Affinage

PJA1

E3 ubiquitin-protein ligase Praja-1 · UniProt Q8NG27

Length
643 aa
Mass
71.0 kDa
Annotated
2026-04-28
26 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PJA1 (Praja1) is a RING-H2 E3 ubiquitin ligase that ubiquitinates a remarkably broad spectrum of substrates to regulate chromatin repression, TGFβ signaling, mitochondrial dynamics, neuronal proteostasis, and synaptic plasticity. It partners with UbcH5/UBE2E3 E2-conjugating enzymes to catalyze K48-linked ubiquitination and proteasomal degradation of substrates including EZH2 and other PRC2 subunits, phosphorylated SMAD3, PGAM5, Dlxin-1, FOXR2, TDP-43 aggregates, tau, polyglutamine-expanded proteins, and α-synuclein (PMID:11959851, PMID:21513699, PMID:32127355, PMID:38906860, PMID:41182881, PMID:35701899). Its activity is modulated by 18:0/22:6-phosphatidic acid binding to the N-terminal domain (Lys141-dependent, generated by DGKδ), by OTUB2-mediated deubiquitylation that stabilizes PJA1 itself, and by signal-dependent nuclear translocation during skeletal muscle differentiation where p38α-phosphorylated EZH2 becomes a substrate (PMID:32134507, PMID:36528254, PMID:35611163, PMID:28067271). In the brain, PJA1 suppresses aggregation of multiple neurodegenerative disease-associated proteins, is transcriptionally activated by TDP-43 in primates, and is rapidly downregulated following LTP induction in hippocampal CA1, where it regulates synaptic protein levels, spine density, and excitatory/inhibitory balance (PMID:35701899, PMID:38194085, PMID:40243483).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2002 High

    Establishing PJA1 as a functional RING-H2 E3 ubiquitin ligase resolved its molecular activity: it partners with UbcH5B and ubiquitinates the MAGE-family protein Dlxin-1 for proteasomal degradation, suppressing Dlx5-dependent transcription.

    Evidence GST pulldown, co-IP, in vitro ubiquitination with RING mutant controls, GAL4 reporter assay

    PMID:11959851 PMID:12036302

    Open questions at the time
    • Physiological context of Dlxin-1 degradation in vivo not established
    • Broader substrate repertoire unknown
  2. 2011 High

    Demonstrating that PJA1 directly ubiquitinates PRC2 subunits (EZH2, EED, SUZ12) in a cell-free system extended its substrate range to chromatin regulators, establishing a link between PJA1 and epigenetic gene silencing.

    Evidence Cell-free reconstituted ubiquitination assay with RING mutant controls, proteasome inhibitor rescue, DZNep-induced PRC2 dissociation model

    PMID:21513699

    Open questions at the time
    • Physiological trigger for PRC2 targeting by PJA1 not identified
    • Selectivity for individual PRC2 subunits versus intact complex unclear
  3. 2013 Medium

    PJA1 overexpression caused proteasome-dependent reduction of NRAGE in neuronal PC12 cells, inhibiting NGF-induced differentiation and neurite outgrowth, providing the first functional link between PJA1 and neuronal differentiation.

    Evidence Overexpression with proteasome inhibitor rescue, neurite outgrowth assay in PC12 cells

    PMID:23717400

    Open questions at the time
    • Direct ubiquitination of NRAGE by PJA1 not demonstrated
    • Endogenous PJA1 role in neuronal differentiation not confirmed by loss-of-function
  4. 2017 High

    Revealing that p38α-mediated phosphorylation of EZH2 at T372 creates a degron recognized by MYOD-induced PJA1 during myogenesis solved how signal-dependent substrate targeting and subcellular redistribution of PJA1 coordinate muscle gene activation.

    Evidence Phospho-mimetic/phospho-dead EZH2 mutants, subcellular fractionation, siRNA knockdown, satellite cell differentiation in vitro and in vivo

    PMID:28067271

    Open questions at the time
    • Whether PJA1 nuclear translocation mechanism involves a specific import signal remains undefined
    • Contribution of PJA1 to in vivo muscle regeneration beyond satellite cell assays not tested
  5. 2018 Medium

    PJA1 was found to restrict DNA viruses (HBV, HSV-1) by facilitating SMC5/6 complex binding to viral episomal DNA in the nucleus, revealing an unexpected role in innate antiviral defense independent of interferon signaling.

    Evidence Co-IP with SMC5/6, ChIP on viral DNA, knockdown/overexpression with viral replication readouts, topoisomerase inhibitor experiments

    PMID:30185588

    Open questions at the time
    • Whether PJA1 ubiquitinates SMC5/6 components or acts as a scaffold is unknown
    • Single-lab finding not independently replicated
    • In vivo relevance to viral infection not tested
  6. 2020 High

    Multiple studies simultaneously expanded PJA1's substrate range and regulatory mechanisms: PJA1 ubiquitinates phospho-SMAD3 to suppress TGFβ tumor-suppressor signaling in HCC, clears TDP-43 aggregates in motor neurons via UBE2E3, and is activated by 18:0/22:6-phosphatidic acid generated by DGKδ, establishing lipid-dependent regulation of E3 ligase activity.

    Evidence Ubiquitination assays with RING inhibitor (RTA405), co-IP with UBE2E3 and TDP-43 CTF, lipid-protein binding assays with DGKδ-KO mouse, in vivo mouse facial motor neuron model, HCC xenograft

    PMID:32127355 PMID:32134507 PMID:32686212

    Open questions at the time
    • Whether PA-mediated activation applies to all substrates or is SERT-specific
    • Structural basis for PA-induced conformational change unknown
    • E2 selectivity for different substrates not systematically mapped
  7. 2021 Medium

    PJA1 suppressed polyglutamine protein aggregation and toxicity across yeast, Drosophila, and neuronal cell models, broadening its neuroprotective role to polyQ diseases including SCA3 and Huntington's disease.

    Evidence Co-IP, degradation assay, yeast toxicity assay, Drosophila SCA3 eye degeneration model

    PMID:34161122

    Open questions at the time
    • Whether PJA1 directly ubiquitinates expanded polyQ proteins or acts indirectly not resolved
    • Mammalian in vivo efficacy in polyQ disease models not tested
  8. 2022 Medium

    Domain mapping revealed that PJA1's N-terminal region (aa 1–224, Lys141-dependent) binds phosphatidic acid while the C-terminal RING domain interacts with DGKδ2, establishing a modular architecture for lipid-regulated ubiquitination; separately, OTUB2 was identified as a deubiquitylase that stabilizes PJA1 itself.

    Evidence Truncation/mutagenesis binding assays for domain mapping; co-IP and cycloheximide chase for OTUB2-PJA1 stabilization with knockdown rescue in HCC

    PMID:35611163 PMID:36528254

    Open questions at the time
    • Whether OTUB2-mediated stabilization of PJA1 occurs in non-cancer contexts unknown
    • Full structural model of PJA1 domains unavailable
  9. 2023 Medium

    Astrocytic GPR30 was shown to transcriptionally induce PJA1 via CREB, and PJA1 binds Serpina3n in astrocytes to regulate learning and memory in female mice, placing PJA1 within a sex-specific neuroimmune signaling axis.

    Evidence Conditional knockout, co-IP of PJA1-Serpina3n, behavioral assays in female mice

    PMID:37712419

    Open questions at the time
    • Whether PJA1 ubiquitinates Serpina3n or acts through a non-degradative mechanism not determined
    • Sex-specificity mechanism unexplored
  10. 2024 High

    Identification of PGAM5 K88 as a PJA1-mediated K48-ubiquitination site linked PJA1 to mitochondrial dynamics: PGAM5 degradation promotes DRP1-S637 phosphorylation, reduces mitochondrial ROS, and suppresses GSDME-mediated pyroptosis, conferring docetaxel resistance in nasopharyngeal carcinoma.

    Evidence K48-linkage-specific ubiquitination assay, K88 mutagenesis, DRP1 phosphorylation, ROS measurement, pyroptosis assay, xenograft

    PMID:38906860

    Open questions at the time
    • Upstream signals that activate PJA1 in drug-resistant tumors not identified
    • Whether PJA1-PGAM5 axis operates in non-cancer mitochondrial biology unknown
  11. 2024 Medium

    Discovery that TDP-43 transcriptionally activates PJA1 by directly binding its promoter in primates—but not rodents—established a primate-specific feedforward neuroprotective loop where PJA1 clears TDP-43 aggregates and TDP-43 sustains PJA1 expression.

    Evidence ChIP/promoter analysis, TDP-43 knockdown in monkey and mouse brain, PJA1 overexpression rescue of neuronal death

    PMID:38194085

    Open questions at the time
    • Rodent models may not recapitulate this regulatory circuit
    • Whether this loop is disrupted in ALS/FTD patients not examined
  12. 2025 High

    PJA1 directly ubiquitinates tau (wild-type and P301L mutant) in reconstituted and cellular assays, and evolutionary analysis showed this interaction arose specifically in placental mammals after Praja gene duplication, placing PJA1 in the context of Alzheimer's-relevant proteostasis.

    Evidence In vitro and in vivo ubiquitination assays in SH-SY5Y cells, E3-dead mutant controls, ancestral sequence reconstruction and mutagenesis

    PMID:41182881

    Open questions at the time
    • In vivo efficacy of PJA1 in reducing tau pathology in animal models not demonstrated
    • Whether PJA1 targets physiological or only pathological tau forms unclear
  13. 2025 Medium

    LTP induction triggers rapid proteasome-dependent degradation of PJA1 in hippocampal CA1, and PJA1 knockdown enhances memory while altering synaptic protein levels and E/I balance, revealing PJA1 as a plasticity brake whose activity-dependent removal enables memory consolidation; spinophilin was identified as a novel interacting substrate.

    Evidence In vitro electrophysiology (LTP), in vivo knockdown, behavioral tests, co-IP with spinophilin, spine density analysis

    PMID:40243483

    Open questions at the time
    • Direct ubiquitination of spinophilin not demonstrated
    • Mechanism of activity-dependent PJA1 degradation unknown
    • Whether PJA1 removal is necessary or merely permissive for LTP not determined

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the structural basis for PJA1's remarkably broad substrate recognition, the mechanisms governing its subcellular redistribution, and whether its neuroprotective functions can be therapeutically harnessed in neurodegenerative diseases.
  • No high-resolution structure of PJA1 or PJA1-substrate complex available
  • No substrate-binding domain outside the RING has been structurally defined
  • In vivo validation of PJA1-mediated neuroprotection in mammalian neurodegenerative disease models is lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 7 GO:0016874 ligase activity 6 GO:0008289 lipid binding 2
Localization
GO:0005634 nucleus 3 GO:0005829 cytosol 1 GO:0005856 cytoskeleton 1
Pathway
R-HSA-392499 Metabolism of proteins 7 R-HSA-112316 Neuronal System 4 R-HSA-162582 Signal Transduction 3 R-HSA-4839726 Chromatin organization 2 R-HSA-5357801 Programmed Cell Death 1
Partners
DGKΔEZH2MAPTOTUB2PGAM5SMAD3TARDBPUBE2E3

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 PJA1 (Praja1) is a RING-H2 E3 ubiquitin ligase that binds the necdin homology domain of Dlxin-1 (a MAGE/Necdin family protein) via GST pulldown and co-immunoprecipitation, promotes Dlxin-1 ubiquitination in vivo, and targets it for proteasomal degradation, thereby suppressing Dlx5-dependent transcriptional activity. A RING finger mutant of Praja1 abolished ubiquitination and degradation, confirming the requirement for E3 ligase activity. GST pulldown, co-immunoprecipitation, overexpression with proteasome inhibitor rescue, RING finger mutagenesis, GAL4-based transcription assay The Journal of biological chemistry High 11959851
2002 Human PJA1 encodes a 71-kDa RING-H2 finger protein that binds the ubiquitin-conjugating enzyme UbcH5B and displays E2-dependent E3 ubiquitin ligase activity in vitro. In vitro binding assay, immunoprecipitation, in vitro ubiquitination assay Genomics High 12036302
2011 PRAJA1 directly ubiquitinates individual PRC2 subunits (EZH2, EED, SUZ12) in a cell-free system, leading to their proteasomal degradation; an inactive RING finger mutant failed to enhance degradation, establishing PRAJA1 as a bona fide E3 for PRC2 subunits. Cell-free ubiquitination assay, RING finger mutagenesis, proteasome inhibitor rescue, DZNep-induced PRC2 dissociation model Biochemical and biophysical research communications High 21513699
2011 Protein microarray profiling identified UbcH5 family E2s as optimal partners for Praja1 in vitro, and revealed a broad set of putative Praja1 substrates consistent with its roles in bone development and brain function. Protein microarray ubiquitination screen, in vitro E2 activity panel Cell biochemistry and biophysics Low 21461837
2013 Praja1 co-localizes with cytoskeletal components and NRAGE in PC12 cells, and its overexpression causes proteasome-dependent reduction of NRAGE protein levels, inhibiting NGF-induced neuronal differentiation and neurite formation. Co-localization immunofluorescence, overexpression with proteasome inhibitor, stable cell lines, neurite outgrowth assay PloS one Medium 23717400
2017 In differentiating skeletal muscle cells, p38α kinase phosphorylates EZH2 at threonine 372, which promotes recognition and ubiquitin-mediated proteasomal degradation of EZH2 by the MYOD-induced E3 ligase PJA1 (Praja1). Low PJA1 levels and its cytoplasmic localization in proliferating myoblasts prevent premature EZH2 degradation, and nuclear translocation upon differentiation enables EZH2 targeting, allowing muscle gene expression. Biochemical co-immunoprecipitation, genetic rescue, phospho-mimetic/phospho-dead mutants, subcellular fractionation, siRNA knockdown, satellite cell differentiation assays Nature communications High 28067271
2018 PJA1 restricts DNA viruses (HBV, HSV-1) and episomal plasmids but not RNA viruses, independent of type I/II interferon pathways. PJA1 physically interacts with the SMC5/6 complex and facilitates its binding to viral and episomal DNAs in the cell nucleus; DNA topoisomerase activity is required for PJA1-mediated silencing. Co-immunoprecipitation, ChIP, knockdown/overexpression with viral replication assays, topoisomerase inhibitor treatment Journal of virology Medium 30185588
2020 PJA1 binds to C-terminal fragment (CTF) TDP-43 and the E2-conjugating enzyme UBE2E3 as shown by co-immunoprecipitation, suppresses phosphorylation and cytoplasmic aggregate formation of TDP-43 in neuronal cells in vitro, and reduces phosphorylated TDP-43 aggregates in mouse facial motor neurons in vivo. Co-immunoprecipitation, adenoviral overexpression, immunofluorescence, in vivo mouse facial motor neuron model Neuropathology : official journal of the Japanese Society of Neuropathology Medium 32686212
2020 PJA1 promotes ubiquitination and proteasomal degradation of phosphorylated SMAD3 in HCC cells, impairing the SMAD3/β2SP tumor-suppressing TGFβ pathway; an inactive RING finger mutant (RTA405-targeted) failed to enhance SMAD3 degradation. Ubiquitination assay, co-immunoprecipitation, RING finger inhibitor (RTA405), knockdown/overexpression, xenograft tumor model Cancer research High 32127355
2020 1-Stearoyl-2-docosahexaenoyl (18:0/22:6)-phosphatidic acid (PA), generated by DGKδ, selectively binds to Praja1 and enhances its E3 ubiquitin ligase activity, providing a lipid-based activation mechanism for Praja1-mediated ubiquitination and degradation of SERT in the brain. Lipid-protein binding assay, DGKδ-knockout mouse brain lipidomics, E3 activity assay FEBS letters Medium 32134507
2020 Mass spectrometry revealed that HMGA2 interacts with PJA1 in the nuclei of HCC cells, and this interaction is enhanced by TGFβ treatment, suggesting PJA1 may regulate HMGA2 through ubiquitination in the context of altered TGFβ signaling. Mass spectrometry, co-localization immunofluorescence Genes & cancer Low 32577156
2021 Praja1 interacts with polyglutamine (polyQ) proteins (ataxin-3/huntingtin), enhances their ubiquitin-mediated degradation, reduces aggregate formation in neuronal cells, and suppresses polyQ toxicity in yeast and in a Drosophila SCA3 model. Co-immunoprecipitation, degradation assay, aggregate quantification, yeast toxicity assay, Drosophila eye degeneration model Molecular biology of the cell Medium 34161122
2021 PJA1 promotes ubiquitin-mediated degradation of FOXR2 in lung adenocarcinoma cells, inhibiting invasion and inducing apoptosis through inactivation of the Wnt/β-catenin signaling pathway. Ubiquitination assay, overexpression/knockdown, invasion assay, apoptosis assay, Wnt/β-catenin reporter Biochemical and biophysical research communications Medium 33839405
2022 PJA1 binds to and suppresses aggregate formation of multiple neurodegenerative disease-related proteins including FUS, SOD1, α-synuclein, ataxin-3, and huntingtin polyQ in neuronal cultures, as demonstrated by co-immunoprecipitation; Parkin, RNF112, and RNF220, though also binding TDP-43, lacked this broad suppressive activity. Co-immunoprecipitation, adenoviral expression, aggregate quantification in cultured neuronal cells Neuropathology : official journal of the Japanese Society of Neuropathology Medium 35701899
2022 The N-terminal region (aa 1–224) of Praja1 binds 18:0/22:6-phosphatidic acid with Lys141 critical for binding, while the C-terminal RING domain (aa 446–615) interacts with DGKδ2 (via its catalytic domain aa 309–466), revealing distinct regulatory and catalytic domains within Praja1 for lipid-mediated activation and E2/substrate recruitment in the DGKδ2-Praja1-SERT complex. Domain deletion/truncation binding assays, mutagenesis (Lys141), in vitro protein-lipid interaction Biochimica et biophysica acta. Molecular and cell biology of lipids Medium 36528254
2022 OTUB2 deubiquitylase stabilizes PJA1 protein by removing ubiquitin chains from PJA1, as demonstrated by co-immunoprecipitation and cycloheximide chase assay, with OTUB2 knockdown reducing PJA1 levels and its oncogenic effects on HCC cells rescued by PJA1 overexpression. Co-immunoprecipitation, cycloheximide chase, overexpression/knockdown rescue experiment Cellular and molecular bioengineering Medium 35611163
2023 Astrocytic GPR30 positively regulates PJA1 expression via the CREB signaling pathway; PJA1 binds to Serpina3n (a neuroinflammation marker) in astrocytes and mediates GPR30-dependent regulation of astrocyte phenotype, learning, and memory in female mice. Conditional knockout, co-immunoprecipitation (PJA1-Serpina3n), astrocyte phenotype assay, behavioral assays The Journal of clinical investigation Medium 37712419
2024 PJA1 promotes K48-linked ubiquitination of the mitochondrial protein PGAM5 at K88, leading to its proteasomal degradation, which further facilitates DRP1 phosphorylation at S637, reduces mitochondrial ROS production, suppresses GSDME-mediated pyroptosis, and thereby confers docetaxel resistance in nasopharyngeal carcinoma cells. Ubiquitination assay (K48-linkage specific), site-directed mutagenesis (K88 of PGAM5), PGAM5 knockdown rescue, DRP1 phosphorylation assay, ROS measurement, pyroptosis assay, in vivo xenograft Nature communications High 38906860
2024 Nuclear TDP-43 directly binds the promoter of the PJA1 gene in primates (but not rodents) and transcriptionally activates it; TDP-43 knockdown suppresses PJA1 expression in monkey brain, reducing PJA1-mediated neuroprotection, while PJA1 overexpression rescues neuronal cell death caused by TDP-43 loss. TDP-43 knockdown in monkey and mouse brain, ChIP/promoter analysis, PJA1 overexpression rescue in vivo Cellular and molecular life sciences : CMLS Medium 38194085
2025 Praja1 ubiquitinates tau protein (both wild-type and P301L) in in vitro and in vivo ubiquitination assays in SH-SY5Y cells, reducing tau levels in an E3 ligase activity-dependent manner; ancestral sequence reconstruction and mutational analysis showed the Praja1-tau interaction evolved specifically in placental mammals after Praja family duplication. In vitro ubiquitination assay, in vivo ubiquitination assay in SH-SY5Y cells, E3 ligase mutant controls, ancestral sequence reconstruction, mutagenesis The FEBS journal High 41182881
2025 LTP induction triggers rapid proteasome-dependent downregulation of PRAJA1 in the CA1 hippocampus; PRAJA1 knockdown in vivo enhances object recognition and spatial memory, reduces spine density and key synaptic proteins, influences E/I balance, and potentiates GABAergic transmission when overexpressed. Spinophilin was identified as a novel PRAJA1 substrate by co-immunoprecipitation. In vitro electrophysiology (LTP), in vivo PRAJA1 knockdown, behavioral assays, protein biochemistry, co-immunoprecipitation (spinophilin), spine density analysis International journal of molecular sciences Medium 40243483

Source papers

Stage 0 corpus · 26 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 A RING finger protein Praja1 regulates Dlx5-dependent transcription through its ubiquitin ligase activity for the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1. The Journal of biological chemistry 93 11959851
2002 PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain. Genomics 51 12036302
2017 Praja1 E3 ubiquitin ligase promotes skeletal myogenesis through degradation of EZH2 upon p38α activation. Nature communications 46 28067271
2011 PRAJA1 is a ubiquitin ligase for the polycomb repressive complex 2 proteins. Biochemical and biophysical research communications 44 21513699
1997 Praja1, a novel gene encoding a RING-H2 motif in mouse development. Oncogene 44 9393880
2007 Contiguous gene deletions involving EFNB1, OPHN1, PJA1 and EDA in patients with craniofrontonasal syndrome. Clinical genetics 36 17941886
2018 PJA1 Coordinates with the SMC5/6 Complex To Restrict DNA Viruses and Episomal Genes in an Interferon-Independent Manner. Journal of virology 32 30185588
2020 Praja1 RING-finger E3 ubiquitin ligase suppresses neuronal cytoplasmic TDP-43 aggregate formation. Neuropathology : official journal of the Japanese Society of Neuropathology 30 32686212
2020 1-Stearoyl-2-docosahexaenoyl-phosphatidic acid interacts with and activates Praja-1, the E3 ubiquitin ligase acting on the serotonin transporter in the brain. FEBS letters 26 32134507
2020 A recurrent PJA1 variant in trigonocephaly and neurodevelopmental disorders. Annals of clinical and translational neurology 23 32530565
2020 Targeting the E3 Ubiquitin Ligase PJA1 Enhances Tumor-Suppressing TGFβ Signaling. Cancer research 22 32127355
2024 PJA1-mediated suppression of pyroptosis as a driver of docetaxel resistance in nasopharyngeal carcinoma. Nature communications 19 38906860
2021 Praja1 ubiquitin ligase facilitates degradation of polyglutamine proteins and suppresses polyglutamine-mediated toxicity. Molecular biology of the cell 15 34161122
2013 The ubiquitin ligase Praja1 reduces NRAGE expression and inhibits neuronal differentiation of PC12 cells. PloS one 15 23717400
2022 Praja1 RING-finger E3 ubiquitin ligase is a common suppressor of neurodegenerative disease-associated protein aggregation. Neuropathology : official journal of the Japanese Society of Neuropathology 13 35701899
2023 PJA1 mediates the effects of astrocytic GPR30 on learning and memory in female mice. The Journal of clinical investigation 12 37712419
2020 Alterations in TGF-β signaling leads to high HMGA2 levels potentially through modulation of PJA1/SMAD3 in HCC cells. Genes & cancer 12 32577156
2020 Dysregulated PJA1-TGF-β signaling in cancer stem cell-associated liver cancers. Oncoscience 12 33457451
2021 E3 ubiquitin ligase PJA1 regulates lung adenocarcinoma apoptosis and invasion through promoting FOXR2 degradation. Biochemical and biophysical research communications 10 33839405
2011 Protein microarrays for the identification of praja1 e3 ubiquitin ligase substrates. Cell biochemistry and biophysics 10 21461837
2022 OTUB2 Promotes Proliferation and Migration of Hepatocellular Carcinoma Cells by PJA1 Deubiquitylation. Cellular and molecular bioengineering 9 35611163
2022 Distinct regions of Praja-1 E3 ubiquitin-protein ligase selectively bind to docosahexaenoic acid-containing phosphatidic acid and diacylglycerol kinase δ. Biochimica et biophysica acta. Molecular and cell biology of lipids 5 36528254
2025 The E3 Ubiquitin Ligase PRAJA1: A Key Regulator of Synaptic Dynamics and Memory Processes with Implications for Alzheimer's Disease. International journal of molecular sciences 3 40243483
2025 E3 ligase Praja1 mediates ubiquitination and degradation of microtubule-associated protein tau. The FEBS journal 3 41182881
2024 Loss of TDP-43 mediates severe neurotoxicity by suppressing PJA1 gene transcription in the monkey brain. Cellular and molecular life sciences : CMLS 1 38194085
2025 Praja1 E3 ubiquitin ligase and the role it plays in neurodegeneration. The FEBS journal 0 41466523