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

Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

Kuvaus

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.
Alkuperäiskielienglanti
LehtiChemistry and Physics of Lipids
Vuosikerta164
Numero6
Sivut443-450
Sivumäärä8
ISSN0009-3084
DOI - pysyväislinkit
TilaJulkaistu - 17 syyskuuta 2011
OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä, vertaisarvioitu

Tieteenalat

  • 3111 Biolääketieteet

Lainaa tätä

Vihervaara, Terhi Marjut ; Jansen, Maurice ; Uronen, Riikka-Liisa Eveliina ; Ohsaki, Yuki ; Ikonen, Elina Maria ; Olkkonen, Vesa M. / Cytoplasmic oxysterol-binding proteins: sterol sensors or transporters?. Julkaisussa: Chemistry and Physics of Lipids. 2011 ; Vuosikerta 164, Nro 6. Sivut 443-450.
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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.",
keywords = "3111 Biomedicine",
author = "Vihervaara, {Terhi Marjut} and Maurice Jansen and Uronen, {Riikka-Liisa Eveliina} and Yuki Ohsaki and Ikonen, {Elina Maria} and Olkkonen, {Vesa M.}",
year = "2011",
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language = "English",
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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.

julkaisussa: Chemistry and Physics of Lipids, Vuosikerta 164, Nro 6, 17.09.2011, s. 443-450.

Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

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

Y1 - 2011/9/17

N2 - 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.

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

M3 - Article

VL - 164

SP - 443

EP - 450

JO - Chemistry and Physics of Lipids

JF - Chemistry and Physics of Lipids

SN - 0009-3084

IS - 6

ER -