| 2010 |
ORP11 localizes to the Golgi complex and late endosomes (co-localizing with GFP-Rab9, TGN46, GFP-Rab7, and a medial-trans-Golgi marker), and the N-terminal fragment (aa 1-292) contains the membrane-targeting determinants. The C-terminal ligand-binding domain (aa 273-747) is cytosolic. |
Fluorescence microscopy with GFP-tagged organelle markers, subcellular fractionation, overexpression of truncation mutants in HEK293 cells |
Experimental cell research |
Medium |
20599956
|
| 2010 |
ORP11 forms a heterodimer with ORP9 via interaction between aa 98-372 of ORP9 and aa 154-292 of ORP11. Overexpressed ORP9 recruits EGFP-ORP11 to membranes, and ORP9 silencing inhibits ORP11 Golgi association, establishing the ORP9-ORP11 dimer as a functional unit. |
Yeast two-hybrid screen, overexpression and co-localization in HEK293 cells, ORP9 siRNA silencing |
Experimental cell research |
Medium |
20599956
|
| 2007 |
ORP11 (via its ORD domain) binds 25-hydroxycholesterol in live cells, as shown by photo-cross-linking with [3H]photo-25OH, indicating it is a sterol-binding protein with a conserved ligand-binding pocket. |
In vitro [3H]25OH-binding assay with recombinant proteins; live cell photo-cross-linking with [3H]photo-25OH in COS7 cells |
The Biochemical journal |
Medium |
17428193
|
| 2022 |
Upon lysosomal membrane permeabilization (LMP), ORP11 (along with ORP9, ORP10, and OSBP) is recruited to damaged lysosomes via lysosomal phosphatidylinositol-4-phosphate generated by PI4K2A, forming new ER-lysosome membrane contact sites that mediate ER-to-lysosome transfer of phosphatidylserine and cholesterol to support lysosomal repair. |
Unbiased proteomics of damaged lysosomes, live imaging, functional lipid transport assays, LMP induction in cell culture |
Nature |
High |
36071159
|
| 2023 |
ORP11 (with ORP9) localizes at ER-trans-Golgi network contact sites via interaction between ORP9's tandem α-helices and ORP10/ORP11. The ORP9-ORP11 complex extracts PI4P from the TGN to prevent its overaccumulation, thereby suppressing OSBP-mediated cholesterol transport to the Golgi. |
Genetic knockout, live fluorescence imaging, lipid mass spectrometry, epistasis experiments in cells depleted of ORP9 and/or GRAMD1s |
Nature communications |
High |
37735529
|
| 2024 |
The ORP9-ORP11 heterodimer localizes at ER-trans-Golgi membrane contact sites and exchanges phosphatidylserine (PS) for phosphatidylinositol-4-phosphate (PI(4)P) between the two organelles. Loss of either ORP9 or ORP11 causes phospholipid imbalances in the Golgi that result in lowered sphingomyelin synthesis. |
Gene knockout library targeting 90 LTPs, whole-cell lipidomics, co-localization imaging, lipid transfer assays |
eLife |
High |
39106189
|
| 2019 |
ORP11 knockdown in RAW264.7 macrophages abrogates the protective action of bis(monoacylglycero)phosphate (BMP) against oxidized LDL-induced apoptosis, causes accumulation of free cholesterol, decreases cholesterol efflux, and reduces ABCG1 expression, demonstrating that ORP11 cooperates with BMP in intracellular cholesterol trafficking at the late endosome. |
Stable shRNA knockdown in RAW264.7 macrophages, lipidomics (oxysterol measurement), cholesterol efflux assays, western blotting for ABCG1 |
Biochimica et biophysica acta. Molecular and cell biology of lipids |
Medium |
31136841
|
| 2012 |
ORP11 silencing in differentiating SGBS adipocytes reduces adiponectin and aP2 mRNA expression and markedly decreases cellular triglyceride storage, demonstrating a functional role for ORP11 in adipocyte differentiation and lipid accumulation. |
siRNA knockdown during SGBS adipocyte differentiation, qRT-PCR, triglyceride content measurement |
PloS one |
Medium |
23028956
|
| 2025 |
OSBPL11 knockdown accelerates mitotic slippage and represses cell death during mitotic arrest (induced by the Eg5 inhibitor STLC or paclitaxel), with decreased cyclin B1 levels in knockdown mitotic cells. Rescue with wild-type OSBPL11 but not lipid transport/binding mutants restores normal cell fate, and the APC/C inhibitor proTAME reverses the knockdown phenotype, placing OSBPL11's lipid transport activity upstream of APC/C-mediated cyclin B1 degradation. |
siRNA knockdown, rescue with wild-type and mutant OSBPL11, cyclin B1 immunoblotting, APC/C inhibition with proTAME, cell fate tracking |
Biochemical and biophysical research communications |
Medium |
41313943
|
| 2025 |
In vitro binding assays and molecular docking showed that OSBPL11 is a vitamin D binding protein capable of binding vitamin D metabolites (25-hydroxyvitamin D). OSBPL11 knockdown in mice results in increased fat mass, reduced triglycerides, and improved glucose tolerance. |
In vitro binding assays, molecular docking, OSBPL11 knockdown mouse model with metabolic phenotyping |
medRxiv (preprint) / Inflammation |
Low |
40492082
|
| 2017 |
Homozygous Arg171Trp variant in OSBPL11 causes intracellular cholesterol accumulation in skin fibroblasts and skin biopsy cells, demonstrating that functional OSBPL11 is required for normal intracellular cholesterol distribution. This effect was also seen in a clinically unaffected sibling homozygous for the variant, suggesting OSBPL11 loss-of-function causes a cholesterol trafficking defect without overt neurological disease. |
Filipin staining for free cholesterol in skin fibroblasts and biopsies from patients and carrier sibling with homozygous OSBPL11 variant |
European journal of human genetics |
Medium |
28051070
|