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DTSTAMP:20260325T140233
DTSTART;TZID=America/Detroit:20260528T160000
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SUMMARY:Workshop / Seminar:Co-Fractionation ‘Multi-omics’ Mass Spectrometry for Lipid-Protein Interactome Analysis
DESCRIPTION:Lipids play essential roles in regulating various biological processes through functional interactions with integral or peripherally associated proteins and protein complexes. While mass spectrometry (MS)-based strategies have enabled global lipidome and proteome identification and quantitative profiling\, high-throughput strategies to investigate the lipid-protein ‘interactome’ at the systems level are currently lacking. Here\, I will first describe the development of advanced ‘shotgun’ lipidomics data acquisition workflows\, including the use of ion-mobility for selective enrichment of low abundance lipid classes\, and UV-photodissociation MS/MS to enable complete lipid structural characterisation [e.g.\, Anal. Chem. 2024\, 96\, 12296-12307.\; Anal. Bioanal. Chem. 2020\, 412\, 2339–2351.]\, and their application to characterise a novel cause of autosomal regressive multisystem mitochondrial disease resulting from deleterious variants in cardiolipin synthase 1 (CRLS1) [Human Mol. Genetics. 2022\, 31\, 3597-3612.]. Next\, using an integrated ‘multi-omics’ workflow for comprehensive lipidome and proteome profiling\, I will report that the knockout of non-mitochondrial genes in peroxisome\, endoplasmic reticulum (ER) and Golgi organelles also results in mitochondrial dysfunction\, caused by unexpected alterations in ether-glycerophospholipid metabolic pathways [Nature. Cell Biol. 2024\, 26\, 57-71]. Finally\, to investigate the lipid–protein interaction relationships in these systems\, a novel Co-Fractionation Multi-Omics Mass Spectrometry (CF-MOMS) strategy will be described to characterise global alterations in the lipid-protein ‘interactome interactomes in WT and CRLS1KO cell lines\, and to highlight the functional involvement of cardiolipin-protein interactions in maintaining the assembly/stability and activity of mitochondrial membrane proteins.
UID:146965-21899887@events.umich.edu
URL:https://events.umich.edu/event/146965
CLASS:PUBLIC
STATUS:CONFIRMED
CATEGORIES:Analytical Chemistry,Chemistry
LOCATION:Chemistry Dow Lab - 1640
CONTACT:
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