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Showing OSBPL8 — ORP8 is a alias.

OSBPL8

Oxysterol-binding protein-related protein 8 · UniProt Q9BZF1

Length
889 aa
Mass
101.2 kDa
Annotated
2026-06-10
23 papers in source corpus 18 papers cited in narrative 18 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

OSBPL8 (ORP8) is an ER-anchored lipid transfer protein that establishes and exploits membrane contact sites to countertransport phospholipids and thereby control plasma membrane lipid identity, organelle physiology, and lipid catabolism (PMID:26206935, PMID:27113756). Anchored in the ER through a C-terminal transmembrane span, it tethers the ER to the plasma membrane via a PH domain that engages PM phosphoinositides, while its OSBP-related domain (ORD) extracts and exchanges phosphatidylserine for PI4P, delivering PI4P to ER Sac1 for degradation and enriching PS at the PM (PMID:26206935, PMID:28970484). The ORD adopts a β-barrel fold with a large lipid-binding cavity whose lid stabilizes cargo and tunes the relative transport efficiency of PS versus PI4P (PMID:37566053). At ER–plasma membrane junctions ORP8 sets a high PI4P/PS ratio that, opposite ORP5, governs STIM1–Orai1 coupling, Ca2+ oscillations, and downstream NFAT translocation (PMID:37607230), and the same exchange activity acts downstream of Sec22b tethering at ER–phagosome contacts to control phagosome maturation and antigen degradation (PMID:37794132). Beyond the PM, ORP8 localizes to ER–mitochondria contacts where it binds PTPIP51 and maintains mitochondrial morphology and respiration (PMID:27113756), and it organizes phosphatidic-acid–rich MAM subdomains to recruit seipin and drive lipid droplet biogenesis (PMID:35969857). Independently of its transfer activity, ORP8 serves as a lipophagy receptor on lipid droplets by directly binding LC3/GABARAPs in an AMPK-phosphorylation–dependent manner, controlling triglyceride clearance in vivo (PMID:37707322). ORP8 also recruits GPX1 to the ER to reduce peroxidized phosphatidic acid as part of a noncanonical, ER-localized ferroptosis pathway (PMID:41720096), and at the nuclear envelope it interacts with Nup62 to modulate SREBP-driven lipid biosynthesis (PMID:21698267).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2007 Medium

    Established ORP8 as an ER-resident oxysterol-binding protein and linked it to cholesterol homeostasis by showing it negatively regulates ABCA1-dependent cholesterol efflux.

    Evidence siRNA knockdown in THP-1 macrophages with ABCA1 promoter-luciferase reporters, cholesterol efflux and ligand binding assays

    PMID:17991739

    Open questions at the time
    • Mechanism connecting ER-localized ORP8 to ABCA1 transcription not resolved
    • Direct lipid transfer activity not yet demonstrated
  2. 2011 Medium

    Identified Nup62 as a direct partner and connected ORP8 to SREBP-controlled lipogenesis, providing a nuclear-envelope route by which ORP8 suppresses cholesterol biosynthesis.

    Evidence Yeast two-hybrid, BiFC, Co-IP, adenoviral overexpression in mouse liver with [3H]acetate labeling and Nup62 RNAi

    PMID:21698267

    Open questions at the time
    • How ORP8-Nup62 binding mechanistically lowers nuclear SREBP is unclear
    • Lipid-transfer dependence of the SREBP effect not tested
  3. 2012 Medium

    Showed ORP8 controls macrophage migration through the same Nup62 partner, competing with Exo70 and placing Nup62 downstream of ORP8.

    Evidence Stable shRNA knockdown, microarray, migration assays and Nup62 RNAi epistasis in RAW264.7 cells

    PMID:22683860

    Open questions at the time
    • Direct biochemistry of ORP8/Exo70/Nup62 competition not structurally defined
    • Link between migration and lipid transfer activity untested
  4. 2014 Medium

    Linked ORP8 to cell-cycle control by identifying SPAG5/Astrin as a partner recruited to ER membranes and mediating oxysterol-induced G2/M arrest.

    Evidence Yeast two-hybrid, pulldown/Co-IP, flow cytometry cell-cycle analysis and RNAi epistasis in HepG2 cells

    PMID:24424245

    Open questions at the time
    • Mechanism by which ER-tethered SPAG5 alters the cell cycle unknown
    • Relationship to ORP8 lipid-transfer function not addressed
  5. 2015 High

    Defined the core biochemical activity: ORP8 (with ORP5) tethers ER to PM and performs PI4P/PS countertransport, establishing it as a lipid transfer protein that shapes PM phosphoinositide and PS content.

    Evidence In vitro lipid transfer assays, gain/loss-of-function, subcellular fractionation and ER-PM contact imaging

    PMID:26206935

    Open questions at the time
    • In vivo physiological consequences of altered PM PS not yet mapped
    • Structural basis of cargo selectivity not resolved at this stage
  6. 2016 High

    Extended ORP8 function to ER-mitochondria contacts, showing PTPIP51 binding and an ORD requirement for MAM localization with consequences for mitochondrial morphology and respiration.

    Evidence Confocal/EM imaging, reciprocal Co-IP with PTPIP51, domain-deletion analysis and respiration assays with RNAi

    PMID:27113756

    Open questions at the time
    • Lipid species transferred at MAMs not directly demonstrated
    • Causal chain from lipid transfer to respiratory defect unclear
  7. 2017 High

    Refined the recruitment mechanism, showing ORP8's PH domain binds PtdIns(4,5)P2 and that PtdIns(4,5)P2 can serve as a co-exchanger for cargo transport.

    Evidence In vitro lipid extraction/transport with purified ORD, PM recruitment and PH-domain binding assays, double siRNA with lipid measurements

    PMID:28970484

    Open questions at the time
    • Relative in vivo contribution of PI4P vs PIP2 co-exchange not quantified
    • Regulation of PH-domain engagement unknown
  8. 2022 Medium

    Connected ORP8's MAM activity to lipid droplet biogenesis by showing it regulates seipin recruitment at phosphatidic-acid-rich MAM subdomains.

    Evidence Fluorescence microscopy, siRNA knockdown, seipin localization and LD biogenesis quantification with contact-site disruption

    PMID:35969857

    Open questions at the time
    • Direct molecular interaction between ORP8 and seipin not established
    • Lipid flux driving seipin recruitment not measured
  9. 2023 High

    Revealed a transfer-independent role as a lipophagy receptor, with AMPK phosphorylation enhancing direct LC3/GABARAP binding to drive LD autophagy and triglyceride clearance in vivo.

    Evidence Co-IP of ORP8-LC3/GABARAP, AMPK phosphorylation assays, ORP8 KO and ob/ob overexpression mice, lipid-transfer domain mutants

    PMID:37707322

    Open questions at the time
    • Phosphosite-resolved structural basis of LC3 binding not fully defined
    • Coordination between lipophagy and transfer functions on the same LD unclear
  10. 2023 High

    Provided the structural framework for cargo handling by solving the ORD8 β-barrel and showing the lid stabilizes cargo and differentiates PS from PI4P transport.

    Evidence X-ray crystallography, docking and fluorescence lipid transport assays comparing lid-deleted and full-length ORD8

    PMID:37566053

    Open questions at the time
    • Conformational dynamics during membrane extraction not captured
    • Structure of full-length membrane-embedded ORP8 unavailable
  11. 2023 Medium

    Showed ORP8 acts as a rheostat at STIM1-organized ER-PM junctions, setting a high PI4P/PS ratio that tunes store-operated Ca2+ entry and NFAT signaling.

    Evidence Targeted ORD expression, PtdSer-specific PLA1a1, Ca2+ imaging, NFAT translocation and STIM1 interaction measurements

    PMID:37607230

    Open questions at the time
    • Direct ORP8-STIM1 physical relationship not defined
    • Quantitative lipid-ratio thresholds for Ca2+ effects not established
  12. 2023 Medium

    Demonstrated ORP8's PS/PI4P exchange operates at ER-phagosome contacts downstream of Sec22b to control phagosome maturation and antigen degradation.

    Evidence Co-IP of Sec22b-ORP8, siRNA knockdown, phagosomal lipid quantification and rescue with lipid-transfer mutant

    PMID:37794132

    Open questions at the time
    • How Sec22b recruits ORP8 mechanistically unclear
    • Generality across phagocyte types untested
  13. 2026 High

    Uncovered a noncanonical ferroptosis role: ORP8 recruits GPX1 to the ER to reduce peroxidized phosphatidic acid, defining an ER-localized lipid-peroxidation defense distinct from GPX4 at the PM.

    Evidence Co-IP of GPX1-OSBPL8, subcellular fractionation, lipidomics, siRNA knockdown and in vivo tumor growth assays

    PMID:41720096

    Open questions at the time
    • Whether lipid-transfer activity contributes to GPX1 recruitment unclear
    • Interplay with the canonical GPX4 pathway not fully mapped

Open questions

Synthesis pass · forward-looking unresolved questions
  • How ORP8's many spatially distinct functions — PM/MAM/phagosome lipid exchange, lipophagy, GPX1-mediated peroxide defense, and nuclear SREBP control — are coordinated and regulated within a single cell remains unresolved.
  • No unifying regulatory logic for partitioning ORP8 among its sites
  • Post-translational switches beyond AMPK phosphorylation not characterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008289 lipid binding 5 GO:0140104 molecular carrier activity 4 GO:0060090 molecular adaptor activity 3 GO:0042393 histone binding 1
Localization
GO:0005783 endoplasmic reticulum 4 GO:0005886 plasma membrane 3 GO:0005739 mitochondrion 2 GO:0005811 lipid droplet 2 GO:0005635 nuclear envelope 1
Pathway
R-HSA-1430728 Metabolism 3 R-HSA-9609507 Protein localization 2 R-HSA-162582 Signal Transduction 1 R-HSA-5357801 Programmed Cell Death 1 R-HSA-9612973 Autophagy 1
Partners
GABARAPGPX1LC3NUP62PTPIP51SEC22BSPAG5

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2007 ORP8 localizes to the endoplasmic reticulum via its C-terminal transmembrane span and binds 25-hydroxycholesterol, identifying it as an ER oxysterol-binding protein. Silencing ORP8 in THP-1 macrophages increased ABCA1 expression and cholesterol efflux to lipid-free apolipoprotein A-I; the effect was partially attenuated by mutation of the DR4 element in the ABCA1 promoter and synergized with LXR agonist treatment, indicating ORP8 negatively regulates ABCA1 transcription involving both LXR and E-box functions. RNA interference (siRNA), ABCA1 promoter-luciferase reporter assays, cholesterol efflux assays, ligand binding studies The Journal of biological chemistry Medium 17991739
2011 ORP8 binds cholesterol in vitro (in addition to 25-hydroxycholesterol). ORP8 overexpression in mouse liver reduced nuclear SREBP-1 and SREBP-2 and their target gene mRNAs, and suppressed cholesterol biosynthesis. Yeast two-hybrid, BiFC, and co-immunoprecipitation identified nuclear pore component Nup62 as a direct interaction partner of ORP8; ORP8 and Nup62 co-localize at the nuclear envelope, and depletion of Nup62 inhibited the effect of ORP8 overexpression on nSREBPs. In vitro cholesterol binding, adenoviral overexpression in mouse liver, [3H]acetate pulse-labeling, yeast two-hybrid, bimolecular fluorescence complementation (BiFC), co-immunoprecipitation, confocal immunofluorescence, Nup62 RNAi PloS one Medium 21698267
2012 ORP8 silencing in RAW264.7 macrophages increased expression and altered subcellular distribution of its interaction partner Nup62 (including intranuclear localization), enhanced cell migration, and promoted a more pronounced microtubule cytoskeleton. ORP8 competed with Exo70 for binding to Nup62, and Nup62 knockdown abolished the migration-enhancing effect of ORP8 silencing, placing Nup62 downstream of ORP8 in migration control. Stable shRNA lentiviral knockdown, microarray transcriptomics, confocal microscopy, migration assays, Nup62 RNAi epistasis Experimental cell research Medium 22683860
2014 Yeast two-hybrid screening followed by pulldown and co-immunoprecipitation identified SPAG5/Astrin as an interaction partner of ORP8. Overexpressed ORP8 recruited SPAG5 onto ER membranes in interphase cells. ORP8 overexpression or 25-hydroxycholesterol treatment caused G2/M accumulation in HepG2 cells; ORP8 knockdown strongly inhibited the oxysterol-induced G2/M arrest, and SPAG5 knockdown reduced the cell-cycle effects of both ORP8 overexpression and 25-OHC, placing SPAG5 downstream of ORP8. Yeast two-hybrid, pulldown, co-immunoprecipitation, flow cytometry cell cycle analysis, RNAi knockdown epistasis Experimental cell research Medium 24424245
2015 ORP5 and ORP8 are ER integral membrane proteins that tether the ER to the plasma membrane via PH domain interaction with PI4P. Their OSBP-related domains (ORDs) carry either PI4P or phosphatidylserine (PS) and exchange these lipids between bilayers, mediating PI4P/PS countertransport: delivering PI4P to ER-localized Sac1 phosphatase for degradation and PS from ER to PM. Gain- and loss-of-function experiments showed these activities control PM PI4P levels and selectively enrich PS at the PM. Gain- and loss-of-function experiments, lipid transfer assays, subcellular fractionation, imaging of ER-PM contacts Science (New York, N.Y.) High 26206935
2015 ORP8 overexpression triggered apoptosis in HCC cells coinciding with relocation of cytoplasmic Fas to the cell plasma membrane and FasL upregulation. ORP8-induced Fas translocation was p53-dependent, and FasL induction occurred via the ER stress response. ORP8 overexpression in HCC cell lines and primary cells, co-culture with T cells/Jurkat cells, western blot, confocal microscopy, xenograft tumor model The Journal of biological chemistry Medium 25596532
2016 In addition to ER-PM contact sites, ORP5 and ORP8 localize to ER-mitochondria contacts (MAM) and interact physically with the outer mitochondrial membrane protein PTPIP51. A functional lipid transfer (ORD) domain was required for this MAM localization. ORP5/ORP8 depletion caused defects in mitochondria morphology and respiratory function. Confocal and electron microscopy, co-immunoprecipitation with PTPIP51, domain deletion analysis, mitochondrial respiration assays, RNAi knockdown EMBO reports High 27113756
2017 The pleckstrin homology (PH) domain of ORP8 mediates recruitment to ER-PM contact sites via binding to PtdIns(4,5)P2, not PtdIns(4)P. The ORD of ORP8 can extract and transport multiple phosphoinositides in vitro. Knockdown of both ORP5 and ORP8 increases PM PtdIns(4,5)P2 levels with little effect on PtdIns(4)P, indicating PtdIns(4,5)P2 can serve as a co-exchanger for cargo lipid transport by ORP8. In vitro lipid extraction/transport assays with purified ORD, PM recruitment assays, PH domain binding studies, siRNA double knockdown with lipid level measurements Nature communications High 28970484
2020 ORP8 overexpression in non-small cell lung cancer cells induced apoptosis via release of cytochrome c from mitochondria into the cytoplasm. ORP8 overexpression, western blot and confocal microscopy for cytochrome c release, MTS/anchorage-independent growth assays Oncology reports Low 32323800
2022 ORP5 and ORP8 localize to MAM subdomains enriched in phosphatidic acid and control lipid droplet (LD) biogenesis at these sites. ORP5/8 regulate seipin recruitment to MAM-LD contacts; loss of ORP5/8 impairs LD biogenesis, and intact ER-mitochondria contact sites are required for this ORP5/8 function. Fluorescence microscopy, siRNA knockdown, seipin localization assays, LD biogenesis quantification, ER-mitochondria contact site disruption The Journal of cell biology Medium 35969857
2023 ORP8 functions as a lipophagy receptor by localizing to lipid droplets and directly interacting with phagophore-anchored LC3/GABARAPs to mediate LD encapsulation by autophagosomes. This function is independent of ORP8's lipid transporter activity. Upon lipophagy induction, AMPK phosphorylates ORP8, enhancing its affinity for LC3/GABARAPs. ORP8 deletion or disruption of the ORP8-LC3/GABARAP interaction causes LD and triglyceride accumulation; ORP8 overexpression alleviates liver lipid accumulation in ob/ob mice, and Osbpl8−/− mice show liver lipid clearance defects. Co-immunoprecipitation (ORP8-LC3/GABARAP), AMPK phosphorylation assays, ORP8 KO mice, ob/ob mouse ORP8 overexpression, lipid transfer domain mutants, LD and triglyceride quantification Protein & cell High 37707322
2023 Crystal structure of the ORP8 lipid transport domain (ORD8) was solved, revealing a β-barrel fold with anti-parallel β-strands and a large cavity (~1860 Å3) as the lipid-binding site. The lid region is required for stable lipid binding and slows transport while stabilizing cargo; fluorescence assays showed differential transport efficiencies for PS versus PI4P. X-ray crystallography, computer docking simulations, fluorescence lipid transport assays, comparative experiments between lid-deleted and full-length ORD8 Cells High 37566053
2023 STIM1-formed ER-PM junctions are required for PI4P/PS exchange by ORP5 and ORP8. ORP5 and ORP8 operate as a rheostat setting junctional PI4P/PtdSer ratio with reciprocal modes: ORP5 sets low and ORP8 sets high junctional PI4P/PtdSer ratio. This ratio controls STIM1-STIM1 and STIM1-Orai1 interactions, SERCA pump activity, Ca2+ oscillation patterns, and NFAT nuclear translocation. Targeting the ORDs to the STIM1 ER subdomain reversed ORP5/ORP8 function. Targeted ORD domain expression at PM vs ER subdomains, targeted PtdSer-specific PLA1a1, Ca2+ imaging, NFAT translocation assays, STIM1 interaction measurements Proceedings of the National Academy of Sciences of the United States of America Medium 37607230
2023 Sec22b co-precipitates with ORP8 at ER-phagosome membrane contact sites. Wild-type but not lipid-transfer-mutant ORP8 rescues phagosomal PI4P levels and reduces antigen degradation in Sec22b knockdown cells, and restores phagolysosome fusion, establishing that ORP8's PS/PI4P exchange activity downstream of Sec22b tethering controls phagosome maturation. Co-immunoprecipitation (Sec22b–ORP8), siRNA knockdown, phagosomal lipid quantification, antigen degradation assays, phagolysosome fusion assays with ORP8 mutant rescue Communications biology Medium 37794132
2023 ORP8 overexpression in renal cell carcinoma cells accelerated ubiquitin-mediated proteasomal degradation of Stathmin1, leading to increased microtubule polymerization and suppression of RCC cell growth, migration, and invasion. ORP8 overexpression and knockdown, proteasome inhibitor experiments, western blot for Stathmin1, microtubule polymerization assays, functional cell assays Experimental cell research Low 37054771
2025 Osbpl8 remodels lipid metabolism in macrophages by inhibiting excessive IRE1α-XBP1-related ER stress. Osbpl8 delivered via extracellular vesicles from anti-inflammatory BMDMs suppressed inflammatory responses and lipotoxicity in hepatocytes during MASH. LC-MS/MS proteomic identification, shRNA knockdown, palmitic acid lipotoxicity model, IRE1α-XBP1 pathway markers, AAV-shRNA in vivo Molecular medicine (Cambridge, Mass.) Low 40448016
2026 OSBPL8 recruits GPX1 to the ER membrane, where GPX1 directly reduces peroxidized phosphatidic acid (PA-OOH) generated by ROS. This GPX1-OSBPL8 axis drives a noncanonical ferroptosis pathway at the ER (distinct from GPX4-dependent plasma membrane ferroptosis); ROS-driven lipid peroxidation accumulates at the ER before plasma membrane rupture. Knockdown of either OSBPL8 or GPX1 promotes ROS-induced ferroptosis and suppresses tumor growth. Co-immunoprecipitation (GPX1-OSBPL8), subcellular fractionation (ER lipid peroxidation), siRNA knockdown, in vivo tumor growth assays, lipidomics (PA peroxidation) Cell High 41720096
2025 Glycosphingolipids (GM3 and SM4) are required to maintain ORP8 (and ORP5) localization to ER-PM membrane contact sites. Genetic deletion or pharmacological inhibition of GM3/SM4 biosynthetic enzymes displaced PI4KIIIα and its adaptor EFR3A from the PM, reducing PM PI4P content and disrupting ORP8 PM interactions, consequently reducing PS transport to the PM. High-resolution imaging, genetic deletion and pharmacological inhibition of GSL biosynthesis enzymes, quantitative lipid measurements (PI4P, PS) bioRxivpreprint Low bio_10.1101_2025.09.26.678863

Source papers

Stage 0 corpus · 23 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2015 INTRACELLULAR TRANSPORT. PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contacts. Science (New York, N.Y.) 513 26206935
2016 ORP5/ORP8 localize to endoplasmic reticulum-mitochondria contacts and are involved in mitochondrial function. EMBO reports 237 27113756
2017 ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P 2) and regulate its level at the plasma membrane. Nature communications 159 28970484
2007 OSBP-related protein 8 (ORP8) suppresses ABCA1 expression and cholesterol efflux from macrophages. The Journal of biological chemistry 111 17991739
2022 ORP5 and ORP8 orchestrate lipid droplet biogenesis and maintenance at ER-mitochondria contact sites. The Journal of cell biology 93 35969857
2023 ORP8 acts as a lipophagy receptor to mediate lipid droplet turnover. Protein & cell 68 37707322
2011 OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid levels and interacts with the nucleoporin Nup62. PloS one 53 21698267
2015 Oxysterol-binding protein-related protein 8 (ORP8) increases sensitivity of hepatocellular carcinoma cells to Fas-mediated apoptosis. The Journal of biological chemistry 36 25596532
2020 ORP5 and ORP8: Sterol Sensors and Phospholipid Transfer Proteins at Membrane Contact Sites? Biomolecules 26 32570981
2012 Silencing of OSBP-related protein 8 (ORP8) modifies the macrophage transcriptome, nucleoporin p62 distribution, and migration capacity. Experimental cell research 25 22683860
2013 Osbpl8 deficiency in mouse causes an elevation of high-density lipoproteins and gender-specific alterations of lipid metabolism. PloS one 21 23554939
2023 PtdSer as a signaling lipid determined by privileged localization of ORP5 and ORP8 at ER/PM junctional foci to determine PM and ER PtdSer/PI(4)P ratio and cell function. Proceedings of the National Academy of Sciences of the United States of America 17 37607230
2014 OSBP-related protein 8 (ORP8) interacts with Homo sapiens sperm associated antigen 5 (SPAG5) and mediates oxysterol interference of HepG2 cell cycle. Experimental cell research 16 24424245
2020 ORP8 induces apoptosis by releasing cytochrome c from mitochondria in non‑small cell lung cancer. Oncology reports 15 32323800
2023 Sec22b regulates phagosome maturation by promoting ORP8-mediated lipid exchange at endoplasmic reticulum-phagosome contact sites. Communications biology 9 37794132
2014 Orp8 deficiency in bone marrow-derived cells reduces atherosclerotic lesion progression in LDL receptor knockout mice. PloS one 9 25347070
2023 Crystal Structure of the ORP8 Lipid Transport ORD Domain: Model of Lipid Transport. Cells 6 37566053
2025 BMDM-derived ORP8 suppresses lipotoxicity and inflammation by relieving endoplasmic reticulum stress in mice with MASH. Molecular medicine (Cambridge, Mass.) 3 40448016
2025 Novel AMPK/ORP8-lipophagy axis: A therapeutic target for asiaticoside-mediated cardioprotection against ischemia-reperfusion injury in hyperlipidemia. Phytomedicine : international journal of phytotherapy and phytopharmacology 3 41027151
2026 A GPX1-OSBPL8 axis mediates noncanonical in vivo ferroptosis and cancer growth suppression. Cell 2 41720096
2025 Gender difference in the association of OSBPL8 polymorphisms with nephrolithiasis within a Chinese cohort. Gene 1 39761801
2023 ORP8 inhibits renal cell carcinoma progression by accelerating Stathmin1 degradation and microtubule polymerization. Experimental cell research 1 37054771
2026 The GPX1-OSBPL8 axis: integrating ER ferroptosis and apoptotic signaling. Apoptosis : an international journal on programmed cell death 0 42149290

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