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http://purl.uniprot.org/citations/35960718http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35960718http://www.w3.org/2000/01/rdf-schema#comment"Protein S-palmitoylation, the addition of a long-chain fatty acid to target proteins, is among the most frequent reversible protein modifications in Metazoa, affecting subcellular protein localization, trafficking and protein-protein interactions. S-palmitoylated proteins are abundant in the neuronal system and are associated with neuronal diseases and cancer. Despite the importance of this post-translational modification, it has not been thoroughly studied in the model organism Drosophila melanogaster. Here we present the palmitoylome of Drosophila S2R+ cells, comprising 198 proteins, an estimated 3.5% of expressed genes in these cells. Comparison of orthologs between mammals and Drosophila suggests that S-palmitoylated proteins are more conserved between these distant phyla than non-S-palmitoylated proteins. To identify putative client proteins and interaction partners of the DHHC family of protein acyl-transferases (PATs) we established DHHC-BioID, a proximity biotinylation-based method. In S2R+ cells, ectopic expression of the DHHC-PAT dHip14-BioID in combination with Snap24 or an interaction-deficient Snap24-mutant as a negative control, resulted in biotinylation of Snap24 but not the Snap24-mutant. DHHC-BioID in S2R+ cells using 10 different DHHC-PATs as bait identified 520 putative DHHC-PAT interaction partners of which 48 were S-palmitoylated and are therefore putative DHHC-PAT client proteins. Comparison of putative client protein/DHHC-PAT combinations indicates that CG8314, CG5196, CG5880 and Patsas have a preference for transmembrane proteins, while S-palmitoylated proteins with the Hip14-interaction motif are most enriched by DHHC-BioID variants of approximated and dHip14. Finally, we show that BioID is active in larval and adult Drosophila and that dHip14-BioID rescues dHip14 mutant flies, indicating that DHHC-BioID is non-toxic. In summary we provide the first systematic analysis of a Drosophila palmitoylome. We show that DHHC-BioID is sensitive and specific enough to identify DHHC-PAT client proteins and provide DHHC-PAT assignment for ca. 25% of the S2R+ cell palmitoylome, providing a valuable resource. In addition, we establish DHHC-BioID as a useful concept for the identification of tissue-specific DHHC-PAT interactomes in Drosophila."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0261543"xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Russell R.B."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Navarro J.A."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Wieland F.T."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Anders S."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Fritsch J."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Metzendorf C."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Shapira I."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Porcellato E."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Gonzalez-Sanchez J.C."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Ahlmann-Eltze C."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/author"Elsakka M.A."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/name"PLoS One"xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/pages"e0261543"xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/title"The S-palmitoylome and DHHC-PAT interactome of Drosophila melanogaster S2R+ cells indicate a high degree of conservation to mammalian palmitoylomes."xsd:string
http://purl.uniprot.org/citations/35960718http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/35960718http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/35960718
http://purl.uniprot.org/citations/35960718http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/35960718
http://purl.uniprot.org/uniprot/#_A0A0B4KF56-mappedCitation-35960718http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35960718
http://purl.uniprot.org/uniprot/#_A0A0B4LEL6-mappedCitation-35960718http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35960718
http://purl.uniprot.org/uniprot/#_A0A0B4LF00-mappedCitation-35960718http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35960718
http://purl.uniprot.org/uniprot/#_A0A0B4LF16-mappedCitation-35960718http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35960718
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