Affinage

PDZD8

PDZ domain-containing protein 8 · UniProt Q8NEN9

Length
1154 aa
Mass
128.6 kDa
Annotated
2026-06-10
34 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PDZD8 is an ER-anchored transmembrane protein that uses an SMP lipid-transfer domain to tether the endoplasmic reticulum to multiple partner organelles and to move lipids across the resulting membrane contact sites (PMID:29097544, PMID:33912962). At ER–mitochondria contacts it is necessary for contact formation and for mitochondrial Ca2+ uptake following ER Ca2+ release, with the outer mitochondrial membrane protein FKBP8 serving as its direct tethering partner that sets ER–OMM distance and shapes mitochondrial morphology (PMID:29097544, PMID:40246839). In parallel, PDZD8 localizes to ER–late endosome/lysosome contacts through a GTP-dependent interaction with Rab7 and an interaction with Protrudin, acting as a Rab7 effector whose SMP domain extracts and transfers glycerophospholipids, ceramides, cholesterol, and phosphatidylserine to drive endolysosomal maturation, lysosome positioning, lipophagy, and autophagic flux (PMID:31636202, PMID:32917905, PMID:33912962, PMID:34552186, PMID:36465123). Stress-induced lysosomal lipid signaling activates this lipid-transfer activity to produce osmotic lysosomal vacuolation, and the same maturation function supports endolysosomal acidification required for TLR9 trafficking and downstream NF-κB activation (PMID:40839735, PMID:40897465). Beyond its tethering roles, PDZD8 is a substrate of AMPK, which phosphorylates it at threonine 527 under low glucose to promote its interaction with and activation of glutaminase 1 (GLS1), linking PDZD8 to glutaminolysis and macrophage cytokine output (PMID:38898113). Through these contact-site activities PDZD8 governs neuronal Ca2+ dynamics, neurite outgrowth, synaptic bouton formation, and brain lipid homeostasis (PMID:29097544, PMID:33912962, PMID:36658656, PMID:40156832).

Mechanistic history

Synthesis pass · year-by-year structured walk · 8 steps
  1. 2017 High

    Established PDZD8 as the first mammalian ER protein required to build ER–mitochondria contacts and to couple ER Ca2+ release to mitochondrial Ca2+ uptake, defining its founding tethering function.

    Evidence Live-cell imaging, fractionation, siRNA knockdown with Ca2+ imaging, and SMP-domain complementation of yeast Mmm1 in mammalian cells

    PMID:29097544

    Open questions at the time
    • Did not identify the mitochondrial tethering partner
    • Did not reconstitute lipid transfer by the SMP domain
  2. 2019 High

    Showed PDZD8 also concentrates at ER–late endosome/lysosome contacts via a GTP-dependent interaction with Rab7, extending its role beyond ER–mitochondria contacts.

    Evidence Colocalization imaging and Co-IP with GTP/GDP-loaded Rab7 plus knockdown

    PMID:31636202

    Open questions at the time
    • Did not demonstrate lipid transfer at these contacts
    • Functional consequence of the Rab7 interaction unresolved
  3. 2020 High

    Identified Protrudin as a second ER-side partner and revealed PDZD8 as a shared component of ER–mitochondria and ER–late endosome contacts that can organize three-way contacts and drive endosome maturation.

    Evidence Co-IP, BioID proximity proteomics, CRISPR knockouts, domain mapping, and lipid-extraction assays in HeLa cells and primary neurons

    PMID:32686675 PMID:32917905

    Open questions at the time
    • Direct lipid species transported not defined in these studies
    • How the three-way contact is coordinated mechanistically unclear
  4. 2021 High

    Demonstrated biochemically that the SMP domain binds and transfers glycerophospholipids and ceramides and that this lipid-transfer activity drives organelle positioning and neurite outgrowth, and solved the structural basis of the Rab7 interaction.

    Evidence In vitro lipid binding and liposome transfer assays with domain mutants, plus X-ray crystallography and ITC of the coiled-coil–Rab7 complex (2:1 GTP-dependent)

    PMID:33912962 PMID:34552186

    Open questions at the time
    • Directionality of lipid flux in cells not established
    • Full-length protein structure and SMP domain orientation at the contact unresolved
  5. 2022 Medium

    Connected PDZD8-dependent contacts to organismal physiology and disease, showing in vivo that modulating ER–mitochondria contacts alters lifespan, mitophagy, and neurodegenerative phenotypes, and that PDZD8 loss causes brain cholesteryl-ester accumulation via impaired lipophagy.

    Evidence Drosophila neuron-specific RNAi with lifespan/locomotor/mitophagy and Aβ42 readouts; PDZD8-KO mouse lipidomics and lysosomal fusion assays

    PMID:35831024 PMID:36465123

    Open questions at the time
    • Causal lipid species at the lysosome contact not fully isolated in vivo
    • Single-lab phenotypes not cross-validated
  6. 2023 Medium

    Linked PDZD8-mediated cholesterol transport and lipid-droplet–lysosome fusion to behavioral outcomes, establishing a brain lipid-homeostasis role.

    Evidence PDZD8-KO mice with cholesterol transport assays, lipid droplet–lysosome fusion assays, and behavioral battery

    PMID:36658656

    Open questions at the time
    • Cell-type-specific contribution to behavior unresolved
    • Direct lipid-transfer step in vivo not reconstituted
  7. 2024 High

    Revealed an unexpected signaling-metabolic role: AMPK phosphorylates PDZD8 at T527 to activate GLS1 and glutaminolysis, coupling PDZD8 to nutrient stress and macrophage inflammation independent of its tethering function.

    Evidence In vitro kinase assay, MS phospho-mapping, Co-IP, GLS1 activity assay, T527A phospho-dead mutant, and in vivo muscle/macrophage assays

    PMID:38898113

    Open questions at the time
    • Whether membrane contact-site localization is required for GLS1 activation is unclear
    • Structural basis of the PDZD8–GLS1 interaction undefined
  8. 2025 High

    Defined the direct ER–mitochondria tethering partner and the lipid-driven mechanism of lysosomal vacuolation, while extending PDZD8 function to endolysosomal acidification-dependent TLR9–NF-κB signaling and disease models.

    Evidence Cryo-ET, CLEM, proximity proteomics, single-molecule tracking and double-KO epistasis identifying FKBP8; SMP lipid-sensing/mutagenesis for lysosomal vacuolation; KO mouse and proximal tubular cell assays for TLR9–NF-κB; β-cell and RVLM neuron Ca2+ pathway studies

    PMID:39069376 PMID:40156832 PMID:40246839 PMID:40418411 PMID:40839735 PMID:40897465

    Open questions at the time
    • How the same SMP domain achieves directional ER-to-lysosome versus ER-to-mitochondria transport is unresolved
    • Reconciliation of pro-apoptotic Ca2+ overload roles with protective neuronal roles across tissues incomplete

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how PDZD8's lipid-transfer activity is directionally and selectively regulated across its distinct contact sites, and how its tethering, lipid-transport, and AMPK–GLS1 signaling functions are integrated within a single protein.
  • No full-length structural model integrating SMP, coiled-coil, and PDZ domains
  • Regulation of partner choice (FKBP8 vs Rab7/Protrudin vs GLS1) not defined
  • Conflicting HIV-1 requirement (KD vs clean KO) unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 3 GO:0140104 molecular carrier activity 3 GO:0008289 lipid binding 2
Localization
GO:0005764 lysosome 3 GO:0005768 endosome 3 GO:0005783 endoplasmic reticulum 3 GO:0005739 mitochondrion 2
Pathway
R-HSA-1430728 Metabolism 3 R-HSA-9609507 Protein localization 2 R-HSA-9612973 Autophagy 2
Partners
FKBP8GLSMSNRAB7ATMEM55BZFYVE27

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2017 PDZD8 is an ER-resident transmembrane protein whose SMP domain is functionally orthologous to the SMP domain of yeast Mmm1 (ERMES subunit). PDZD8 localizes to ER-mitochondria contact sites and is necessary for formation of these contacts in mammalian cells. In neurons, PDZD8 is required for Ca2+ uptake by mitochondria following synaptically induced Ca2+ release from ER, thereby regulating cytoplasmic Ca2+ dynamics. Live-cell imaging, subcellular fractionation, co-localization, siRNA knockdown with Ca2+ imaging readout, SMP domain functional complementation assay Science High 29097544
2020 PDZD8 uses distinct domains to interact with GTP-bound Rab7 and the ER transmembrane protein Protrudin, localizing to ER-late endosome membrane contact sites. At these MCSs, mitochondria are also recruited, forming a three-way contact. PDZD8 thus serves as a shared component of both ER-mitochondria and ER-late endosome MCSs. Co-immunoprecipitation, proximity proteomics (BioID), live-cell imaging, CRISPR-Cas9 knockouts, domain mapping Nature Communications High 32686675
2019 PDZD8, an intrinsic ER membrane protein with an SMP lipid transport domain, concentrates at ER-late endosome/lysosome contacts, where it interacts specifically with GTP-bound Rab7 (GTP-dependent interaction). Colocalization imaging, co-immunoprecipitation with GTP/GDP-loaded Rab7, knockdown PNAS High 31636202
2020 PDZD8 interacts with Protrudin at ER-endolysosome (LyLE) MCSs. The SMP domain of PDZD8 mediates lipid extraction from ER membranes. PDZD8 and Protrudin cooperatively promote endosome maturation by mediating ER-LyLE tethering and lipid extraction at MCSs, which is essential for neuronal polarity and integrity. Co-immunoprecipitation, overexpression and siRNA knockdown in HeLa cells and mouse primary neurons, live-cell imaging, endosomal morphology assays, lipid extraction assay Nature Communications High 32917905
2021 The SMP domain of PDZD8 binds glycerophospholipids and ceramides both in vivo and in vitro, and can transport lipids between membranes in vitro. PDZD8 acts as a tether at ER-late endosome/lysosome MCSs and its lipid transfer activity is required for late endosome/lysosome positioning and neurite outgrowth. In vitro lipid binding assay, in vitro lipid transfer assay between liposomes, PDZD8 knockdown with neurite outgrowth and organelle positioning readouts, confocal imaging Journal of Cell Science High 33912962
2021 Crystal structure of the human PDZD8 C-terminal coiled-coil (CC) domain in complex with GTP-bound Rab7 was determined. The PDZD8 CC contains one short helix and two helices forming an antiparallel coiled-coil; two Rab7 molecules bind opposite sides of the CC in a 2:1 stoichiometry via their switch I/II and interswitch regions. Isothermal titration calorimetry confirmed the GTP-dependent 2:1 binding. X-ray crystallography, isothermal titration calorimetry (ITC) Scientific Reports High 34552186
2024 PDZD8 is a substrate of AMPK; AMPK phosphorylates PDZD8 at threonine 527 (T527) under low-glucose conditions. This phosphorylation promotes the interaction of PDZD8 with glutaminase 1 (GLS1), activating GLS1 and promoting glutaminolysis. The PDZD8-T527A mutation abolishes this interaction and dampens glutaminolysis and pro-inflammatory cytokine secretion in macrophages. In vitro kinase assay, mass spectrometry phospho-mapping, co-immunoprecipitation, GLS1 activity assay, T527A phospho-dead mutant, in vivo skeletal muscle and macrophage assays Cell Research High 38898113
2025 FKBP8, an outer mitochondrial membrane (OMM) protein, is the direct tethering partner of ER-resident PDZD8 at ER-mitochondria contact sites (MERCS). Single-molecule tracking shows PDZD8 diffuses dynamically along the ER membrane with pauses and captures at MERCS. Overexpression of FKBP8 narrows the ER-OMM distance; combined deletion of PDZD8 and FKBP8 is interdependent for MERCS formation. PDZD8 enhances mitochondrial complexity (morphology) in a FKBP8-dependent manner. Unbiased proximity proteomics, CRISPR-Cas9 endogenous tagging, cryo-electron tomography, correlative light-electron microscopy (CLEM), single-molecule tracking, overexpression and double-KO epistasis Nature Communications High 40246839
2010 PDZD8 interacts with HIV-1 Gag protein (identified by yeast two-hybrid, confirmed by co-immunoprecipitation). PDZD8 overexpression promotes initiation of reverse transcription and increases retroviral infection, while knockdown decreases HIV-1 infection. A PDZD8 mutant lacking its predicted coiled-coil domain fails to bind Gag and loses ability to promote HIV-1 infection, mapping the Gag-interacting region. Yeast two-hybrid, co-immunoprecipitation, overexpression and siRNA knockdown, reverse transcription efficiency assay, domain deletion mutagenesis Journal of Virology Medium 20573829
2014 PDZD8 is a critical component of a heat-labile, >100 kDa cytoplasmic factor that slows spontaneous disassembly of HIV-1 capsid-nucleocapsid (CA-NC) complexes in vitro. PDZD8 knockdown accelerates HIV-1 capsid disassembly (uncoating) in infected cells and decreases reverse transcription. The coiled-coil domain is sufficient for capsid binding, but the PDZ domain is additionally required for capsid stabilization and supporting HIV-1 infection. In vitro capsid disassembly assay, PDZD8 knockdown, immunoprecipitation, domain deletion mutagenesis, reverse transcription assay in cells Journal of Virology Medium 24554657
2015 Stable CRISPR-Cas9 knockout of PDZD8 does not reduce HIV-1 or murine leukemia virus infection efficiency compared to parental cells, indicating PDZD8 is not absolutely required for retroviral infection. CRISPR-Cas9 knockout cell lines, HIV-1 and MLV infection assays Virology Medium 25771112
2011 PDZD8 interacts with moesin (an ERM family protein) as identified by co-immunoprecipitation. Exogenous expression of PDZD8 or moesin reduces levels of stable (acetylated) microtubules, suggesting PDZD8 functions as part of a cytoskeletal regulatory complex. Overexpression or siRNA knockdown of PDZD8 affects HSV-1 infection levels. Co-immunoprecipitation, siRNA knockdown, overexpression, microtubule acetylation assay, HSV-1 infection assay Virology Medium 21549406
2022 In Drosophila, reducing pdzd8-mediated ER-mitochondria contacts (MERCs) in neurons slows age-associated locomotor decline and increases lifespan, correlating with increased mitophagy. Conversely, increasing MERCs via a synthetic ER-mitochondria tether disrupts mitochondrial transport and synapse formation and reduces lifespan. Pdzd8 knockdown also rescues locomotor defects in a fly model of Alzheimer's disease expressing Aβ42, demonstrating that MERC reduction is protective in a neurodegenerative context. Drosophila neuron-specific RNAi knockdown, lifespan assay, locomotor assay, mitophagy reporter, synthetic ER-mitochondria tether overexpression, Aβ42 disease model Life Science Alliance Medium 35831024
2022 PDZD8-deficient mice accumulate cholesteryl esters (CEs) in the brain due to impaired lipophagy (lysosomal degradation of lipid droplets). PDZD8 functions as a Rab7 effector that transfers lipids (cholesterol and phosphatidylserine) between ER and Rab7-positive organelles to promote endolysosome maturation and fusion of CE-containing lipid droplets with lysosomes. PDZD8-KO mouse model, lipidomics (CE quantification), lipid droplet morphology assays, lysosomal fusion assays, Rab7 interaction studies iScience Medium 36465123
2023 PDZD8 transports cholesterol to lipid droplets and promotes fusion of lipid droplets with lysosomes (lipophagy). PDZD8-KO mice exhibit impaired lipid droplet degradation and abnormal accumulation of cholesteryl esters in the brain, leading to behavioral abnormalities in emotion, cognition, and adaptation. PDZD8-KO mouse model, cholesterol transport assay, lipid droplet-lysosome fusion assay, behavioral battery (open field, fear conditioning, etc.) Molecular Brain Medium 36658656
2025 PDZD8 (LYVAC) is a general mediator of lysosomal vacuolation. Upon lysosomal osmotic stress, diverse vacuolation inducers trigger PDZD8 recruitment to lysosomes through multivalent interactions. Stress-induced lysosomal lipid signaling (phosphatidylserine and cholesterol) activates PDZD8's SMP lipid transfer domain, driving directional ER-to-lysosome lipid movement that causes osmotic membrane expansion of lysosomes. Human cell line imaging, PDZD8 KO and rescue, live-cell imaging, lipid sensing assays, domain mutagenesis of lipid-binding residues Science High 40839735
2025 PDZD8 promotes autophagy at ER-late endosome/lysosome MCSs by promoting lysosome maturation and accelerating autophagic flux. PDZD8 is required for activity-dependent synaptic bouton formation in Drosophila neurons, and is sufficient to drive excess bouton formation through an autophagy-dependent mechanism. SMP domain mutational analysis suggests lipid transfer from ER to late endosomes/lysosomes is the mechanistic basis for lysosome maturation. In vivo CRISPR screen in Drosophila, genetic loss-of-function and gain-of-function, autophagic flux assays, lysosome maturation assays, SMP domain mutagenesis, synaptic bouton counting Cell Reports Medium 40156832
2025 PDZD8 regulates endolysosomal maturation and acidification, which is required for proper translocation of TLR9 to endolysosomes and downstream NF-κB activation in kidney proximal tubular cells. PDZD8 KO mice show reduced cisplatin-induced AKI severity and reduced NF-κB pathway activation. PDZD8 knockdown did not alter mitochondrial morphology or cytosolic leakage of mitochondrial DNA. Pdzd8 KO mouse, in vitro PDZD8 knockdown in human proximal tubular cells, lysosomal acidification assay, TLR9 localization by immunofluorescence, NF-κB reporter, cisplatin AKI model American Journal of Physiology - Renal Physiology Medium 40897465
2024 PDZD8 augments ER-mitochondria contact (MAM) formation in pancreatic β-cells. PDZD8 knockdown shortens MAM perimeter, suppresses MAM-related proteins (IP3R1, GRP75, VDAC1), inhibits VDAC1-IP3R1 interaction, alleviates mitochondrial Ca2+ overload, and decreases Cyclophilin D (CypD) expression, thereby reducing β-cell apoptosis. Cyclophilin D overexpression rescues β-cell death, placing PDZD8 upstream of CypD in the apoptotic pathway. PDZD8 knockdown in INS-1 cells and HFD mouse model, proximity ligation assay for VDAC1-IP3R1 interaction, Ca2+ imaging, mitochondrial membrane potential assay, Western blot, epistasis with CypD overexpression Diabetes & Metabolism Journal Medium 39069376
2025 PDZD8 dysregulation in RVLM neurons activates Ca2+-Calpain-2 (CAPN2) signaling: PDZD8 deficiency elevates cytoplasmic Ca2+ levels, which upregulates CAPN2, leading to ER stress, mitochondrial dysfunction, and neuronal apoptosis. CAPN2 inhibition rescues PDZD8-deficiency-induced ER stress and mitochondrial dysfunction. In vivo, PDZD8 upregulation in RVLM suppresses neuronal hyperexcitation and reduces blood pressure in stress-induced hypertension rats. PDZD8 siRNA knockdown in N2a cells, AAV2-mediated PDZD8 overexpression in rat RVLM, CAPN2 inhibitor treatment, Western blot, flow cytometry, immunofluorescence, RSNA/BP measurement Molecular Neurobiology Medium 40418411
2025 TMEM55B is identified as a lysosomal PDZD8-associated protein. TMEM55B depletion reduces lysosomal acidification, impairs lipid droplet turnover, attenuates lysosomal Ca2+ release and reuptake, and diminishes ER Ca2+ responses, consistent with impaired CICR at ER-lysosome MCSs. Mitochondrial Ca2+ dynamics were unaffected, suggesting specificity to the ER-lysosome axis. Co-immunoprecipitation/proximity assay for PDZD8-TMEM55B interaction, lysosomal pH assay, lipid droplet assay, Ca2+ imaging, siRNA knockdown bioRxiv (preprint)preprint Low bio_10.1101_2025.10.21.683636
2025 Live-cell imaging using a novel ddFP-based MERCS sensor (MERCdRED) demonstrated that large MERCS are more stable than smaller ones. Nutrient deprivation reduces MERCS area in a PDZD8-dependent manner, establishing PDZD8 as required for nutrient-regulated MERCS dynamics. Novel MERCS fluorescent sensor (ddFP-based), CLEM validation, live-cell imaging, PDZD8 KO under nutrient deprivation bioRxiv (preprint)preprint Low bio_10.1101_2025.04.17.649323

Source papers

Stage 0 corpus · 34 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 ER-mitochondria tethering by PDZD8 regulates Ca2+ dynamics in mammalian neurons. Science (New York, N.Y.) 402 29097544
2020 PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria. Nature communications 96 32686675
2019 PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes. Proceedings of the National Academy of Sciences of the United States of America 70 31636202
2020 Protrudin and PDZD8 contribute to neuronal integrity by promoting lipid extraction required for endosome maturation. Nature communications 65 32917905
2021 PDZD8-mediated lipid transfer at contacts between the ER and late endosomes/lysosomes is required for neurite outgrowth. Journal of cell science 46 33912962
2024 AMPK targets PDZD8 to trigger carbon source shift from glucose to glutamine. Cell research 34 38898113
2022 Decreasing pdzd8-mediated mito-ER contacts improves organismal fitness and mitigates Aβ42 toxicity. Life science alliance 31 35831024
2010 PDZD8 is a novel Gag-interacting factor that promotes retroviral infection. Journal of virology 31 20573829
2014 Contribution of PDZD8 to stabilization of the human immunodeficiency virus type 1 capsid. Journal of virology 28 24554657
2025 Mitochondrial complexity is regulated at ER-mitochondria contact sites via PDZD8-FKBP8 tethering. Nature communications 27 40246839
2018 PDZD8 is not the 'functional ortholog' of Mmm1, it is a paralog. F1000Research 26 30109028
2022 PDZD8 Disruption Causes Cognitive Impairment in Humans, Mice, and Fruit Flies. Biological psychiatry 22 35227461
2011 PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1. Virology 22 21549406
2022 Sunitinib and Pterostilbene Combination Treatment Exerts Antitumor Effects in Gastric Cancer via Suppression of PDZD8. International journal of molecular sciences 21 35409367
2015 Efficient human immunodeficiency virus (HIV-1) infection of cells lacking PDZD8. Virology 21 25771112
2021 Structural basis of human PDZD8-Rab7 interaction for the ER-late endosome tethering. Scientific reports 17 34552186
2020 Lipid Transfer-Dependent Endosome Maturation Mediated by Protrudin and PDZD8 in Neurons. Frontiers in cell and developmental biology 15 33385000
2024 PDZD8 Augments Endoplasmic Reticulum-Mitochondria Contact and Regulates Ca2+ Dynamics and Cypd Expression to Induce Pancreatic β-Cell Death during Diabetes. Diabetes & metabolism journal 14 39069376
2023 PDZD8-mediated endoplasmic reticulum-mitochondria associations regulate sympathetic drive and blood pressure through the intervention of neuronal mitochondrial homeostasis in stress-induced hypertension. Neurobiology of disease 14 37247681
2025 LYVAC/PDZD8 is a lysosomal vacuolator. Science (New York, N.Y.) 11 40839735
2023 PDZD8-deficient mice manifest behavioral abnormalities related to emotion, cognition, and adaptation due to dyslipidemia in the brain. Molecular brain 10 36658656
2022 PDZD8-deficient mice accumulate cholesteryl esters in the brain as a result of impaired lipophagy. iScience 10 36465123
2022 Lidocaine represses the malignant behavior of lung carcinoma cells via the circ_PDZD8/miR-516b-5p/GOLT1A axis. Histology and histopathology 8 35060113
2024 PDZD8-FKBP8 tethering complex at ER-mitochondria contact sites regulates mitochondrial complexity. bioRxiv : the preprint server for biology 7 38895210
2022 circ_0020123 promotes cell proliferation and migration in lung adenocarcinoma via PDZD8. Open medicine (Warsaw, Poland) 7 35415250
2025 PDZD8 promotes autophagy at ER-lysosome membrane contact sites to regulate activity-dependent synaptic growth. Cell reports 6 40156832
2023 Circ-PDZD8 promotes cell growth and glutamine metabolism in non-small cell lung cancer by enriching LARP1 via sequestering miR-330-5p. Thoracic cancer 5 37349870
2023 PDZD8 promotes autophagy at ER-Lysosome contact sites to regulate synaptogenesis. bioRxiv : the preprint server for biology 5 37961523
2025 PDZD8 Dysregulation Mediates RVLM Neuronal Hyperexcitation Via Activation of Ca2+-Calpain-2 Signaling in Stress-Induced Hypertension. Molecular neurobiology 3 40418411
2025 PDZD8 links organelle crosstalk to synaptic remodeling via autophagy. Autophagy 1 40754808
2026 Glutamine Starvation Induces Ferroptosis in NSCLC via AMPK/PDZD8-Mediated Ferritinophagy. Nutrients 0 42197056
2025 Autistic behavior is a common outcome of biallelic disruption of PDZD8 in humans and mice. Molecular autism 0 40016860
2025 The organelle-tethering protein PDZD8 regulates endolysosomal maturation and TLR9-NF-κB signaling in cisplatin-induced acute kidney injury. American journal of physiology. Renal physiology 0 40897465
2025 Overexpression of miR-1283 inhibits cell proliferation and migration of colorectal cancer cells by targeting PDZD8. Translational cancer research 0 40950703

Missed literature

Know a paper Affinage missed for PDZD8? Flag it for the maintainers and the community.

No submissions yet.