Affinage

DUSP22

Dual specificity protein phosphatase 22 · UniProt Q9NRW4

Length
184 aa
Mass
20.9 kDa
Annotated
2026-04-28
67 papers in source corpus 20 papers cited in narrative 20 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DUSP22 is a myristoylated dual-specificity phosphatase that functions as a broad negative regulator of receptor-proximal signaling by directly dephosphorylating multiple kinases and signaling proteins, while also serving a phosphatase-independent scaffold role in JNK activation. In T cells, DUSP22 suppresses TCR signaling through two convergent mechanisms: direct dephosphorylation of Lck at Tyr394 and dephosphorylation of the E3 ligase UBR2, which triggers UBR2 degradation and loss of Lck K63-ubiquitination required for Lck activation; accordingly, DUSP22-knockout mice develop spontaneous autoimmunity (PMID:24714587, PMID:38225265). Beyond T-cell regulation, DUSP22 dephosphorylates FAK (Tyr397/576/577), EGFR, AKT (Ser473/Thr308), ERα (Ser118), and LGALS1 (Ser8/Thr58), thereby suppressing downstream ERK, NF-κB, and PI3K-AKT pathways in contexts including hepatocellular carcinoma, lung cancer, and tumor immune evasion (PMID:36209205, PMID:38877005, PMID:37937915, PMID:17384676, PMID:41611244). Independently of its phosphatase activity, DUSP22 scaffolds an ASK1–MKK7–JNK complex to promote JNK phosphorylation and apoptosis, and its catalytic mechanism depends on a structurally defined DPN-triloop hydrogen bonding network among residues D57, S93, and N128 (PMID:27711255, PMID:33053837).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2001 High

    Identification of DUSP22 as a dual-specificity phosphatase that paradoxically activates JNK and dephosphorylates ERK2 established the enzyme as a MAP kinase regulator with context-dependent outputs on different MAPK branches.

    Evidence Transient cotransfection JNK activation assays in mammalian cells; in vitro ERK2 dephosphorylation and TCR-induced NFAT/AP-1 reporter suppression in Jurkat T cells

    PMID:11717427 PMID:11733513

    Open questions at the time
    • Mechanism of JNK activation versus ERK inhibition by the same phosphatase was unresolved
    • No substrate specificity determinants identified
    • In vivo relevance not yet established
  2. 2002 High

    Demonstration that DUSP22 associates with JNK and MKK7 in vivo but not JNK in vitro, and that gene disruption abolishes cytokine-induced JNK activation, revealed an indirect scaffolding mechanism rather than direct JNK dephosphorylation for JNK activation.

    Evidence Co-immunoprecipitation of JNK and MKK7 with DUSP22 in HEK293T cells; targeted gene disruption in murine ES cells abolishing TNF-α/TGF-β-induced JNK activation

    PMID:12138158

    Open questions at the time
    • Stoichiometry and structural basis of the scaffold complex unknown
    • How phosphatase activity and scaffold function are coordinated was unclear
  3. 2004 High

    Establishing that N-terminal myristoylation at Gly-2 is required for plasma membrane targeting resolved how DUSP22 gains access to membrane-proximal substrates.

    Evidence Myristoylation site mutagenesis and fluorescence microscopy in 293T and NIH-3T3 cells

    PMID:15138252

    Open questions at the time
    • Whether membrane localization is required for all or only specific substrate interactions was untested
    • Dynamic regulation of DUSP22 membrane association not examined
  4. 2007 High

    Discovery that DUSP22 associates with ERα and dephosphorylates Ser118 to suppress ERα-dependent transcription expanded the substrate repertoire beyond MAPKs to nuclear hormone receptors.

    Evidence Reciprocal co-immunoprecipitation of endogenous proteins in T47D breast cancer cells; catalytic mutant and siRNA controls with ERα reporter assays

    PMID:17384676

    Open questions at the time
    • How DUSP22 accesses nuclear ERα given its membrane localization was not addressed
    • Physiological consequences in mammary tissue unknown
  5. 2014 High

    Identification of Lck Tyr394 as a direct DUSP22 substrate, together with the spontaneous autoimmunity phenotype in knockout mice, established DUSP22 as a critical negative regulator of TCR-proximal signaling in vivo.

    Evidence In vitro Lck pTyr394 dephosphorylation assay; JKAP-knockout mouse with enhanced T-cell responses and spontaneous autoimmunity; adoptive transfer EAE model

    PMID:24714587

    Open questions at the time
    • Whether Lck was the sole T-cell substrate was unknown
    • Mechanism linking DUSP22 loss to specific autoimmune disease subtypes not defined
  6. 2016 Medium

    Reconstitution of the ASK1–MKK7–JNK scaffold complex with phosphatase-dead DUSP22 mutants confirmed that the JNK-activating function is independent of catalytic activity, demonstrating a dual-function protein.

    Evidence Co-immunoprecipitation of ASK1, MKK7, JNK with WT and catalytically inactive DUSP22; biphasic dose-dependent JNK phosphorylation and apoptosis assays

    PMID:27711255

    Open questions at the time
    • Single lab; independent replication needed
    • Structural basis for scaffold versus phosphatase substrate selection unknown
    • In vivo relevance of scaffold function not demonstrated with genetic tools
  7. 2019 Medium

    Showing DUSP22 dephosphorylates EGFR and AR extended its tumor-suppressive role to receptor tyrosine kinase and androgen receptor signaling in prostate cancer.

    Evidence Co-immunoprecipitation and phosphorylation assays with catalytic mutant controls in prostate cancer cell lines

    PMID:31693867

    Open questions at the time
    • Single lab; specific EGFR phosphorylation sites not mapped
    • In vivo validation in prostate cancer models not provided
  8. 2020 High

    Crystal structure and NMR of DUSP22 defined the DPN-triloop hydrogen bonding network (D57–S93–N128) essential for catalysis, providing the structural basis for understanding how somatic mutations inactivate the enzyme.

    Evidence X-ray crystallography, NMR spectroscopy, alanine mutagenesis with kcat/KM measurements showing >100-fold reduction

    PMID:33053837

    Open questions at the time
    • No substrate-bound co-crystal structure
    • How DPN-triloop perturbation affects scaffold function not tested
  9. 2022 High

    Demonstration that DUSP22 dephosphorylates FAK at Tyr397/576/577 to suppress ERK1/2 and NF-κB signaling in hepatic-specific KO and transgenic mice linked DUSP22 loss to NASH and HCC progression.

    Evidence In vitro FAK dephosphorylation assays, hepatic-specific DUSP22 KO and transgenic OE mouse models, AAV-mediated gene therapy

    PMID:36209205

    Open questions at the time
    • Whether FAK is the sole hepatic substrate is unclear
    • Therapeutic window and long-term safety of AAV-mediated DUSP22 restoration not established
  10. 2023 Medium

    Direct dephosphorylation of AKT at Ser473 and Thr308 by DUSP22 added PI3K-AKT to the list of pathways negatively regulated by DUSP22 in lung cancer cells.

    Evidence Co-immunoprecipitation and in vitro phosphatase assays in A549 and H1299 NSCLC cells with phosphatase-activity-dependent controls

    PMID:37937915

    Open questions at the time
    • Single lab; independent confirmation needed
    • In vivo lung cancer models not included
  11. 2024 High

    Uncovering DUSP22's dephosphorylation of UBR2, leading to its degradation and loss of Lck K63-ubiquitination, revealed a second, indirect mechanism by which DUSP22 suppresses T-cell activation and linked DUSP22 deficiency to systemic lupus erythematosus.

    Evidence UBR2 KO, K63-linkage-specific ubiquitination assays, mass spectrometry for UBR2 phosphorylation sites, single-cell RNA-seq, human SLE patient samples

    PMID:38225265

    Open questions at the time
    • Specific UBR2 serine residues dephosphorylated by DUSP22 identified but whether all are equally important is unclear
    • Causal role in human SLE beyond correlation not established
  12. 2025 Medium

    Finding that DUSP22 upregulation in sarcopenic muscle drives JNK-FOXO3a-dependent atrophy, inhibitable by BML-260, revealed a pathogenic gain-of-function context for DUSP22's JNK-regulatory role.

    Evidence DUSP22 knockdown in muscle cells, BML-260 pharmacological treatment, sarcopenia mouse models, JNK and FOXO3a phosphorylation assays

    PMID:40263624

    Open questions at the time
    • Whether DUSP22 activates or inhibits JNK in muscle (conflicting with scaffold activation model) needs clarification
    • BML-260 selectivity for DUSP22 not fully characterized
  13. 2026 High

    Identification of LGALS1 as a DUSP22 substrate (dephosphorylation at Ser8/Thr58 triggers LGALS1 degradation) established a mechanism by which DUSP22 relieves immunosuppression and promotes CD8+ T-cell tumor infiltration.

    Evidence Genome-wide Sleeping Beauty transposon screen, mass spectrometry, phosphomimetic mutants, in vivo mouse tumor models, single-cell RNA-seq

    PMID:41611244

    Open questions at the time
    • Whether DUSP22 regulation of LGALS1 operates in all tumor types or is context-specific
    • Direct structural basis for DUSP22–LGALS1 interaction not resolved
  14. 2026 High

    DUSP22 was shown to be essential for integrin activation and SYK/HCK phosphorylation in neutrophils during vascular inflammation, revealing a cell-type-specific positive signaling role distinct from its T-cell inhibitory function.

    Evidence JSP1-knockout mouse Shwartzman reaction model, neutrophil adoptive transfer, integrin activation and SYK/HCK phosphorylation assays

    PMID:41850398

    Open questions at the time
    • Direct substrate in integrin signaling not identified
    • How DUSP22 promotes rather than inhibits SRC-family kinase signaling in neutrophils is mechanistically unresolved
  15. 2026 High

    Cardiac-specific DUSP22 knockout exacerbating doxorubicin cardiotoxicity through JNK-dependent mitophagy failure demonstrated tissue-specific protective roles via the DUSP22–JNK axis.

    Evidence Cardiac-specific DUSP22 KO and OE mouse models, JNK phosphorylation assays, mitophagy flux assays

    PMID:41950821

    Open questions at the time
    • Whether DUSP22 directly dephosphorylates JNK or acts through scaffold disassembly in cardiomyocytes is unclear
    • Mitophagy receptor target of DUSP22-JNK regulation not identified

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include how DUSP22 switches between phosphatase and scaffold modes in different cell types, the structural basis for its remarkably broad substrate recognition, and whether its positive role in neutrophil integrin signaling involves direct or indirect phosphatase activity.
  • No substrate-bound co-crystal structure to explain broad specificity
  • Cell-type-specific regulatory mechanisms (membrane targeting, post-translational modifications) controlling functional output are undefined
  • Relative physiological importance of scaffold versus phosphatase functions in vivo is not genetically dissected

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 10 GO:0098772 molecular function regulator activity 3 GO:0060090 molecular adaptor activity 2
Localization
GO:0005829 cytosol 1 GO:0005886 plasma membrane 1
Pathway
R-HSA-168256 Immune System 4 R-HSA-1643685 Disease 3 R-HSA-5357801 Programmed Cell Death 2
Partners
ASK1EGFRFAKJNK1LCKLGALS1MKK7UBR2
Complex memberships
ASK1-MKK7-JNK scaffold complex

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 DUSP22 (JSP-1) is a dual-specificity phosphatase that, contrary to expectation, activates rather than inactivates the MAPK JNK in transient cotransfection assays, functioning as a selective JNK activator (JNK Stimulatory Phosphatase-1). Transient cotransfection assay in mammalian cells, in vitro phosphatase characterization Proceedings of the National Academy of Sciences of the United States of America High 11717427
2002 DUSP22 (JKAP) specifically activates JNK but not p38 or ERK2; it associates with JNK and MKK7 (but not SEK1) in vivo but does not interact with JNK in vitro, indicating an indirect scaffolding-like mechanism. Targeted gene disruption abolished TNF-α- and TGF-β-induced JNK activation. Co-immunoprecipitation, overexpression and dominant-negative mutant (JKAP-C88S) in HEK293T cells, targeted gene disruption in murine ES cells, JNK activation assays The Journal of biological chemistry High 12138158
2001 DUSP22 (VHX) dephosphorylates ERK2 in vitro and suppresses TCR-induced ERK2 activation and NFAT/AP-1 reporter activity (but not NF-κB) when expressed in Jurkat T cells. In vitro phosphatase assay with ERK2, cotransfection with NFAT/AP-1 and NF-κB luciferase reporters in Jurkat T cells The Journal of biological chemistry High 11733513
2004 DUSP22 (VHX) is N-terminally myristoylated at Gly-2, and this myristoylation is required for its plasma membrane localization; mutation of the myristoylation site abrogates membrane targeting. Myristoylation site mutagenesis, subcellular localization by fluorescence microscopy in 293T and NIH-3T3 cells The Journal of biological chemistry High 15138252
2007 DUSP22 associates with estrogen receptor alpha (ERα) in vivo, dephosphorylates ERα at Ser-118, and suppresses ERα-mediated transcription; catalytically inactive DUSP22 mutants fail to suppress ERα activation. Co-immunoprecipitation in breast cancer cells (T47D), overexpression of WT and catalytic mutants, siRNA knockdown, ERα transcription reporter assays Oncogene High 17384676
2014 DUSP22 (JKAP) directly inactivates Lck by dephosphorylating its activating Tyr-394 residue during TCR signaling, thereby suppressing T-cell activation; JKAP-knockout mice develop enhanced T-cell responses and spontaneous autoimmunity. JKAP-knockout mouse model, in vitro dephosphorylation assay of Lck pTyr394, T-cell proliferation and cytokine production assays, adoptive transfer EAE model Nature communications High 24714587
2014 DUSP22 inhibits PKA activity and thereby regulates TAU phosphorylation status and CREB signaling in hippocampal neurons; DUSP22 promoter hypermethylation in Alzheimer's disease leads to its silencing and consequent PKA-dependent TAU hyperphosphorylation. DNA methylation profiling of human hippocampus, functional assays showing DUSP22 inhibition of PKA and effects on TAU phosphorylation and CREB activation Hippocampus Medium 24436131
2016 DUSP22 acts as a scaffold protein for the ASK1-MKK7-JNK signaling complex, selectively associating with ASK1, MKK7, and JNK1/2; this scaffold function increases JNK phosphorylation and apoptosis in a concentration-dependent biphasic manner independently of DUSP22 phosphatase activity. Co-immunoprecipitation of ASK1, MKK7, and JNK with DUSP22; phosphatase-dead DUSP22 mutant overexpression; concentration-dependent JNK phosphorylation and apoptosis assays in mammalian cells PloS one Medium 27711255
2019 DUSP22 interacts with EGFR and dephosphorylates it, suppressing ERK1/2 signaling; DUSP22 also interacts with androgen receptor (AR) and inhibits EGF-induced AR phosphorylation at Tyr534, suppressing prostate-specific antigen expression in prostate cancer cells. Co-immunoprecipitation, overexpression of DUSP22 and catalytic mutants in prostate cancer cell lines, ERK1/2 and AR phosphorylation assays, colony formation assays FASEB journal Medium 31693867
2020 Crystal structure and NMR analysis of DUSP22 active site revealed that conserved residues D57 (D-loop), S93 (P-loop), and N128 (N-loop) form a hydrogen bonding network (DPN-triloop interaction) essential for catalytic activity; alanine mutations or somatic mutations at these positions reduce catalytic efficiency (kcat/KM) by >100-fold. X-ray crystallography, NMR spectroscopy, site-directed alanine mutagenesis, kinetic enzyme assays (kcat/KM measurements) International journal of molecular sciences High 33053837
2022 DUSP22 directly interacts with focal adhesion kinase (FAK) and dephosphorylates it at Tyr397 and Tyr576+Tyr577, inhibiting downstream ERK1/2 and NF-κB signaling to suppress NASH and HCC progression; both FAK binding and dephosphorylation are required for DUSP22's protective effects. Co-immunoprecipitation, in vitro dephosphorylation assays, hepatic-specific DUSP22 knockout and transgenic overexpression mouse models, AAV-mediated gene therapy, phosphorylation assays Nature communications High 36209205
2024 DUSP22 dephosphorylates UBR2 at specific serine residues, leading to ubiquitin-mediated UBR2 degradation; UBR2 in turn mediates Lys63-linked ubiquitination of Lck at Lys99 and Lys276, which is required for Lck Tyr394 phosphorylation and activation during TCR signaling. DUSP22 thus inhibits T-cell activation by destabilizing UBR2, a positive upstream regulator of Lck. Co-immunoprecipitation, single-cell RNA sequencing, ubiquitination assays (K63-linkage specific), phosphorylation assays, UBR2 knockout, mass spectrometry, human SLE patient samples Nature communications High 38225265
2024 DUSP22 inhibits lung tumorigenesis by dephosphorylating EGFR and suppressing downstream c-Met, ERK1/2, and PD-L1 signaling; DUSP22 deletion enhances EGFR-driven lung tumorigenesis and increases c-Met-dependent cancer cell migration. shRNA knockdown, exogenous DUSP22 expression, xenograft tumor models, EGFR phosphorylation assays, c-Met inhibitor rescue experiments, genetic deletion of DUSP22 Cell death discovery Medium 38877005
2023 DUSP22 directly interacts with AKT via its phosphatase domain and dephosphorylates AKT at Ser473 and Thr308, inhibiting AKT-driven proliferation and migration of non-small cell lung cancer cells; this effect requires DUSP22 phosphatase activity. Co-immunoprecipitation, in vitro kinase/phosphatase assays, AKT phosphorylation assays, cell viability and migration assays in A549 and H1299 cells Molecular carcinogenesis Medium 37937915
2025 DUSP22 is upregulated in sarcopenic muscle; targeting DUSP22 with knockdown or the small molecule BML-260 prevents muscle wasting by suppressing FOXO3a through downregulation of JNK, independently of Akt activation. DUSP22 knockdown in muscle cells, BML-260 pharmacological treatment, sarcopenia mouse models, JNK and FOXO3a phosphorylation assays, human skeletal muscle cell atrophy model EMBO molecular medicine Medium 40263624
2026 DUSP22 binds LGALS1 and dephosphorylates it at Ser8 and Thr58, leading to LGALS1 protein degradation and relief of LGALS1-mediated immunosuppression, thereby enhancing CD8+ T-cell infiltration into the tumor microenvironment. Genome-wide Sleeping Beauty transposon screen, mass spectrometry, Co-immunoprecipitation, phosphomimetic mutant experiments, flow cytometry, in vitro T-cell transendothelial migration assay, in vivo mouse models, bulk and single-cell RNA sequencing Journal for immunotherapy of cancer High 41611244
2026 DUSP22 (JSP1) is essential for integrin activation and adhesion in neutrophils during LPS/TNF-α-induced vascular inflammation; JSP1-knockout neutrophils show reduced SYK and HCK phosphorylation, consistent with impaired integrin-SRC signaling. JSP1-knockout mouse model (local Shwartzman reaction), neutrophil depletion and adoptive transfer experiments, integrin activation assays, SYK and HCK phosphorylation assays The Journal of biological chemistry High 41850398
2026 DUSP22 directly interacts with JNK, inhibits JNK phosphorylation, promotes mitophagy flux, improves mitochondrial quality, and reduces mitochondrial disorder-related apoptosis in cardiomyocytes; cardiac-specific DUSP22 knockout exacerbates doxorubicin-induced cardiotoxicity. Cardiac-specific DUSP22 knockout and overexpression mouse models, Western blot, immunofluorescence, RT-qPCR, JNK phosphorylation assays, mitophagy flux assays Biochimica et biophysica acta. Molecular basis of disease High 41950821
2010 NOTCH1 regulates DUSP22 expression by modulating promoter methylation through a nuclear complex controlling DNMT3A activity; NOTCH1 PEST domain mutations stabilize NOTCH1 signaling, leading to increased DUSP22 promoter methylation and silencing, which promotes CCL19-driven CLL cell chemotaxis. CRISPR/Cas9-generated cell line models, DNA methylation analysis, DNMT3A activity assays, chemotaxis assays, xenograft models Leukemia Medium 28017968
2017 In mouse fibroblast NIH3T3 cells, exogenous Myc-tagged DUSP22 is diffusely distributed in the cytoplasm and partially colocalizes with the actin cytoskeleton. Immunofluorescence microscopy with anti-Myc and actin co-staining in NIH3T3 cells Medical molecular morphology Low 29282540

Source papers

Stage 0 corpus · 67 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 The phosphatase JKAP/DUSP22 inhibits T-cell receptor signalling and autoimmunity by inactivating Lck. Nature communications 120 24714587
2018 Molecular profiling reveals immunogenic cues in anaplastic large cell lymphomas with DUSP22 rearrangements. Blood 101 30093402
2005 Rhodanine derivatives as inhibitors of JSP-1. Bioorganic & medicinal chemistry letters 97 15961311
2016 Morphologic Features of ALK-negative Anaplastic Large Cell Lymphomas With DUSP22 Rearrangements. The American journal of surgical pathology 93 26379151
2014 Promoter hypermethylation of the phosphatase DUSP22 mediates PKA-dependent TAU phosphorylation and CREB activation in Alzheimer's disease. Hippocampus 89 24436131
2002 The dual specificity JKAP specifically activates the c-Jun N-terminal kinase pathway. The Journal of biological chemistry 85 12138158
2001 Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1. Proceedings of the National Academy of Sciences of the United States of America 71 11717427
2001 Inhibition of T cell antigen receptor signaling by VHR-related MKPX (VHX), a new dual specificity phosphatase related to VH1 related (VHR). The Journal of biological chemistry 68 11733513
2007 DUSP22/LMW-DSP2 regulates estrogen receptor-alpha-mediated signaling through dephosphorylation of Ser-118. Oncogene 66 17384676
2016 Mutations in NOTCH1 PEST domain orchestrate CCL19-driven homing of chronic lymphocytic leukemia cells by modulating the tumor suppressor gene DUSP22. Leukemia 58 28017968
2016 Downregulation of the phosphatase JKAP/DUSP22 in T cells as a potential new biomarker of systemic lupus erythematosus nephritis. Oncotarget 52 27557500
2022 Hepatocyte phosphatase DUSP22 mitigates NASH-HCC progression by targeting FAK. Nature communications 50 36209205
2017 JNK Pathway-Associated Phosphatase/DUSP22 Suppresses CD4+ T-Cell Activation and Th1/Th17-Cell Differentiation and Negatively Correlates with Clinical Activity in Inflammatory Bowel Disease. Frontiers in immunology 46 28725226
2016 Molecular alterations and tumor suppressive function of the DUSP22 (Dual Specificity Phosphatase 22) gene in peripheral T-cell lymphoma subtypes. Oncotarget 41 27626696
2018 Hypomethylation of CYP2E1 and DUSP22 Promoters Associated With Disease Activity and Erosive Disease Among Rheumatoid Arthritis Patients. Arthritis & rheumatology (Hoboken, N.J.) 36 29287311
2018 Genetic vulnerability to DUSP22 promoter hypermethylation is involved in the relation between in utero famine exposure and schizophrenia. NPJ schizophrenia 33 30131491
2016 Scaffold Role of DUSP22 in ASK1-MKK7-JNK Signaling Pathway. PloS one 33 27711255
2023 DUSP22 rearrangement is associated with a distinctive immunophenotype but not outcome in patients with systemic ALK-negative anaplastic large cell lymphoma. Haematologica 27 36453104
2021 Striking Association of Lymphoid Enhancing Factor (LEF1) Overexpression and DUSP22 Rearrangements in Anaplastic Large Cell Lymphoma. The American journal of surgical pathology 27 33165091
2004 VHY, a novel myristoylated testis-restricted dual specificity protein phosphatase related to VHX. The Journal of biological chemistry 24 15138252
2021 JKAP, Th1 cells, and Th17 cells are dysregulated and inter-correlated, among them JKAP and Th17 cells relate to cognitive impairment progression in Alzheimer's disease patients. Irish journal of medical science 22 34595688
2021 JKAP relates to disease risk, severity, and Th1 and Th17 differentiation in Parkinson's disease. Annals of clinical and translational neurology 19 34289265
2024 The phosphatase DUSP22 inhibits UBR2-mediated K63-ubiquitination and activation of Lck downstream of TCR signalling. Nature communications 18 38225265
2019 DUSP22 suppresses prostate cancer proliferation by targeting the EGFR-AR axis. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 18 31693867
2022 The longitudinal changes of serum JKAP and IL-17A, and their linkage with anxiety, depression, and cognitive impairment in acute ischemic stroke patients. Journal of clinical laboratory analysis 13 36397283
2024 Exosomal miR-1228-5p down-regulates DUSP22 to promotes cell proliferation and migration in small cell lung cancer. Life sciences 12 38851418
2022 JKAP serves as a potential biomarker for the evaluation of inflammatory condition, disease activity, and treatment response to TNF inhibitor in ankylosing spondylitis patients. Modern rheumatology 10 34918117
2007 Quinoxalinylurea derivatives as a novel class of JSP-1 inhibitors. Bioorganic & medicinal chemistry letters 10 17303416
2015 Expression of the chemokine receptor gene, CCR8, is associated With DUSP22 rearrangements in anaplastic large cell lymphoma. Applied immunohistochemistry & molecular morphology : AIMM 9 25390351
2021 JKAP correlates with lower disease risk and inflammation, and its increment during etanercept treatment associates with commendable treatment efficiency in rheumatoid arthritis patients. European review for medical and pharmacological sciences 8 33829452
2021 Patch/plaque mycosis-fungoides-like presentations of DUSP22-translocated T-cell lymphomas. Journal of cutaneous pathology 8 34699105
2020 Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases. International journal of molecular sciences 8 33053837
1976 Effect of VHa locus allotype-suppression on the expression of closely linked VHx, VHy, and Cmun genes in heterozygous rabbits. Journal of immunology (Baltimore, Md. : 1950) 8 1245736
2023 Lymphomatoid papulosis with DUSP22-IRF4 rearrangement: A case report and literature review. Journal of cutaneous pathology 7 36944579
2017 Expression analyses of Dusp22 (Dual-specificity phosphatase 22) in mouse tissues. Medical molecular morphology 7 29282540
2024 DUSP22 Ameliorates Endothelial-to-Mesenchymal Transition in HUVECs through Smad2/3 and MAPK Signaling Pathways. Cardiovascular therapeutics 6 38495810
2022 Clinical value of serum JKAP in acute ischemic stroke patients. Journal of clinical laboratory analysis 6 35274367
2022 Cutaneous presentation of enteropathy-associated T-cell lymphoma masquerading as a DUSP22-rearranged CD30+ lymphoproliferation. Virchows Archiv : an international journal of pathology 6 35366115
2021 Central nervous system ALK-negative anaplastic large cell lymphoma with IRF4/DUSP22 rearrangement. Brain tumor pathology 6 34791573
2020 Reduced JKAP correlates with advanced disease features, inflammation, as well as increased exacerbation risk and severity in asthmatic children. Irish journal of medical science 6 33156444
2025 BMSC exosomes deliver JKAP to restore Th17/Treg balance via AKT/ERK, alleviating rheumatoid arthritis. iScience 5 40687841
2021 Primary cutaneous anaplastic large-cell lymphoma with DUSP22-IRF4 rearrangement following insect bites. Journal of cutaneous pathology 5 34622970
2019 DUSP22-IRF4 rearrangement in AIDS-associated ALK-negative anaplastic large cell lymphoma. BMJ case reports 5 31570354
2025 Modulating phosphatase DUSP22 with BML-260 ameliorates skeletal muscle wasting via Akt independent JNK-FOXO3a repression. EMBO molecular medicine 4 40263624
2024 DUSP22-rearranged primary cutaneous CD30-positive T-cell lymphoproliferative disorders and adult T-cell leukemia/lymphoma frequently share the LEF1+/TIA1- immunophenotype. Human pathology 4 38971328
2023 DUSP22-IRF4 Rearranged CD30-Positive Primary Cutaneous Lymphoproliferative Disorder With Gamma/Delta Phenotype. The American Journal of dermatopathology 4 37883980
2024 DUSP22 inhibits lung tumorigenesis by suppression of EGFR/c-Met signaling. Cell death discovery 3 38877005
2021 DUSP22 promotes senescence of HS-1 skin cancer cells through triggering MAPK signaling pathway. European review for medical and pharmacological sciences 3 33629281
2019 [Detection of chromosomal translocations of DUSP22 and TP63 in ALK-negative anaplastic large cell lymphoma by fluorescence in situ hybridization and related clinical relevance]. Zhonghua bing li xue za zhi = Chinese journal of pathology 3 31594044
2018 DUSP22 promotes senescence of HS-1 skin cancer cells through triggering MAPK signaling pathway. European review for medical and pharmacological sciences 3 30536326
2023 Vesicular Lymphomatoid Papulosis With DUSP22-IRF4 Rearrangement on Chromosome 6p25.3: A Case Report. The American Journal of dermatopathology 2 36939126
2023 Anaplastic large cell lymphomas with equivocal DUSP22 FISH results: recommendations for clinical reporting and diagnostic evaluation. Human pathology 2 37633531
2023 DUSP22 suppresses tumor progression by directly dephosphorylating AKT in non-small cell lung cancer. Molecular carcinogenesis 2 37937915
2024 Serum JKAP reflects Th2 and Th17 cell levels, and diabetic nephropathy risk and severity in diabetes mellitus patients. Biomarkers in medicine 1 38179996
2024 Circulating JKAP levels may correlate with postpartum anxiety and depression through its interaction with T helper 17 cells. Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas 1 39383378
2023 Constant small-cell changes and variable LEF1 expression in DUSP22-rearranged primary cutaneous anaplastic large-cell lymphoma: Analysis of the repeated biopsies of three patients. Pathology international 1 37530485
2023 Primary cutaneous CD30+ lymphoproliferative disorders with DUSP22 translocation. Pathologie (Heidelberg, Germany) 1 38010388
2022 Systemic ALK-negative anaplastic large cell lymphoma with distinctive myxoid change and DUSP22 rearrangement. Virchows Archiv : an international journal of pathology 1 35879438
2022 Primary effusion anaplastic large cell lymphoma with indolent clinical course and IRF4/DUSP22 rearrangement: a case report expanding the spectrum of effusion-based lymphoma. Virchows Archiv : an international journal of pathology 1 35984488
2026 DUSP22 dephosphorylates LGALS1 to enhance T cell-driven antitumor immunity. Journal for immunotherapy of cancer 0 41611244
2026 Dual Specificity Phosphatase (DUSP22) promoter hypomethylation in cell-free DNA is associated with rheumatoid arthritis and its radiographic severity. Frontiers in medicine 0 41709899
2026 The dual-specificity phosphatase JSP1 regulates neutrophil adhesion via integrin-SRC signaling in vascular inflammation. The Journal of biological chemistry 0 41850398
2026 Dusp22 deficiency in cardiomyocytes exacerbates doxorubicin-induced cardiotoxicity by aggravating mitochondria-dependent apoptosis via JNK pathway. Biochimica et biophysica acta. Molecular basis of disease 0 41950821
2025 JSP1 Regulates Neutrophil Adhesion via Integrin-SRC Signaling in Vascular Inflammation. bioRxiv : the preprint server for biology 0 40950139
2025 CD30-Positive Lymphoproliferative Disorder With DUSP22-IRF4 Rearrangement and Gamma-Delta T-Cell Phenotype: A Novel Indolent Presentation. Journal of cutaneous pathology 0 41189357
2024 Small cell pattern of ALK-negative anaplastic large cell lymphoma with double-hit rearrangements of DUSP22 and TP63. EJHaem 0 39157603
2024 Lymphomatoid Papulosis With DUSP22 Rearrangement in a Patient With a Historical Diagnosis of Primary Cutaneous Anaplastic Large Cell Lymphoma. Cureus 0 39221352