Search results for OSBP

Showing 14 results out of 18

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Protein (7 results from a total of 11)

Identifier: R-HSA-429725
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: OSBP: P22059
Identifier: R-HSA-8867856
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: OSBPL5: Q9H0X9
Identifier: R-HSA-8867870
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: OSBPL8: Q9BZF1
Identifier: R-HSA-8867529
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: OSBPL10: Q9BXB5
Identifier: R-HSA-8867527
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: OSBPL2: Q9H1P3
Identifier: R-HSA-8867534
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: OSBPL6: Q9BZF3
Identifier: R-HSA-8867532
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: OSBPL3: Q9H4L5

Reaction (4 results from a total of 4)

Identifier: R-HSA-8868402
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane, Golgi membrane
Oxysterol-binding protein 1 (OSBP) is involved in lipid countertransport between the Golgi and the ER membranes. It specifically exchanges sterols such as 25-hydroxycholesterol (25OH-CHOL) with phosphatidylinositol 4-phosphate (PI4P), delivering it to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatases in the ER. The PH-FFAT region of OSBP is necessary for membrane tethering, which then directs forward sterol and backward PI4P transport by the ORD domain of OSBP (Mesmin et al. 2013).
Identifier: R-HSA-8867667
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane, plasma membrane
Oxysterol-binding proteins (OSBPs) and OSBP-related proteins (ORPs) comprise a 12-member mammalian gene family of intracellular lipid receptors which bind oxygenated cholesterol derivatives and are thought to mediate sterol and phospholipid synthesis (Olkkonen & Li 2013, Weber-Boyvat et al. 2013). A conserved OSBP homology domain (OHD) binds sterols and lipids and a pleckstrin homology (PH) domain and two phenylalanines in an acidic tract (FFAT) motif mediate interaction with organelle membranes (Olkkonen 2015). The primary function of the protein family remains unresolved. Most (OSBPL2,3,6,7,9 and 1A), if not all of the OSBPLs are thought to bind and coordinate distribution of oxygenated cholesterol derivatives such as 25-hydroxycholesterol (25OH-CHOL). Oxysterol-binding protein 2 (OSBP2, aka ORP4) is primarily expressed in brain, and to a lesser extent in heart, skeletal muscle, spleen and kidney. It has a diffuse cytoplasmic localisation profile and is a high-affinity 25OH-CHOL binding protein (Wang et al. 2002, Suchanek et al. 2007). RNAi silencing of all OSBP2 variants in HEK293 and HeLa cells resulted in growth arrest but not cell death, suggesting OSBP2 is essential for cell proliferation and survival (Charman et al. 2014).
Identifier: R-HSA-8867876
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, plasma membrane, cytosol
Phosphatidylserine (PS) is a lipid component of cellular membranes. It is synthesised in the endoplasmic reticulum and then preferentially associates with the inner leaflet of the plasma membrane by as-yet unknown mechanisms. Intracellular lipids can travel through aqueous phases via transport vesicles or lipid-transfer proteins (LTPs). Oxysterol-binding protein-related proteins 5, 8 and 10 (OSBPL5, OSBPL8 and OSBPL10) bind and transport PS from ER compartments to the plasma membrane. They tether the ER to the plasma membrane via interaction of their pleckstrin homology domains with phosphatidylinositol 4-phosphate (PI4P) and mediate PI4P/PS countertransport between the ER and the plasma membrane (Du et al. 2011, Chung et al. 2015, Perttila et al. 2009, Maeda et al. 2013). OSBPL10 is also implicated in apolipoprotein B100 secretion (Nissila et al. 2012).
Identifier: R-HSA-429683
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
CERT1-2 (ceramide transfer protein, isoform 2), associated with the cytosolic face of the endoplasmic reticulum (ER) in a complex with VAPA or VAPB (VAMP-associated proteins A or B) (Kawano et al. 2006) and PPM1L (protein phosphatase 1-like) (Saito et al. 2008), can bridge the gap between the ER and the Golgi apparatus via its PH domain and transfer a molecule of ceramide extracted from the ER membrane to the Golgi at the ER-Golgi membrane contact sites (MCS) (Hanada et al. 2003; Saito et al. 2008). CERT1-2-mediated ceramide transfer is positively regulated by OSBP (oxysterol binding protein), apparently through accumulation of phosphatidylinositol 4-phosphate (PI-4P) at MCS (Perry and Ridgway 2006; Goto et al., 2016). Non-vesicular transport of ceramide from endoplasmic reticulum to Golgi membranes is essential for cellular lipid homeostasis (reviewed by Olaiyoye et al., 2012; Kumagai & Hanada, 2019).

Set (2 results from a total of 2)

Identifier: R-HSA-8868084
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-8867857
Species: Homo sapiens
Compartment: cytosol

Interactor (1 results from a total of 1)

Identifier: Q969R2-2
Species: Homo sapiens
Primary external reference: UniProt: Q969R2-2
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