Differential sorting and fate of endocytosed GPI-anchored proteins

Marc Fivaz, Francis Vilbois, Sarah Thurnheer, Christian Pasquali, Laurence Abrami, Perry E. Bickel, Robert G. Parton, F. Gisou Van der Goot

Research output: Contribution to journalArticlepeer-review

193 Scopus citations


In this paper, we studied the fate of endocytosed glycosylphosphatidyl inositol anchored proteins (GPI-APs) in mammalian cells, using aerolysin, a bacterial toxin that binds to the GPI anchor, as a probe. We find that GPI-APs are transported down the endocytic pathway to reducing late endosomes in BHK cells, using biochemical, morphological and functional approaches. We also find that this transport correlates with the association to raft-like membranes and thus that lipid rafts are present in late endosomes (in addition to the Golgi and the plasma membrane). In marked contrast, endocytosed GPI-APs reach the recycling endosome in CHO cells and this transport correlates with a decreased raft association. GPI-APs are, however, diverted from the recycling endosome and routed to late endosomes in CHO cells, when their raft association is increased by clustering seven or less GPI-APs with an aerolysin mutant. We conclude that the different endocytic routes followed by GPI-APs in different cell types depend on the residence time of GPI-APs in lipid rafts, and hence that raft partitioning regulates GPI-APs sorting in the endocytic pathway.

Original languageEnglish (US)
Pages (from-to)3989-4000
Number of pages12
JournalEMBO Journal
Issue number15
StatePublished - Aug 1 2002


  • Aerolysin
  • GPI
  • Late endosome
  • Raft
  • Recycling endosome

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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