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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Oxysterol binding protein

OSBP, Oxysterol-binding protein
Oxysterol binding protein is an intracellular protein that is believed to transport sterols from lysosomes to the nucleus where the sterol down-regulates the genes for the LDL receptor, HMG-CoA reductase, and HMG synthetase [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, V1a, ACID, HAD, ORP3
Papers on OSBP
Oxysterol-binding Protein Activation at Endoplasmic Reticulum-Golgi Contact Sites Reorganizes Phosphatidylinositol 4-Phosphate Pools.
Ridgway et al., Halifax, Canada. In J Biol Chem, Feb 2016
Oxysterol-binding protein (OSBP) exchanges cholesterol and phosphatidylinositol 4-phosphate (PI-4P) at contact sites between the endoplasmic reticulum (ER) and the trans-Golgi/trans-Golgi network.
CARTS biogenesis requires VAP-lipid transfer protein complexes functioning at the endoplasmic reticulum-Golgi interface.
Tagaya et al., Hachiƍji, Japan. In Mol Biol Cell, Jan 2016
Vesicle-associated membrane protein-associated protein (VAP) is an endoplasmic reticulum (ER)-resident integral membrane protein that controls a nonvesicular mode of ceramide and cholesterol transfer from the ER to the Golgi complex by interacting with ceramide transfer protein and oxysterol-binding protein (OSBP), respectively.
MicroRNA124 Regulated Neurite Elongation by Targeting OSBP.
Wang et al., Guangzhou, China. In Mol Neurobiol, Dec 2015
In this study, we demonstrated that miR-124 directly targeted and downregulated the endogenous expression of oxysterol-binding protein (OSBP).
Delivery of Constitutively Active Mutant MKK6(E) With TAT-OSBP Induces Apoptosis in Human Ovarian Carcinoma HO8910 Cells.
Shuai et al., Guangzhou, China. In Int J Gynecol Cancer, Nov 2015
In this study, we evaluated the tumor selectivity, cellular internalization, and biological activity of a cell-permeable ovarian cancer cell-specific therapeutic protein consisting of TAT-OSBP and constitutively active MKK6(E), an upstream kinase of the p38 signaling pathway that mediates cellular apoptosis.
Modulation of the Host Lipid Landscape to Promote RNA Virus Replication: The Picornavirus Encephalomyocarditis Virus Converges on the Pathway Used by Hepatitis C Virus.
van Kuppeveld et al., Utrecht, Netherlands. In Plos Pathog, Sep 2015
The ensuing phosphatidylinositol 4-phosphate (PI4P) proved important for the recruitment of oxysterol-binding protein (OSBP), which delivers cholesterol to EMCV ROs in a PI4P-dependent manner.
Novel mechanisms of intracellular cholesterol transport: oxysterol-binding proteins and membrane contact sites.
Yang et al., Sydney, Australia. In Curr Opin Cell Biol, Aug 2015
Sterol transfer by lipid-binding proteins, such as OSBP (oxysterol-binding protein), coupled with phosphatidylinositol 4-phosphate exchange at membrane contact sites (MCSs) has emerged as a new theme of cholesterol transport between organellar membranes.
INTRACELLULAR TRANSPORT. PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contacts.
De Camilli et al., New Haven, United States. In Science, Aug 2015
We found that two similar ER integral membrane proteins, oxysterol-binding protein (OSBP)-related protein 5 (ORP5) and ORP8, tethered the ER to the plasma membrane (PM) via the interaction of their pleckstrin homology domains with phosphatidylinositol 4-phosphate (PI4P) in this membrane.
Mitogen-activated Protein Kinase Kinase 6-fusion Protein (MAP2K6-FP) Potentiates the Anti-tumor effects of Paclitaxel in Ovarian Cancer.
Deng et al., Guangzhou, China. In Anticancer Agents Med Chem, 2014
OBJECTIVE: To investigate the antitumor effects of a mitogen-activated protein kinase (MAPK) kinase fusion protein, TAT-OSBP-MKK6E (MAP2K6-FP), and paclitaxel as single agents and in combination against HO8910 human ovarian cancer cells.
OSBP-Related Protein Family in Lipid Transport Over Membrane Contact Sites.
Olkkonen, Helsinki, Finland. In Lipid Insights, 2014
Increasing evidence suggests that oxysterol-binding protein-related proteins (ORPs) localize at membrane contact sites, which are high-capacity platforms for inter-organelle exchange of small molecules and information.
NPC1, intracellular cholesterol trafficking and atherosclerosis.
Tang et al., Hengyang, China. In Clin Chim Acta, 2014
Niemann-Pick type C1 (NPC1), an integral membrane protein on the limiting membrane of late endosome/lysosome (LE/LY), is known to accept cholesterol from NPC2 and then mediate cholesterol transport from LE/LY to endoplasmic reticulum (ER) and plasma membrane in a vesicle- or oxysterol-binding protein (OSBP)-related protein 5 (ORP5)-dependent manner.
A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP.
Antonny et al., Antibes, France. In Cell, 2013
We show that in oxysterol binding protein (OSBP) these two activities are coupled by a four-step cycle.
Oxysterol-binding proteins: sterol and phosphoinositide sensors coordinating transport, signaling and metabolism.
Li et al., Helsinki, Finland. In Prog Lipid Res, 2013
Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) constitute a family of sterol and phosphoinositide binding proteins conserved in eukaryotes.
OSBP-related proteins: liganding by glycerophospholipids opens new insight into their function.
Olkkonen, Helsinki, Finland. In Molecules, 2012
Oxysterol-binding protein (OSBP) and its homologs designated OSBP-related (ORP) or OSBP-like (OSBPL) proteins constitute a conserved family of lipid binding/transfer proteins (LTP) in eukaryotes.
Protein kinase D negatively regulates hepatitis C virus secretion through phosphorylation of oxysterol-binding protein and ceramide transfer protein.
Siddiqui et al., San Diego, United States. In J Biol Chem, 2011
PKD negatively regulates HCV secretion/release by attenuating OSBP and CERT functions by phosphorylation inhibition. This study identifies the key role of the Golgi components in the HCV maturation process.
Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation.
Toker et al., Boston, United States. In Mol Biol Cell, 2010
Results identify a novel substrate of protein kinase D at the Golgi, the oxysterol-binding protein OSBP.
Functional implications of sterol transport by the oxysterol-binding protein gene family.
Ridgway et al., Halifax, Canada. In Biochem J, 2010
This review summarizes recent evidence of sterol transfer activity by OSBP, suggesting seemingly disparate functions that could be the result of alterations in membrane sterol distribution or ancillary to this primary activity.
Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies.
Kojima et al., Nara, Japan. In J Biol Chem, 2010
Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies.
Role of oxysterol binding protein in hepatitis C virus infection.
Siddiqui et al., San Diego, United States. In J Virol, 2009
functional role of OSBP in the HCV maturation process.
Structural mechanism for sterol sensing and transport by OSBP-related proteins.
Hurley et al., Bethesda, United States. In Nature, 2005
The oxysterol-binding-protein (OSBP)-related proteins (ORPs) are conserved from yeast to humans, and are implicated in the regulation of sterol homeostasis and in signal transduction pathways.
OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation.
Anderson et al., Dallas, United States. In Science, 2005
OSBP was found to function as a cholesterol-binding scaffolding protein coordinating the activity of two phosphatases to control the extracellular signal-regulated kinase (ERK) signaling pathway
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