We are analyzing https://link.springer.com/article/10.1007/s00018-010-0470-z.

Title:
Sterol binding by OSBP-related protein 1L regulates late endosome motility and function | Cellular and Molecular Life Sciences
Description:
ORP1L is an oxysterol binding homologue that regulates late endosome (LE) positioning. We show that ORP1L binds several oxysterols and cholesterol, and characterize a mutant, ORP1L Δ560–563, defective in oxysterol binding. While wild-type ORP1L clusters LE, ORP1L Δ560–563 induces LE scattering, which is reversed by disruption of the endoplasmic reticulum (ER) targeting FFAT motif, suggesting that it is due to enhanced LE–ER interactions. Endosome motility is reduced upon overexpression of ORP1L. Both wild-type ORP1L and the Δ560–563 mutant induce the recruitment of both dynactin and kinesin-2 on LE. Most of the LE decorated by overexpressed ORP1L fail to accept endocytosed dextran or EGF, and the transfected cells display defective degradation of internalized EGF. ORP1L silencing in macrophage foam cells enhances endosome motility and results in inhibition of [3H]cholesterol efflux to apolipoprotein A-I. These data demonstrate that LE motility and functions in both protein and lipid transport are regulated by ORP1L.
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Keywords {🔍}

article, google, scholar, pubmed, cas, protein, biol, cell, cells, orpl, olkkonen, binding, motility, oxysterolbinding, oxysterol, osbprelated, endosome, res, late, cholesterol, lipid, orp, chem, ridgway, sterol, regulates, membrane, brown, proteins, helsinki, moesmesmmpeg, supplemental, video, lelysosomes, les, labeled, internalization, imaged, live, confocal, microscope, taking, framesecond, total, minute, mpeg, transfected, transport, lehto, human,

Topics {✒️}

oxysterol-binding protein-related protein-9 control rab7-rilp-p150 glued mammalian oxysterol-binding protein month download article/chapter rab-interacting lysosomal protein oxysterol-binding protein recognises orp1-mediated cholesterol transport oxysterol-binding protein homologues osbp-related protein family regulates late endosome orp10-mediated lipid countertransport elina ikonen & vesa position-specific gap penalties oxysterol profiles oxidized monocyte-derived macrophages cholesterol-regulated scaffolding protein ldl receptor-deficient mice enhanced le–er interactions [3h]cholesterol efflux apolipoprotein e-deficient mice late endosome positioning glutathione-s-transferase hdl endosome motility quantitation gfp-rilp cdna construct oxysterol-binding protein oxysterol binding protein gfp-orp1l δ560-563 mffat oxysterol binding homologue oxysterol-binding domains oxysterol binding proteins oxysterol-binding proteins osbp-related protein 3 osbp-related protein 2 osbp-related protein 8 cholesterol transfer protein orp1l silenced macrophage late endosomes/lysosomes lipid-regulated sterol transfer enhances endocytosis cytosolic binding protein osbp-related proteins full article pdf wild-type orp1l cholesterol efflux author information authors er protein vap late endocytic compartments er provide sites privacy choices/manage cookies endosome motility

Questions {❓}

Olkkonen VM, Levine TP (2004) Oxysterol binding proteins: in more than one place at one time?

Schema {🗺️}

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         description:ORP1L is an oxysterol binding homologue that regulates late endosome (LE) positioning. We show that ORP1L binds several oxysterols and cholesterol, and characterize a mutant, ORP1L Δ560–563, defective in oxysterol binding. While wild-type ORP1L clusters LE, ORP1L Δ560–563 induces LE scattering, which is reversed by disruption of the endoplasmic reticulum (ER) targeting FFAT motif, suggesting that it is due to enhanced LE–ER interactions. Endosome motility is reduced upon overexpression of ORP1L. Both wild-type ORP1L and the Δ560–563 mutant induce the recruitment of both dynactin and kinesin-2 on LE. Most of the LE decorated by overexpressed ORP1L fail to accept endocytosed dextran or EGF, and the transfected cells display defective degradation of internalized EGF. ORP1L silencing in macrophage foam cells enhances endosome motility and results in inhibition of [3H]cholesterol efflux to apolipoprotein A-I. These data demonstrate that LE motility and functions in both protein and lipid transport are regulated by ORP1L.
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      description:ORP1L is an oxysterol binding homologue that regulates late endosome (LE) positioning. We show that ORP1L binds several oxysterols and cholesterol, and characterize a mutant, ORP1L Δ560–563, defective in oxysterol binding. While wild-type ORP1L clusters LE, ORP1L Δ560–563 induces LE scattering, which is reversed by disruption of the endoplasmic reticulum (ER) targeting FFAT motif, suggesting that it is due to enhanced LE–ER interactions. Endosome motility is reduced upon overexpression of ORP1L. Both wild-type ORP1L and the Δ560–563 mutant induce the recruitment of both dynactin and kinesin-2 on LE. Most of the LE decorated by overexpressed ORP1L fail to accept endocytosed dextran or EGF, and the transfected cells display defective degradation of internalized EGF. ORP1L silencing in macrophage foam cells enhances endosome motility and results in inhibition of [3H]cholesterol efflux to apolipoprotein A-I. These data demonstrate that LE motility and functions in both protein and lipid transport are regulated by ORP1L.
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         general
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         Biochemistry
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