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10.4137/LPI.S31726 http://scihub22266oqcxt.onion/10.4137/LPI.S31726 C4685180!4685180!26715851     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Lipid+Insights 2015 ; 8 (Suppl 1): 1-9 Nephropedia Template TP {{tp|p=26715851|t=2015. OSBP-Related Protein Family in Lipid Transport Over Membrane Contact Sites |pdf=|usr=}}{{26715851}} gab.com Text OSBP-Related Protein Family in Lipid Transport Over Membrane Contact Sites JO: Lipid Insights http://www.kidney.de/pget.php?&tw=1&pmid=26715851 #FOAvip 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. ORPs can simultaneously associate with the two apposed membranes and transfer lipids across the interbilayer gap. Oxysterol-binding protein moves cholesterol from the endoplasmic reticulum to trans-Golgi, driven by the retrograde transport of phosphatidylinositol-4-phosphate (PI4P). Analogously, yeast Osh6p mediates the transport of phosphatidylserine from the endoplasmic reticulum to the plasma membrane in exchange for PI4P, and ORP5 and -8 are suggested to execute similar functions in mammalian cells. ORPs may share the capacity to bind PI4P within their ligand-binding domain, prompting the hypothesis that bidirectional transport of a phosphoinositide and another lipid may be a common theme among the protein family. This model, however, needs more experimental support and does not exclude a function of ORPs in lipid signaling. Twit Text FOAVip OSBP-Related Protein Family in Lipid Transport Over Membrane Contact Sites ????Lipid Insights http://www.kidney.de/pget.php?&tw=1&pmid=26715851 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26715851 #FOAvip English Wikipedia <ref>{{Cite pmid|26715851}}</ref> OSBP-Related Protein Family in Lipid Transport Over Membrane Contact Sites #MMPMID26715851 Olkkonen VM Lipid Insights 2015[]; 8 (Suppl 1): 1-9 PMID26715851show ga 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. ORPs can simultaneously associate with the two apposed membranes and transfer lipids across the interbilayer gap. Oxysterol-binding protein moves cholesterol from the endoplasmic reticulum to trans-Golgi, driven by the retrograde transport of phosphatidylinositol-4-phosphate (PI4P). Analogously, yeast Osh6p mediates the transport of phosphatidylserine from the endoplasmic reticulum to the plasma membrane in exchange for PI4P, and ORP5 and -8 are suggested to execute similar functions in mammalian cells. ORPs may share the capacity to bind PI4P within their ligand-binding domain, prompting the hypothesis that bidirectional transport of a phosphoinositide and another lipid may be a common theme among the protein family. This model, however, needs more experimental support and does not exclude a function of ORPs in lipid signaling. äOSBP-Related Protein Family in Lipid Transport Over Membrane Contact S(epmc).pdf DeepDyve Pubget Overpricing