ArticleThe Journal of biological chemistry2014
Oxysterol-binding protein (OSBP)-related protein 4 (ORP4) is essential for cell proliferation and survival.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 96 citations in OpenAlex.
- Organelle contact sites in cancer cells.Cell death & disease · 2026Review
- Role of Oxysterol-Binding Protein Family in Cholesterol Metabolism and Cancer Progression: A Review.Medical science monitor : international medical journal of experimental and clinical research · 2026Review
- A multiomics recovery factor predicts long COVID in the IMPACC study.The Journal of clinical investigation · 2025Article
- OSBPL2 deficiency inhibits Rho/ROCK2/p-ERM signaling and impairs actin cytoskeletal regulation in auditory cells.Journal of biomedical research · 2025Article
- Anti-SARS-CoV-2 Small Molecule Targeting of Oxysterol-Binding Protein (OSBP) Activates Cellular Antiviral Innate Immunity.ACS infectious diseases · 2025Article
- Orpinolide disrupts a leukemic dependency on cholesterol transport by inhibiting OSBP.Nature chemical biology · 2025Article
- Anthropogenic noise exposure suppresses the immune response inFrontiers in immunology · 2025Article
- Comprehensive analysis of plasma cell heterogeneity and immune interactions in multiple myeloma.Frontiers in immunology · 2025Article
- Dysregulation of PI4P in the trans Golgi regions activates the mammalian Golgi stress response.The Journal of biological chemistry · 2025Article
- Enzymatically Formed Oxysterols and Cell Death.Advances in experimental medicine and biology · 2024Review
- Regulation of cellular cholesterol distribution via non-vesicular lipid transport at ER-Golgi contact sites.Nature communications · 2023Article
- Integrated bioinformatics analysis reveals the function and prognostic value of OSBPL3 in hepatocellular carcinoma.Heliyon · 2023Article
- Structure-Activity Relationships of Ligand Binding to Oxysterol-Binding Protein (OSBP) and OSBP-Related Protein 4.Journal of medicinal chemistry · 2023Article
- Review
- Roles of Phosphatidylinositol 4-Phosphorylation in Non-vesicular Cholesterol Trafficking.Advances in experimental medicine and biology · 2023Article
- The relationships of OSBPL3 expression with KI-67 expression and KRAS mutations in CRC: implications for diagnosis and prognosis.BMC medical genomics · 2022Article
- An acquired phosphatidylinositol 4-phosphate transport initiates T-cell deterioration and leukemogenesis.Nature communications · 2022Article
- Linking Late Endosomal Cholesterol with Cancer Progression and Anticancer Drug Resistance.International journal of molecular sciences · 2022Review
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Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) comprise a large gene family with sterol/lipid transport and regulatory activities. ORP4 (OSBP2) is a closely related paralogue of OSBP, but its function is unknown. Here we show that ORP4 binds similar sterol and lipid ligands as OSBP and other ORPs but is uniquely required for the proliferation and survival of cultured cells. Recombinant ORP4L and a variant without a pleckstrin homology (PH) domain (ORP4S) bind 25-hydroxycholesterol and extract and transfer cholesterol between liposomes. Two conserved histidine residues in the OSBP homology domain ORP4 are essential for binding phosphatidylinositol 4-phosphate but not sterols. The PH domain of ORP4L also binds phosphatidylinositol 4-phosphate in the Golgi apparatus. However, in the context of ORP4L, the PH domain is required for normal organization of the vimentin network. Unlike OSBP, RNAi silencing of all ORP4 variants (including a partial PH domain truncation termed ORP4M) in HEK293 and HeLa cells resulted in growth arrest but not cell death. ORP4 silencing in non-transformed intestinal epithelial cells (IEC)-18 caused apoptosis characterized by caspase 3 and poly(ADP-ribose) polymerase processing, DNA cleavage, and JNK phosphorylation. IEC-18 transformed with oncogenic H-Ras have increased expression of ORP4L and ORP4S proteins and are resistant to the growth-inhibitory effects of ORP4 silencing. Results suggest that ORP4 promotes the survival of rapidly proliferating cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.