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Showing OSBPL3 — ORP3 is a alias.

OSBPL3

Oxysterol-binding protein-related protein 3 · UniProt Q9H4L5

Length
887 aa
Mass
101.2 kDa
Annotated
2026-06-10
26 papers in source corpus 18 papers cited in narrative 18 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

OSBPL3/ORP3 is a PI4P-binding lipid transfer protein that operates at endoplasmic reticulum–plasma membrane (ER-PM) contact sites to couple membrane lipid homeostasis with adhesion signaling and cytoskeletal organization (PMID:32041906, PMID:33857182, PMID:32234213). Its N-terminal PH domain binds PI3K products PI(3,4)P2/PI(3,4,5)P3 and PI(4,5)P2/PI4P to target the plasma membrane, while an FFAT motif and a second FFAT-like motif engage the ER protein VAPA, with ER targeting dominating over PM targeting (PMID:16143324, PMID:25447204, PMID:14593528). The OSBP-related lipid transfer domain (ORD) adopts a helix-grip β-barrel fold whose hydrophobic pocket binds PI4P—but not sterol—and this PI4P-binding activity is the conserved essential function of the domain (PMID:33857182, PMID:32819557). Upon PKC-dependent phosphorylation, often combined with Ca2+ influx, ORP3 forms ORP3-VAPA complexes recruited to ER-PM contacts where it extracts PI4P from the plasma membrane in exchange for phosphatidylcholine, lowering PM PI4P and modulating store-operated Ca2+ entry (PMID:25447204, PMID:32041906, PMID:32234213). Through these complexes ORP3 activates R-Ras/Akt signaling and regulates β1-integrin-dependent adhesion and actin organization (PMID:18270267, PMID:25447204); it also forms a complex with IQSec1 that, upon Ca2+ influx, translocates to contacts adjacent to focal adhesions, allosterically activating the Arf5 GEF activity of IQSec1 to drive focal adhesion disassembly during migration (PMID:32234213). During mitosis, ORP3-mediated PI4P transfer controls PM PI(4,5)P2 levels required for spindle geometry, chromosome segregation, and abscission, and ORP3 interacts with γ-tubulin at centrosomes; loss of ORP3 produces aneuploidy and, in mice, high-penetrance B-cell lymphoma, establishing a tumor-suppressor role [PMID:bio_10.1101_2025.10.22.684039, PMID:37740130, PMID:31659255]. In multiple epithelial cancers ORP3 instead acts pro-tumorigenically, activating RAS/Akt and Hippo-YAP signaling downstream of HIF1A induction (PMID:34584127, PMID:32709922, PMID:41794997). ORP3 additionally cooperates with VAPB in PI4P-dependent membrane trafficking and participates with VAP-A and Rab7 in nuclear envelope invaginations exploited by HIV-1 (PMID:26812496, PMID:37563144).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2003 Medium

    Established the basic subcellular partitioning of ORP3, defining it as a dual-targeted protein before any transfer or signaling function was known.

    Evidence Truncation constructs with fractionation and fluorescence microscopy in cultured cells

    PMID:14593528

    Open questions at the time
    • No molecular determinant of ER versus PM partitioning identified
    • No lipid ligand or transport function tested
  2. 2005 High

    Resolved how ORP3 reaches each membrane, showing PH-domain phosphoinositide binding directs PM targeting and an FFAT motif directs VAP-A-dependent ER targeting that dominates.

    Evidence Point/truncation mutants, lipid-binding assays, and co-overexpression imaging in cells

    PMID:16143324

    Open questions at the time
    • Did not establish lipid transfer activity at contact sites
    • Physiological trigger for relative targeting unknown
  3. 2008 High

    Linked ORP3 to adhesion signaling by identifying R-Ras as a partner and tying ORP3 to β1-integrin activity, actin organization, and adhesion-coupled phosphorylation.

    Evidence Co-IP, RNAi and overexpression with integrin and phagocytosis phenotypes in HEK293 and macrophages

    PMID:18270267

    Open questions at the time
    • Kinase responsible for adhesion-dependent phosphorylation not identified
    • Connection between lipid binding and R-Ras regulation not established
  4. 2014 High

    Defined the phospho-switch controlling ORP3 function: hyperphosphorylation drives VAPA association via two FFAT-type motifs, and ORP3-VAPA complexes activate R-Ras/Akt and integrin signaling at PM contact sites.

    Evidence Fractionation, reciprocal Co-IP, FFAT/FFAT-like mutagenesis, PMA stimulation, R-Ras and Akt assays in cells

    PMID:25447204

    Open questions at the time
    • Identity of the responsible kinase not pinned down
    • Mechanistic link from PI4P transfer to R-Ras activation unresolved
  5. 2016 Medium

    Showed ORP3 cooperates with VAPB to regulate PI4P levels and ERGIC-to-nuclear-envelope trafficking, providing a disease-relevant rescue of ALS-linked VAPB-P56S.

    Evidence ORP3 overexpression rescue and knockdown, PI4P measurement, Emerin trafficking and detergent solubility assays

    PMID:26812496

    Open questions at the time
    • Direct lipid transfer at this site not demonstrated
    • Generalizability beyond VAPB-P56S overexpression unclear
  6. 2020 High

    Demonstrated direct PI4P/lipid exchange activity and a Ca2+/PKC-triggered translocation mechanism, and connected ORP3 to IQSec1/Arf5 GEF activation driving focal adhesion disassembly.

    Evidence Co-IP, live imaging, in vitro lipid exchange and GEF assays, SOCE measurements, biosensors, and focal adhesion disassembly assays across multiple studies

    PMID:32041906 PMID:32234213

    Open questions at the time
    • Stoichiometry and structural basis of the ORP3-IQSec1 complex not defined
    • How lipid exchange and GEF activation are coordinated mechanistically unresolved
  7. 2020 High

    Provided the structural basis for ligand selectivity, showing the ORD binds PI4P but not sterol due to a narrow tunnel, and that PI4P binding is the conserved essential function.

    Evidence X-ray crystallography of apo and PI4P-bound ORD, binding-site mutagenesis, and yeast OSH complementation

    PMID:32819557 PMID:33857182

    Open questions at the time
    • Structure of full-length protein with PH and FFAT regions not solved
    • Counter-transported lipid not captured structurally
  8. 2019 High

    Established ORP3 as a tumor suppressor whose loss causes aneuploidy and B-cell lymphoma, linking its lipid function to genome stability.

    Evidence Orp3 knockout mice with lymphoma histopathology, phospholipid metabolomics, aneuploidy assays, and human fibroblast transformation

    PMID:31659255

    Open questions at the time
    • Molecular route from phospholipid dysregulation to aneuploidy not defined at the time
    • Cell-of-origin and tumor driver events incompletely mapped
  9. 2023 Medium

    Connected ORP3's genome-stability role to the centrosome via γ-tubulin interaction and extended the tumor-suppressor phenotype to bladder carcinoma.

    Evidence Co-IP/pulldown with γ-tubulin, actin co-localization, aneuploidy assays, and tissue-specific KO carcinogenesis mouse model

    PMID:37740130

    Open questions at the time
    • Functional consequence of the γ-tubulin interaction for centrosome biology not mechanistically resolved
    • Single-lab interaction without reciprocal structural mapping
  10. 2023 High

    Revealed an unexpected ORP3 role in viral pathogenesis through a hyperphosphorylated ORP3-VAP-A-Rab7 (VOR) complex driving nuclear envelope invaginations used by HIV-1.

    Evidence Co-IP of trimeric complex, siRNA silencing, NEI imaging, and HIV-1 infection assays in HeLa and CD4+ T cells

    PMID:37563144

    Open questions at the time
    • Direct contribution of ORP3 lipid transfer activity to NEI formation not isolated
    • How Rab7 is incorporated into the VAP-A/ORP3 complex structurally unclear
  11. 2021 Medium

    Showed that in epithelial cancers OSBPL3 acts pro-tumorigenically by activating R-Ras/Akt, and that it is transcriptionally induced by HIF1A under hypoxia.

    Evidence siRNA/xenograft, active Ras pull-down, Akt western blot in gastric cancer; ChIP and promoter reporter for HIF1A in colorectal cancer

    PMID:32709922 PMID:34584127

    Open questions at the time
    • Reconciliation of pro-tumorigenic epithelial role with tumor-suppressor lymphoid role unresolved
    • Whether lipid transfer activity is required for cancer-promoting signaling not tested
  12. 2026 Medium

    Expanded the oncogenic signaling repertoire of OSBPL3 to Hippo-YAP, NFE2L2/PLAU glycolytic, and NOTCH stemness axes across colorectal, lung, and pancreatic cancers.

    Evidence Co-IP with 14-3-3, NFE2L2; nuclear translocation, transcription, glycolysis and lipidomics assays; organoid and xenograft drug-resistance models

    PMID:41687403 PMID:41794997 PMID:41799203

    Open questions at the time
    • Whether these interactions are direct and lipid-transfer-dependent not established
    • Mechanistic unification of multiple downstream pathways in a single cell type lacking
  13. 2025 High

    Placed ORP3-mediated PI4P transfer directly in mitotic control, showing it regulates PM PI(4,5)P2, spindle geometry, chromosome segregation, and abscission via VAPA-dependent recruitment.

    Evidence PI4P/PI(4,5)P2 biosensor imaging, ORP3 KD/KO, VAPA-binding-motif phospho-mutants, and mitotic/abscission assays (preprint)

    PMID:bio_10.1101_2025.10.22.684039

    Open questions at the time
    • Preprint not yet peer-reviewed
    • Direct mechanistic link between PI(4,5)P2 levels and spindle defects not fully resolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how the same PI4P-transfer activity produces opposing tumor-suppressor (genome stability) and oncogenic (RAS/YAP/NOTCH signaling) outcomes in different tissues.
  • Context-specificity of ORP3 function across cell types not mechanistically explained
  • Whether lipid-transfer activity versus scaffolding drives each outcome unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008289 lipid binding 6 GO:0060089 molecular transducer activity 3 GO:0060090 molecular adaptor activity 3 GO:0140104 molecular carrier activity 3 GO:0098772 molecular function regulator activity 1
Localization
GO:0005886 plasma membrane 5 GO:0005783 endoplasmic reticulum 4 GO:0005635 nuclear envelope 2 GO:0005815 microtubule organizing center 1 GO:0005829 cytosol 1
Pathway
R-HSA-162582 Signal Transduction 5 R-HSA-1430728 Metabolism 4 R-HSA-1640170 Cell Cycle 3 R-HSA-1643685 Disease 3 R-HSA-1500931 Cell-Cell communication 2
Partners
14-3-3GAMMA-TUBULINIQSEC1NFE2L2R-RASRAB7VAPAVAPB
Complex memberships
ORP3-IQSec1 complexORP3-VAPA complexVOR complex (VAP-A/ORP3/Rab7)

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2008 ORP3 interacts with R-Ras (a small GTPase regulating cell adhesion) as demonstrated by co-immunoprecipitation. Gene silencing of ORP3 in HEK293 cells alters actin cytoskeleton organization, impairs cell-cell adhesion, enhances cell spreading, and increases β1 integrin activity—effects mimicking constitutively active R-Ras(38V). Overexpression of ORP3 leads to polarized cell-surface protrusions, impaired cell spreading, and decreased β1 integrin activity. In macrophages, ORP3 overexpression causes disappearance of podosomes and decreased phagocytosis. ORP3 is phosphorylated when cells lose adhesive contacts, indicating regulation by outside-in adhesion receptor signals. Co-immunoprecipitation, gene silencing (RNAi), overexpression, actin cytoskeleton imaging, β1 integrin activity assay, phagocytosis assay Journal of cell science High 18270267
2005 The PH domain of ORP3 binds PI3K products PI(3,4)P2 and PI(3,4,5)P3, and together with flanking sequences is required for plasma membrane targeting. An FFAT motif (EFFDAxE) mediates interaction with VAP-A and is required for ER targeting; FFAT-mediated ER targeting dominates over PH domain-mediated PM targeting. Co-overexpression of ORP3 with VAP-A induces stacked ER membrane structures (OSER). Lipid starvation promotes formation of dilated peripheral ER (DPER) structures dependent on ORP3. Truncation and point-mutant constructs, fluorescence microscopy, lipid-binding assays, co-overexpression imaging Experimental cell research High 16143324
2014 Hyperphosphorylated ORP3 selectively interacts with ER membrane protein VAPA; ORP3-VAPA complexes are targeted to plasma membrane contact sites via the ORP3 PH domain. A novel FFAT-like motif was identified in ORP3; disruption of both FFAT-like and canonical FFAT motifs abolished PMA-stimulated interaction of phospho-ORP3 with VAPA. Co-expression of ORP3 and VAPA induces R-Ras activation, and downstream Akt(S473) phosphorylation and β1-integrin activity are enhanced by ORP3-VAPA. Thus, ORP3 phosphorylation controls VAPA association and ORP3-VAPA complexes stimulate R-Ras signaling. Biochemical fractionation, co-immunoprecipitation, cell imaging, FFAT/FFAT-like motif mutagenesis, PMA stimulation, R-Ras activation assay, Akt phosphorylation western blot, β1-integrin activity assay Experimental cell research High 25447204
2003 ORP3 protein is distributed between cytosol and ER membranes, with a minor portion at the plasma membrane. The N-terminal PH domain-containing region strongly targets to the plasma membrane, while the C-terminal half remains largely cytosolic, as established by truncation constructs in cultured cells. Truncated construct expression, subcellular fractionation, fluorescence microscopy Cell and tissue research Medium 14593528
2020 IQSec1 forms a complex with the lipid transfer protein ORP3. Ca2+ influx via STIM1/Orai1 channels triggers PKC-dependent translocation of the IQSec1-ORP3 complex to ER/plasma membrane contact sites adjacent to focal adhesions. ORP3 allosterically activates IQSec1 (a GEF for Arf5) and also extracts PI4P from the plasma membrane in exchange for phosphatidylcholine. Both the IQSec1-activating and the lipid-exchange activities of ORP3 are required for focal adhesion disassembly during cell migration. Co-immunoprecipitation, live cell imaging of complex translocation, lipid exchange assay, GEF activity assay, focal adhesion disassembly assay, Ca2+ channel manipulation eLife High 32234213
2020 PKC activation (especially combined with Ca2+ increases) triggers ORP3 translocation to the plasma membrane, determined by both PI(4,5)P2 and PI4P. Upon activation, ORP3 efficiently extracts PI4P and to a lesser extent phosphatidic acid from the PM, and slightly increases PM cholesterol levels. Full ORP3 activation decreases PM PI4P levels and inhibits store-operated Ca2+ entry (SOCE). The C-terminal region following the lipid transfer domain is critical for proper localization and function. Live cell imaging, lipid biosensor assays, PI4P extraction assay, store-operated Ca2+ entry measurements, C-terminal deletion constructs Journal of cell science High 32041906
2016 ORP3 overexpression rescues the ALS-linked VAPB-P56S mutant phenotype: it resolves mutant VAPB-induced membrane expansions, restores solubility of mutant VAPB in non-ionic detergent, and restores Emerin trafficking to the nuclear envelope. Knockdown of ORP3 (or VAPB) increases intracellular PI4P levels. Reducing PI4P synthesis reduces the severity of VAPB-P56S-induced membrane expansions and restores Emerin trafficking, indicating that ORP3 and VAPB cooperatively regulate ERGIC-to-nuclear envelope trafficking by modulating PI4P levels. ORP3 overexpression rescue assay, ORP3 knockdown, PI4P level measurement, Emerin trafficking assay, non-ionic detergent solubility assay Experimental cell research Medium 26812496
2021 Crystal structure of the ORP3 ORD (OSBP-related domain) at 2.6–2.7 Å resolution in apo and PI(4)P-bound forms reveals a helix-grip β-barrel fold with a deep hydrophobic pocket conserved across the OSBP family. ORP3 binds PI4P via residues around the tunnel entrance and hydrophobic pocket but lacks sterol-binding capacity due to a narrow hydrophobic tunnel. The ORP3 ORD (and OSBP1 ORD) rescues lethality of yeast OSH1-7 knockout, but a PI4P-binding site mutant of ORP3 ORD does not complement, establishing that PI4P-binding by the ORD is the conserved essential function. X-ray crystallography (2.6–2.7 Å), PI4P-binding site mutagenesis, yeast OSH knockout complementation assay PloS one High 33857182
2020 Crystal structure of the human ORP3 ORD at 2.1 Å (apo) and 3.2 Å (PI4P complex) confirms PI4P as a ligand and demonstrates conservation of the PI4P-binding mode across the ORP family. In vitro binding assay confirms PI4P binding by ORP3. X-ray crystallography (2.1 Å and 3.2 Å), in vitro lipid-binding assay Biochemical and biophysical research communications High 32819557
2023 In HIV-1-infected HeLa cells and activated CD4+ T cells, Rab7+ late endosomes promote nuclear envelope invagination (NEI) formation through a VOR complex composed of outer nuclear membrane protein VAP-A, hyperphosphorylated ORP3, and Rab7. Silencing VAP-A or ORP3, or drug-mediated impairment of Rab7 binding to ORP3-VAP-A, inhibited nuclear transfer of HIV-1 components and productive infection. In HIV-1-resistant quiescent CD4+ T cells, ORP3 was not hyperphosphorylated and the VOR complex and NEIs were not formed. Co-immunoprecipitation of VAP-A/ORP3/Rab7 complex, siRNA silencing, live imaging of nuclear envelope invaginations, HIV-1 infection assay, phosphorylation state analysis Nature communications High 37563144
2019 Knockout of Orp3 in mice results in aberrant expansion of lymphoid progenitor cells and high-penetrance formation of chromosomally unstable, pauci-clonal B-cell lymphoma in aging animals. Pre-tumorous lymphoid cells from Orp3 knockout mice exhibit deregulated phospholipid metabolism and aberrant induction of proliferation-regulating pathways, associated with increased aneuploidy in hematopoietic progenitor cells. ORP3 knockdown also enhances malignant transformation of human fibroblasts. Mouse Orp3 knockout, flow cytometry of lymphoid progenitors, B-cell lymphoma histopathology, phospholipid metabolomics, aneuploidy assays, human fibroblast transformation assay Oncogene High 31659255
2023 ORP3 protein interacts with γ-tubulin at centrosomes and with components of the actin cytoskeleton. Altering ORP3 expression in telomerase-immortalized urothelial cells induces aneuploidy and genomic instability. ORP3 loss increases incidence of invasive bladder carcinoma in tissue-specific knockout mice (BBN model) and influences migration and invasive capacity of bladder cancer cell lines. Co-immunoprecipitation/pulldown of ORP3 with γ-tubulin, actin cytoskeleton co-localization, ORP3 KO/KD with aneuploidy assays, tissue-specific knockout mouse carcinogenesis model Cellular and molecular life sciences : CMLS Medium 37740130
2021 OSBPL3 knockdown in gastric cancer cells reduces cell growth in vitro and in vivo by inhibiting cell cycle progression. Active Ras pull-down assay and western blotting demonstrate that OSBPL3 activates the R-Ras/Akt signaling pathway in gastric cancer cells. siRNA knockdown, xenograft tumor model, active Ras pull-down assay, western blot for Akt phosphorylation, cell cycle analysis Scientific reports Medium 34584127
2020 HIF1A binds the hypoxia response element (HRE) in the OSBPL3 promoter under hypoxia, transcriptionally upregulating OSBPL3 expression. OSBPL3 in turn promotes colorectal cancer progression through activation of the RAS signaling pathway. Chromatin immunoprecipitation (ChIP) of HIF1A on OSBPL3 HRE, promoter reporter assay, OSBPL3 overexpression/knockdown with RAS pathway western blot, in vitro and in vivo tumor models Cell death & disease Medium 32709922
2026 OSBPL3 binds 14-3-3 proteins to promote YAP1 nuclear translocation, activating downstream Hippo-YAP oncogenic pathways in colorectal cancer. Depleting OSBPL3 impairs proliferation, invasion, and cell cycle progression. Tumors with high OSBPL3 expression are resistant to MEK inhibitors, but this resistance is overcome by YAP1 suppression or combined YAP/MEK inhibition. Co-immunoprecipitation of ORP3 with 14-3-3 proteins, YAP1 nuclear translocation assay, OSBPL3 KD/OE with proliferation and invasion readouts, patient-derived organoid drug resistance assay Communications biology Medium 41794997
2026 OSBPL3 interacts with transcription factor NFE2L2 and promotes its nuclear translocation, enhancing transcriptional activation of PLAU. Upregulation of PLAU stimulates key glycolytic enzymes through PI3K/AKT pathway activation, increasing glucose consumption and lactate secretion to drive LUAD progression. Co-immunoprecipitation of OSBPL3 with NFE2L2, NFE2L2 nuclear translocation assay, PLAU promoter transcription assay, glycolytic metabolite measurement, AKT inhibitor rescue, in vivo xenograft Translational oncology Medium 41687403
2026 OSBPL3 promotes pancreatic cancer cell proliferation, stemness, migration, invasion, and chemoresistance. Increased OSBPL3 expression is associated with enrichment of cholesterol esters and steroid metabolites. NOTCH pathway activation mediates OSBPL3-driven drug resistance and stemness, as NOTCH pathway inhibition attenuates these phenotypes in vivo. OSBPL3 KD/OE functional assays, mass spectrometry lipid profiling, NOTCH pathway inhibitor rescue, in vivo mouse models Theranostics Medium 41799203
2025 ORP3 transfers PI4P from the plasma membrane to the ER at ER-PM contact sites during mitosis. ORP3 defects alter PM PI4P and PI(4,5)P2 distributions, actin cytoskeleton distribution, mitotic spindle geometry, chromosome segregation, and abscission, leading to multinucleated cells and aneuploidy. The mitotic function of ORP3 requires VAPA and phosphorylation of the ORP3 VAPA-binding motif, which recruits ORP3 to the ER to prime PI4P transfer. ORP3 also prevents PI4P accumulation at the cytoplasmic bridge during abscission. Live cell imaging of PI4P/PI(4,5)P2 biosensors, ORP3 knockdown/knockout, VAPA interaction assay, phospho-mimetic/phospho-dead FFAT motif mutants, mitotic spindle and chromosome segregation assays, cytokinesis abscission assay bioRxivpreprint High bio_10.1101_2025.10.22.684039

Source papers

Stage 0 corpus · 26 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2008 The R-Ras interaction partner ORP3 regulates cell adhesion. Journal of cell science 79 18270267
2005 Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants. Experimental cell research 77 16143324
2014 OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity. Experimental cell research 74 25447204
2020 Calcium-stimulated disassembly of focal adhesions mediated by an ORP3/IQSec1 complex. eLife 60 32234213
2003 Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7. Cell and tissue research 51 14593528
2020 ORP3 phosphorylation regulates phosphatidylinositol 4-phosphate and Ca2+ dynamics at plasma membrane-ER contact sites. Journal of cell science 43 32041906
2021 Oxysterol binding protein-like 3 (OSBPL3) is a novel driver gene that promotes tumor growth in part through R-Ras/Akt signaling in gastric cancer. Scientific reports 25 34584127
2020 Upregulation of OSBPL3 by HIF1A promotes colorectal cancer progression through activation of RAS signaling pathway. Cell death & disease 21 32709922
2003 ORP3 splice variants and their expression in human tissues and hematopoietic cells. DNA and cell biology 18 12590732
2001 ORP-3, a human oxysterol-binding protein gene differentially expressed in hematopoietic cells. Blood 18 11568019
2019 Aneuploidy-inducing gene knockdowns overlap with cancer mutations and identify Orp3 as a B-cell lymphoma suppressor. Oncogene 17 31659255
2023 HIV-1-induced nuclear invaginations mediated by VAP-A, ORP3, and Rab7 complex explain infection of activated T cells. Nature communications 15 37563144
2016 Oxysterol-binding protein ORP3 rescues the Amyotrophic Lateral Sclerosis-linked mutant VAPB phenotype. Experimental cell research 15 26812496
2021 Structure of human ORP3 ORD reveals conservation of a key function and ligand specificity in OSBP-related proteins. PloS one 13 33857182
2021 Clinical Value and Potential Mechanisms of Oxysterol-Binding Protein Like 3 (OSBPL3) in Human Tumors. Frontiers in molecular biosciences 11 34738015
2020 The crystal structure of ORP3 reveals the conservative PI4P binding pattern. Biochemical and biophysical research communications 10 32819557
2020 Downregulation of ORP3 Correlates with Reduced Survival of Colon Cancer Patients with Advanced Nodal Metastasis and of Female Patients with Grade 3 Colon Cancer. International journal of molecular sciences 10 32824360
2023 Loss of ORP3 induces aneuploidy and promotes bladder cancer cell invasion through deregulated microtubule and actin dynamics. Cellular and molecular life sciences : CMLS 9 37740130
2024 ENST00000534735 inhibits proliferation and migration, promotes apoptosis and pyroptosis of endometrial cancer via OSBPL3 through APMK/SIRT1/NF-κB pathway. Heliyon 7 38370231
2025 OSBPL3 modulates the immunosuppressive microenvironment and predicts therapeutic outcomes in pancreatic cancer. Biology direct 5 39789613
2026 OSBPL3 promotes LUAD metastasis and glycolysis through transcriptional upregulation of PLAU via NFE2L2. Translational oncology 0 41687403
2026 OSBPL3 drives colorectal cancer progression via Hippo-YAP signaling and modulates MEK inhibitor sensitivity. Communications biology 0 41794997
2026 OSBPL3-driven sterol metabolic reprogramming promotes oncogenic signaling and therapeutic resistance in pancreatic cancer. Theranostics 0 41799203
2026 OSBPL3 promotes colorectal cancer progression through modulation of TGF-β signaling and immune cell infiltration. Translational cancer research 0 42180901
2025 Hsa-miR-181a-5p Enhances the Chemosensitivity of Breast Cancer Cells to Tamoxifen by Regulation of the OSBPL3/RAS Signaling Pathway. Cureus 0 41267704
2025 Exploring the potential mechanisms of OSBPL3 in metabolic dysfunction-associated steatotic liver disease by integrating bulk and single-cell RNA sequencing data. Medicine 0 41466006

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