Cytoplasmic oxysterol-binding proteins: sterol sensors or transporters?

Terhi Marjut Vihervaara, Maurice Jansen, Riikka-Liisa Eveliina Uronen, Yuki Ohsaki, Elina Maria Ikonen, Vesa M. Olkkonen

Research output: Contribution to journalArticleScientificpeer-review


Families of oxysterol-binding protein (ORP) homologues are present in eukaryotes from yeast to man. Their hallmark feature is a characteristic ligand binding domain that, for several family members, has been shown to accommodate different oxysterols and/or cholesterol. ORPs of the “long” subtype contain targeting determinants for the endoplasmic reticulum and to other organelle membranes, the most prominent of which are phosphoinositide-binding pleckstrin homology domains, while “short” ORPs comprise a ligand binding domain with little additional sequences. There is increasing evidence that both long and short ORPs can be enriched at membrane contact sites, junctions of the endoplasmic reticulum with other organelles, where they are suggested to execute regulatory or sterol transfer functions. In this review we discuss the current evidence for putative roles of ORPs as sterol sensors or transporters.
Original languageEnglish
JournalChemistry and Physics of Lipids
Issue number6
Pages (from-to)443-450
Number of pages8
Publication statusPublished - 17 Sep 2011
MoE publication typeA1 Journal article-refereed

Fields of Science

  • 3111 Biomedicine

Cite this