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

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

Sammanfattning

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.
Originalspråkengelska
TidskriftChemistry and Physics of Lipids
Volym164
Utgåva6
Sidor (från-till)443-450
Antal sidor8
ISSN0009-3084
DOI
StatusPublicerad - 17 sep 2011
MoE-publikationstypA1 Tidskriftsartikel-refererad

Vetenskapsgrenar

  • 3111 Biomedicinska vetenskaper

Citera det här

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title = "Cytoplasmic oxysterol-binding proteins: sterol sensors or transporters?",
abstract = "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.",
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Cytoplasmic oxysterol-binding proteins: sterol sensors or transporters? / Vihervaara, Terhi Marjut; Jansen, Maurice; Uronen, Riikka-Liisa Eveliina; Ohsaki, Yuki; Ikonen, Elina Maria; Olkkonen, Vesa M.

I: Chemistry and Physics of Lipids, Vol. 164, Nr. 6, 17.09.2011, s. 443-450.

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

TY - JOUR

T1 - Cytoplasmic oxysterol-binding proteins: sterol sensors or transporters?

AU - Vihervaara, Terhi Marjut

AU - Jansen, Maurice

AU - Uronen, Riikka-Liisa Eveliina

AU - Ohsaki, Yuki

AU - Ikonen, Elina Maria

AU - Olkkonen, Vesa M.

PY - 2011/9/17

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AB - 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.

KW - 3111 Biomedicine

U2 - 10.1016/j.chemphyslip.2011.03.002

DO - 10.1016/j.chemphyslip.2011.03.002

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SP - 443

EP - 450

JO - Chemistry and Physics of Lipids

JF - Chemistry and Physics of Lipids

SN - 0009-3084

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