated with loss of Ppt1, further supporting distinct functions and substrates for these two thioesterases. These results will serve as the basis for a more complete understanding of the protein palmitoylome's normal cellular functions in the fly and will lead to further insights into the molecular etiology of diseases associated with the mis-regulation of palmitoylation.
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