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Previous work has showed that ergosterol and sphingolipids become sorted to secretory vesicles immunoisolated using a chimeric, artificial raft membrane protein as bait. In this study, we have extended this analysis to three populations of secretory vesicles isolated using natural yeast plasma membrane (PM) proteins: Pma1p, Mid2p and Gap1*p as baits. We compared the lipidomes of the immunoisolated vesicles with each other and with the lipidomes of the donor compartment, the trans-Golgi network, and the acceptor compartment, the PM, using a quantitative mass spectrometry approach that provided a complete lipid overview of the yeast late secretory pathway. We could show that vesicles captured with different baits carry the same cargo and have almost identical lipid compositions; being highly enriched in ergosterol and sphingolipids. This finding indicates that lipid raft sorting is a generic feature of vesicles carrying PM cargo and suggests a common lipid-based mechanism for their formation.

Original publication




Journal article



Publication Date





1139 - 1147


Amino Acid Transport Systems, Ergosterol, Intracellular Signaling Peptides and Proteins, Lipid Metabolism, Mass Spectrometry, Membrane Glycoproteins, Membrane Microdomains, Membrane Proteins, Proton-Translocating ATPases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Secretory Vesicles, Sphingolipids, trans-Golgi Network