Sterol trafficking between the endoplasmic reticulum and plasma membrane in yeast

D. P. Sullivan, H. Ohvo-Rekilä, N. A. Baumann, C. T. Beh, A. K. Menon*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

76 Scopus citations


We recently showed that transport of ergosterol from the ER (endoplasmic reticulum) to the sterol-enriched PM (plasma membrane) in yeast occurs by a non-vesicular (Sec18p-independent) mechanism that results in the equilibration of sterol pools in the two organelles [Baumann, Sullivan, Ohvo-Rekilä, Simonot, Pottekat, Klaassen, Beh and Menon (2005) Biochemistry 44, 5816-5826]. To explore how this occurs, we tested the role of proteins that might act as sterol transporters. We chose to study oxysterol-binding protein homologues (Osh proteins), a family of seven proteins in yeast, all of which contain a putative sterol-binding pocket. Recent structural analyses of one of the Osh proteins [Im, Raychaudhuri, Prinz and Hurley (2005) Nature (London) 437, 154-158] suggested a possible transport cycle in which Osh proteins could act to equilibrate ER and PM pools of sterol. Our results indicate that the transport of newly synthesized ergosterol from the ER to the PM in an OSH deletion mutant lacking all seven Osh proteins is slowed only 5-fold relative to the isogenic wild-type strain. Our results suggest that the Osh proteins are not sterol transporters themselves, but affect sterol transport in vivo indirectly by affecting the ability of the PM to sequester sterols.

Original languageEnglish (US)
Pages (from-to)356-358
Number of pages3
JournalBiochemical Society transactions
Issue number3
StatePublished - Jun 2006


  • Endoplasmic reticulum
  • Ergosterol
  • Osh protein
  • Sphingolipid
  • Sterol trafficking
  • Yeast

ASJC Scopus subject areas

  • Biochemistry


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