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• W4225763319 endingPage "3283" @default.
• W4225763319 startingPage "3276" @default.
• W4225763319 abstract "Alcohol consumption leads to formation of phosphatidylethanol (PEth) via the transphosphatidylation activity of phospholipase D (PLD) enzymes. Though this non-natural phospholipid routinely serves as a biomarker of chronic alcoholism, its pathophysiological roles remain unknown. We use a minimalist diazirine alkyne alcohol as an ethanol surrogate to generate clickable, photoaffinity lipid reporters of PEth localization and lipid-protein interactions via PLD-mediated transphosphatidylation. We use these tools to visualize phosphatidyl alcohols in a manner compatible with standard permeabilization and immunofluorescence methods. We also use click chemistry tagging, enrichment, and proteomics analysis to define the phosphatidyl alcohol interactome. Our analysis reveals an enrichment of putative interactors at various membrane locations, and we validate one such interaction with the single-pass transmembrane protein basigin/CD147. This study provides a comprehensive view of the molecular interactions of phosphatidyl alcohols with the cellular proteome and points to future work to connect such interactions to potential pathophysiological roles of PEth." @default.
• W4225763319 created "2022-05-05" @default.
• W4225763319 creator A5026295078 @default.
• W4225763319 creator A5032711623 @default.
• W4225763319 creator A5033010189 @default.
• W4225763319 creator A5059297673 @default.
• W4225763319 date "2021-12-15" @default.
• W4225763319 modified "2023-09-28" @default.
• W4225763319 title "A Chemoproteomics Approach to Profile Phospholipase D-Derived Phosphatidyl Alcohol Interactions" @default.
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• W4225763319 doi "https://doi.org/10.1021/acschembio.1c00584" @default.
• W4225763319 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34908404" @default.
• W4225763319 hasPublicationYear "2021" @default.
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