Generic sorting of raft lipids into secretory vesicles in yeast

Traffic. 2011 Sep;12(9):1139-47. doi: 10.1111/j.1600-0854.2011.01221.x. Epub 2011 Jun 15.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Transport Systems / chemistry
  • Amino Acid Transport Systems / genetics
  • Amino Acid Transport Systems / metabolism
  • Ergosterol / chemistry
  • Ergosterol / metabolism*
  • Intracellular Signaling Peptides and Proteins / chemistry
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Lipid Metabolism
  • Mass Spectrometry
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism
  • Membrane Microdomains / chemistry
  • Membrane Microdomains / metabolism*
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Proton-Translocating ATPases / chemistry
  • Proton-Translocating ATPases / genetics
  • Proton-Translocating ATPases / metabolism
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Secretory Vesicles / chemistry
  • Secretory Vesicles / metabolism*
  • Sphingolipids / chemistry
  • Sphingolipids / metabolism*
  • trans-Golgi Network / metabolism

Substances

  • Amino Acid Transport Systems
  • GAP1 protein, S cerevisiae
  • Intracellular Signaling Peptides and Proteins
  • MID2 protein, S cerevisiae
  • Membrane Glycoproteins
  • Membrane Proteins
  • Saccharomyces cerevisiae Proteins
  • Sphingolipids
  • PMA1 protein, S cerevisiae
  • Proton-Translocating ATPases
  • Ergosterol