Affinage

DUSP22

Dual specificity protein phosphatase 22 · UniProt Q9NRW4

Length
184 aa
Mass
20.9 kDa
Annotated
2026-06-09
67 papers in source corpus 23 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 5/5 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DUSP22 is a myristoylated dual-specificity phosphatase that operates as both a catalytic enzyme and a non-catalytic scaffold to regulate MAP kinase signaling, T cell activation, and tumor suppression across multiple tissues (PMID:12138158, PMID:24714587, PMID:27711255). Its phosphatase activity depends on a DPN-triloop hydrogen-bonding network (D57, S93, N128) that positions the active-site loops for catalysis, and N-terminal myristoylation at Gly-2 directs it to the plasma membrane (PMID:33053837, PMID:15138252). Catalytically, DUSP22 directly dephosphorylates a range of substrates to restrain growth and inflammatory signaling: it inactivates Lck at the activating Tyr394 to suppress TCR signaling, dephosphorylates the E3 ligase UBR2 to block UBR2-driven K63-ubiquitination and activation of Lck, dephosphorylates ERα at Ser118, EGFR, FAK at Tyr397/576/577, and AKT at Ser473/Thr308, and removes phosphates from Galectin-1 (Ser8/Thr58) to drive its degradation and relieve tumor-microenvironment immunosuppression (PMID:24714587, PMID:38225265, PMID:17384676, PMID:36209205, PMID:37937915, PMID:41611244). Independently of catalysis, DUSP22 acts as a scaffold assembling ASK1–MKK7–JNK complexes to promote JNK activation and JNK-dependent apoptosis in a concentration-dependent manner (PMID:27711255, PMID:12138158). Through these activities DUSP22 functions as a negative regulator of TCR signaling whose loss promotes T cell hyperactivation and autoimmunity, as a tumor suppressor in peripheral T-cell lymphoma, and as a protective factor limiting NASH/HCC progression and doxorubicin cardiotoxicity (PMID:24714587, PMID:38225265, PMID:27626696, PMID:36209205, PMID:41950821).

Mechanistic history

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

    Established DUSP22 as a dual-specificity phosphatase and a negative regulator of TCR-triggered MAP kinase signaling, framing it as a potential brake on T cell activation.

    Evidence In vitro ERK2 dephosphorylation assay and NFAT/AP-1 reporter assays in Jurkat T cells

    PMID:11733513

    Open questions at the time
    • Direct physiological substrate in T cells not yet identified
    • Mechanism of MAPK selectivity unresolved
  2. 2002 High

    Resolved the paradox of a phosphatase activating JNK by showing DUSP22 acts through an indirect scaffolding mechanism, associating with JNK and MKK7 in vivo but not binding JNK directly in vitro.

    Evidence Overexpression and C88S dominant-negative analysis in HEK293T, ES-cell gene disruption, Co-IP, and in vitro binding assays

    PMID:12138158

    Open questions at the time
    • Stoichiometry and composition of the scaffold complex not defined
    • Whether scaffold and catalytic functions act on the same pathway in vivo unclear
  3. 2004 Medium

    Defined how DUSP22 reaches its site of action by establishing Gly-2 myristoylation as the determinant of plasma membrane localization.

    Evidence Gly-2 mutagenesis with subcellular localization imaging and biochemical confirmation of myristoylation in 293T/NIH-3T3 cells

    PMID:15138252

    Open questions at the time
    • Functional consequence of membrane targeting for specific substrates not tested
    • Regulation of myristoylation not addressed
  4. 2007 High

    Demonstrated a catalytic substrate beyond MAPKs, linking DUSP22 to hormone signaling by showing it dephosphorylates ERα Ser118 to suppress estrogen-driven transcription.

    Evidence Reciprocal endogenous Co-IP, siRNA and overexpression, phospho-Ser118 Western blot, and catalytic-mutant reporter assays in T47D cells

    PMID:17384676

    Open questions at the time
    • In vivo relevance to breast tissue not established
    • Whether ERα is a direct enzymatic substrate vs. complex effect not fully separated
  5. 2014 High

    Identified Lck Tyr394 as a direct substrate and established DUSP22 as a T cell-intrinsic negative regulator of TCR signaling with autoimmune consequences in vivo.

    Evidence JKAP-knockout mice, in vitro Lck pTyr394 dephosphorylation assay, T cell functional assays, adoptive transfer, and EAE model

    PMID:24714587

    Open questions at the time
    • Membrane recruitment relative to Lck not mechanistically connected
    • Upstream regulators of DUSP22 in T cells unknown at this stage
  6. 2016 Medium

    Separated DUSP22's catalytic and scaffold functions by showing phosphatase-dead DUSP22 still assembles ASK1-MKK7-JNK complexes and drives JNK apoptosis in a bell-shaped, scaffold-characteristic manner; in parallel established DUSP22 as a tumor suppressor in T-cell lymphoma.

    Evidence Co-IP of ASK1/MKK7/JNK1/2, phosphatase-dead mutant titration and apoptosis assays; lentiviral re-expression rescue with clonogenicity and xenograft assays

    PMID:27626696 PMID:27711255

    Open questions at the time
    • Concentration thresholds in vivo unknown
    • How scaffold pro-apoptotic role reconciles with TCR-suppressive role not integrated
  7. 2019 Medium

    Extended the catalytic repertoire to receptor tyrosine kinase signaling by showing DUSP22 dephosphorylates EGFR and antagonizes AR phosphorylation, with reciprocal ERK1/2 regulation in prostate cancer.

    Evidence Exogenous expression, phospho-specific Western blot (EGFR, ERK1/2, AR Tyr534), Co-IP with AR, and Ser58Ala mutagenesis with colony formation assays

    PMID:31693867

    Open questions at the time
    • Whether AR is a direct substrate or indirect target unclear
    • In vivo prostate cancer relevance not tested
  8. 2020 High

    Provided the structural basis for catalysis, defining the DPN-triloop (D57, S93, N128) network required for active-site formation.

    Evidence Crystal structure and NMR of DUSP22 mutants with site-directed alanine mutagenesis and kcat/KM kinetics

    PMID:33053837

    Open questions at the time
    • Substrate-bound structures not determined
    • Structural basis of substrate selectivity not resolved
  9. 2022 High

    Established DUSP22 as a protective factor in liver disease by identifying FAK (Tyr397, Tyr576/577) as a direct hepatocyte substrate controlling ERK1/2 and NF-κB to limit NASH-HCC progression.

    Evidence Hepatic-specific KO and transgenic OE mice, AAV gene delivery, Co-IP with FAK, and phospho-specific Western blots in NASH/HCC models

    PMID:36209205

    Open questions at the time
    • Tissue specificity of FAK substrate preference vs. other tissues unclear
    • Translational dosing of AAV approach not defined
  10. 2023 Medium

    Added AKT (Ser473, Thr308) as a direct substrate, linking DUSP22 to PI3K-AKT-driven proliferation and migration in NSCLC.

    Evidence Co-IP, in vitro phosphatase assays, phospho-specific Western blots, and viability/migration assays in A549 and H1299 cells

    PMID:37937915

    Open questions at the time
    • In vivo lung tumor validation limited
    • Relative contribution vs. EGFR pathway in same cells not dissected
  11. 2024 High

    Resolved the upstream control of Lck by showing DUSP22 dephosphorylates UBR2, triggering its degradation and thereby blocking UBR2-mediated K63-ubiquitination and activation of Lck — extending the TCR-suppressive mechanism to human SLE T cells.

    Evidence Co-IP, scRNA-seq, UBR2 KO, site-specific K63-ubiquitination mapping (Lck Lys99/Lys276), DUSP22/UBR2 double-knockout epistasis, and SLE patient T cell analysis

    PMID:38225265

    Open questions at the time
    • Precise UBR2 serine sites and their structural context not fully mapped
    • Whether membrane localization gates UBR2 access not addressed
  12. 2024 High

    Connected DUSP22 to antitumor immunity by identifying Galectin-1 (Ser8/Thr58) as a substrate whose dephosphorylation and degradation relieves immunosuppression and boosts CD8+ T cell infiltration.

    Evidence Genome-wide Sleeping Beauty screen, MS-identified interaction validated by Co-IP, phosphomimetic mutagenesis, flow/IHC for CD8+ infiltration, and in vivo tumor models

    PMID:41611244

    Open questions at the time
    • Degradation pathway downstream of dephosphorylation not detailed
    • Combination with checkpoint blockade not tested
  13. 2024 Medium

    Broadened the functional reach to lung cancer EGFR/c-Met and PD-L1 biology and to endothelial biology, showing DUSP22 loss enhances RTK-driven migration and aggravates TGF-β-induced EndMT.

    Evidence Genetic deletion/knockdown and overexpression with phospho-specific readouts and inhibitor epistasis (gefitinib, cabozantinib) in lung cancer; OE/KD with pathway inhibitors in HUVEC EndMT model

    PMID:38495810 PMID:38877005

    Open questions at the time
    • EndMT placement relies on inhibitors without direct substrate (Low confidence)
    • Direct vs. indirect c-Met regulation not established
  14. 2025 Medium

    Implicated DUSP22 in tissue homeostasis beyond cancer/immunity, showing it drives muscle atrophy via JNK-FOXO3a and is protective in cardiomyocytes by dephosphorylating JNK to promote mitophagy.

    Evidence DUSP22 knockdown and BML-260 inhibition with JNK/FOXO3a readouts in muscle wasting models; cardiac-specific KO/OE mice, Co-IP with JNK, mitophagy and apoptosis assays in doxorubicin cardiotoxicity

    PMID:40263624 PMID:41950821

    Open questions at the time
    • Opposite directional effects on JNK across tissues not mechanistically reconciled
    • Whether catalytic or scaffold function dominates in each tissue unclear
  15. 2026 High

    Established a role in innate immunity by showing JSP1/DUSP22 is required for neutrophil integrin activation and vascular inflammatory injury, with reduced SYK/HCK phosphorylation in its absence.

    Evidence JSP1-knockout mice, Shwartzman vascular injury model, neutrophil depletion and adoptive transfer, and phospho-SYK/HCK Western blots

    PMID:40950139 PMID:41850398

    Open questions at the time
    • Direct substrate in the integrin-SRC pathway not identified
    • Whether DUSP22 acts catalytically or as scaffold in neutrophils unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How DUSP22 selects among its many catalytic substrates and toggles between catalytic and scaffold modes in a tissue- and context-specific manner remains unresolved.
  • No substrate-bound structure to explain selectivity
  • No unified model reconciling JNK-activating scaffold role with JNK-dephosphorylating catalytic role across tissues
  • Regulation of DUSP22 expression/localization upstream largely uncharacterized in the corpus

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 8 GO:0016787 hydrolase activity 2 GO:0060090 molecular adaptor activity 2 GO:0098772 molecular function regulator activity 2
Localization
GO:0005829 cytosol 1 GO:0005886 plasma membrane 1
Pathway
R-HSA-162582 Signal Transduction 5 R-HSA-168256 Immune System 4 R-HSA-1643685 Disease 2 R-HSA-5357801 Programmed Cell Death 2
Partners
AKT1EGFRESR1LCKLGALS1MAP2K7MAP3K5MAPK8PTK2UBR2
Complex memberships
ASK1-MKK7-JNK signaling complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 DUSP22/JSP-1 (VHX) is a dual-specificity phosphatase that 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, identifying it as a negative regulator of TCR-triggered MAP kinase signaling. In vitro phosphatase assay with ERK2 substrate; transient transfection in Jurkat T cells with NFAT/AP-1 and NF-κB luciferase reporters; Western blot for ERK2 phosphorylation The Journal of Biological Chemistry Medium 11733513
2001 DUSP22/JSP-1 functions as a selective activator of JNK (not ERK or p38) in transient co-transfection assays in human cells, contrary to the expected MAPK-inactivating role of dual-specificity phosphatases. Transient co-transfection overexpression assays in human cells; MAPK activity measurements for JNK, ERK, and p38 Proceedings of the National Academy of Sciences of the United States of America Medium 11717427
2002 Murine JKAP/DUSP22 specifically activates JNK but not p38 or ERK2 upon overexpression in HEK293T cells; a catalytically inactive mutant (C88S) blocks TNF-α-induced JNK activation. Targeted gene disruption in embryonic stem cells abolished JNK activation by TNF-α and TGF-β but not UV-C. JKAP associated with JNK and MKK7 (but not SEK1) in vivo (co-immunoprecipitation), but did not interact with JNK in vitro, indicating an indirect scaffolding mechanism. Overexpression in HEK293T cells; catalytic mutant (C88S) dominant-negative analysis; targeted gene disruption in murine ES cells; co-immunoprecipitation; in vitro binding assay The Journal of Biological Chemistry High 12138158
2005 Rhodanine-based compounds are potent and selective inhibitors of JSP-1/DUSP22 phosphatase enzymatic activity, establishing DUSP22 as a druggable dual-specificity phosphatase. In vitro enzymatic inhibition assay with synthesized rhodanine derivatives against JSP-1 and other DSP family members Bioorganic & Medicinal Chemistry Letters Medium 15961311
2004 DUSP22/VHX is N-terminally myristoylated at Gly-2, and this modification is required for its membrane localization; mutation of the myristoylation site Gly-2 abrogated plasma membrane targeting. Mutagenesis of Gly-2 myristoylation site; subcellular localization imaging in 293T and NIH-3T3 cells; biochemical confirmation of myristoylation The Journal of Biological Chemistry Medium 15138252
2007 DUSP22 associates with estrogen receptor alpha (ERα) in vivo (co-immunoprecipitation in ERα-positive breast cancer T47D cells) and dephosphorylates ERα at Ser-118, thereby suppressing ERα-mediated transcription. Catalytically inactive DUSP22 mutants failed to suppress E2-induced ERα phosphorylation and transcription; siRNA knockdown of DUSP22 enhanced ERα-mediated gene expression. Co-immunoprecipitation of endogenous proteins; overexpression and siRNA knockdown; phospho-specific Western blot for ERα Ser-118; transcriptional reporter assays; catalytic mutant analysis Oncogene High 17384676
2014 JKAP/DUSP22 directly inactivates Lck by dephosphorylating its activating Tyr-394 residue during TCR signalling. JKAP-knockout T cells display enhanced proliferation and cytokine production. JKAP-knockout mice are more susceptible to EAE, and adoptive transfer of knockout T cells exacerbates EAE, establishing JKAP as a negative regulator of TCR signalling in vivo. JKAP-knockout mice; in vitro phosphatase assay (dephosphorylation of Lck pTyr394); adoptive transfer experiments; T cell proliferation and cytokine production assays; EAE model Nature Communications High 24714587
2014 DUSP22 promoter hypermethylation in Alzheimer's disease hippocampus leads to reduced DUSP22 expression, which in turn increases PKA activity (since DUSP22 inhibits PKA), resulting in elevated TAU phosphorylation and altered CREB signaling. DNA methylation profiling of human hippocampus; functional assays demonstrating DUSP22 inhibition of PKA activity and effects on TAU phosphorylation and CREB signaling Hippocampus Medium 24436131
2016 DUSP22 acts as a scaffold protein for the ASK1-MKK7-JNK signaling pathway independently of its phosphatase catalytic activity at low concentrations. DUSP22 selectively associates with ASK1, MKK7, and JNK1/2 (co-immunoprecipitation), and increases JNK phosphorylation and JNK-mediated apoptosis in a bell-shaped concentration-dependent manner characteristic of scaffold proteins, even when phosphatase activity is abolished. Co-immunoprecipitation of DUSP22 with ASK1, MKK7, JNK1/2; overexpression at varying concentrations; phosphatase-dead mutant analysis; apoptosis assays PloS One Medium 27711255
2016 Restoring DUSP22 expression in DUSP22-deficient malignant T cells inhibits cellular expansion by stimulating apoptosis and impairs soft agar clonogenicity and tumorigenicity, establishing DUSP22 as a tumor suppressor in peripheral T-cell lymphoma. Lentiviral re-expression of DUSP22 in DUSP22-deficient T-cell lymphoma cells; apoptosis assays; soft agar clonogenicity assay; xenograft tumorigenicity assay Oncotarget Medium 27626696
2019 DUSP22 directly dephosphorylates EGFR and suppresses downstream ERK1/2 signaling in prostate cancer cells. DUSP22 also physically interacts with androgen receptor (AR) and interferes with EGF-induced AR phosphorylation at Tyr534, suppressing AR-dependent signaling. A Ser58Ala mutation in DUSP22 (targeting an ERK1/2 phosphorylation site) was sufficient to suppress growth in cells with elevated p-ERK1/2, revealing a mutually antagonistic relationship between DUSP22 and ERK1/2. Exogenous DUSP22 expression in multiple prostate cancer cell lines; phospho-specific Western blot (EGFR, ERK1/2, AR Tyr534); co-immunoprecipitation of DUSP22 with AR; Ser58Ala mutagenesis; colony formation assays FASEB Journal Medium 31693867
2020 DUSP22 active site formation requires a DPN-triloop hydrogen bonding network involving D57 (D-loop), S93 (P-loop), and N128 (N-loop). Alanine or somatic mutations of any of these residues reduce catalytic efficiency (kcat/KM) by >100-fold. NMR and crystal structures show each residue stabilizes correct positioning of the three loops for substrate interaction and catalysis. Crystal structure and NMR of DUSP22 mutants; site-directed alanine mutagenesis of D57, S93, N128; in vitro kinetic assay (kcat/KM measurement) International Journal of Molecular Sciences High 33053837
2022 Hepatocyte DUSP22 directly interacts with focal adhesion kinase (FAK) and dephosphorylates FAK at Tyr397 and Tyr576+577, subsequently inhibiting downstream ERK1/2 and NF-κB signaling to suppress NASH and HCC progression. Hepatic-specific DUSP22 deletion exacerbates lipid deposition, inflammation, and fibrosis; overexpression or AAV-mediated gene delivery inhibits NASH-related phenotypes. Hepatic-specific DUSP22 knockout and transgenic overexpression mice; AAV/lentivirus gene therapy; co-immunoprecipitation of DUSP22 with FAK; phospho-specific Western blot (FAK Tyr397, Tyr576+577); ERK1/2 and NF-κB activity assays; NASH/HCC models Nature Communications High 36209205
2024 DUSP22 dephosphorylates the E3 ubiquitin ligase UBR2 at specific serine residues, targeting it for ubiquitin-mediated degradation. UBR2 in turn induces Lys63-linked ubiquitination of Lck at Lys99 and Lys276, promoting subsequent Lck Tyr394 phosphorylation and activation downstream of TCR signalling. Inflammatory phenotypes from TCR-triggered Lck activation or DUSP22 knockout are attenuated by UBR2 genomic deletion, establishing UBR2 as a positive upstream regulator of Lck that is negatively controlled by DUSP22. Co-immunoprecipitation; single-cell RNA sequencing; UBR2 loss-of-function (KO); site-specific ubiquitination assays (K63-linkage at Lys99, Lys276 of Lck); phospho-specific Western blot (Lck Tyr394); epistasis by double knockout (DUSP22 KO + UBR2 KO); analysis of human SLE patient T cells Nature Communications High 38225265
2023 DUSP22 directly interacts with AKT via its phosphatase domain and dephosphorylates AKT at Ser473 and Thr308, inhibiting AKT-dependent proliferation and migration of NSCLC cells. This inhibitory effect is contingent upon DUSP22 phosphatase activity. Co-immunoprecipitation; in vitro kinase/phosphatase assays; phospho-specific Western blot (AKT Ser473, Thr308); DUSP22 overexpression in A549 and H1299 cells; cell viability and migration assays Molecular Carcinogenesis Medium 37937915
2024 DUSP22 dephosphorylates EGFR and suppresses c-Met signaling in lung cancer cells; DUSP22 loss enhances EGFR/c-Met and PD-L1-dependent migration. Gefitinib (EGFR inhibitor) suppresses migration induced by DUSP22 deletion and inhibits c-Met activity; cabozantinib (c-Met inhibitor) reduces migration and attenuates EGFR activation from DUSP22 loss. Exogenous DUSP22 expression; shRNA knockdown; genetic DUSP22 deletion; phospho-specific Western blot (EGFR, ERK1/2, c-Met); colony formation and migration assays; xenograft tumor growth Cell Death Discovery Medium 38877005
2024 DUSP22 binds to Galectin-1 (LGALS1) and dephosphorylates it at Ser8 and Thr58, leading to LGALS1 degradation and relief of LGALS1-mediated immunosuppression in the tumor microenvironment, resulting in increased CD8+ T cell infiltration and enhanced antitumor immunity. Genome-wide Sleeping Beauty transposon screen; mass spectrometry identification of DUSP22-LGALS1 interaction; co-immunoprecipitation validation; phosphomimetic mutant experiments for Ser8/Thr58; flow cytometry and IHC for CD8+ T cell infiltration; in vitro T cell transendothelial migration assay; in vivo mouse tumor models Journal for Immunotherapy of Cancer High 41611244
2025 In skeletal muscle, DUSP22 is upregulated in sarcopenia and models of muscle wasting; DUSP22 knockdown or treatment with BML-260 prevents muscle atrophy by suppressing FOXO3a via downregulation of JNK, independently of Akt activation. Targeting DUSP22 reduces JNK-mediated FOXO3a activation. DUSP22 knockdown in skeletal muscle cells; BML-260 pharmacological inhibition; JNK activity and FOXO3a phosphorylation Western blots; multiple muscle wasting model systems including human skeletal muscle cells EMBO Molecular Medicine Medium 40263624
2026 JSP1/DUSP22 is essential for neutrophil integrin activation and adhesion in vascular inflammation. JSP1-knockout mice show reduced LPS-TNFα-induced vascular hemorrhage; neutrophil depletion and adoptive transfer established that JSP1-expressing neutrophils mediate this injury. Reduced SYK and HCK phosphorylation in JSP1-knockout neutrophils is consistent with impaired integrin-SRC signaling. JSP1-knockout mouse model; local Shwartzman reaction (LPS-TNFα vascular injury); neutrophil depletion; adoptive transfer of JSP1-expressing neutrophils; phospho-SYK and phospho-HCK Western blot; integrin activation assays The Journal of Biological Chemistry High 40950139 41850398
2026 DUSP22 directly interacts with JNK in cardiomyocytes and inhibits JNK phosphorylation. Cardiac-specific DUSP22 knockout exacerbates doxorubicin-induced cardiotoxicity and increases mortality; cardiac-specific overexpression is protective. Mechanistically, DUSP22 dephosphorylation of JNK promotes mitophagy flux, improves mitochondrial quality, and reduces mitochondria-dependent apoptosis. Cardiac-specific Dusp22 knockout and overexpression mice; doxorubicin cardiotoxicity model; Western blot for JNK phosphorylation; co-immunoprecipitation of DUSP22 with JNK; mitophagy assays; apoptosis assays; immunofluorescence Biochimica et Biophysica Acta - Molecular Basis of Disease Medium 41950821
2024 DUSP22 ameliorates TGF-β-induced endothelial-to-mesenchymal transition (EndMT) in HUVECs; DUSP22 deficiency aggravates EndMT while overexpression ameliorates it, acting through Smad2/3 and MAPK signaling pathways. TGF-β-induced EndMT model in HUVECs; DUSP22 overexpression and knockdown; signaling pathway inhibitors; Western blot for EndMT markers and pathway activation Cardiovascular Therapeutics Low 38495810
2017 DUSP22 is expressed in mouse tissues with a tissue-dependent profile; in NIH3T3 fibroblasts, endogenous and Myc-tagged Dusp22 are diffusely distributed in the cytoplasm, and overexpressed Myc-Dusp22 partially co-localizes with the actin cytoskeleton. Specific anti-Dusp22 antibody generation; Western blotting of mouse tissues; immunofluorescence localization 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 122 24714587
2018 Molecular profiling reveals immunogenic cues in anaplastic large cell lymphomas with DUSP22 rearrangements. Blood 103 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 95 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 87 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 73 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 69 11733513
2007 DUSP22/LMW-DSP2 regulates estrogen receptor-alpha-mediated signaling through dephosphorylation of Ser-118. Oncogene 67 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 54 27557500
2022 Hepatocyte phosphatase DUSP22 mitigates NASH-HCC progression by targeting FAK. Nature communications 53 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 48 28725226
2016 Molecular alterations and tumor suppressive function of the DUSP22 (Dual Specificity Phosphatase 22) gene in peripheral T-cell lymphoma subtypes. Oncotarget 42 27626696
2018 Hypomethylation of CYP2E1 and DUSP22 Promoters Associated With Disease Activity and Erosive Disease Among Rheumatoid Arthritis Patients. Arthritis & rheumatology (Hoboken, N.J.) 38 29287311
2018 Genetic vulnerability to DUSP22 promoter hypermethylation is involved in the relation between in utero famine exposure and schizophrenia. NPJ schizophrenia 34 30131491
2016 Scaffold Role of DUSP22 in ASK1-MKK7-JNK Signaling Pathway. PloS one 34 27711255
2023 DUSP22 rearrangement is associated with a distinctive immunophenotype but not outcome in patients with systemic ALK-negative anaplastic large cell lymphoma. Haematologica 28 36453104
2021 Striking Association of Lymphoid Enhancing Factor (LEF1) Overexpression and DUSP22 Rearrangements in Anaplastic Large Cell Lymphoma. The American journal of surgical pathology 28 33165091
2004 VHY, a novel myristoylated testis-restricted dual specificity protein phosphatase related to VHX. The Journal of biological chemistry 27 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
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 21 31693867
2024 The phosphatase DUSP22 inhibits UBR2-mediated K63-ubiquitination and activation of Lck downstream of TCR signalling. Nature communications 20 38225265
2021 JKAP relates to disease risk, severity, and Th1 and Th17 differentiation in Parkinson's disease. Annals of clinical and translational neurology 20 34289265
2024 Exosomal miR-1228-5p down-regulates DUSP22 to promotes cell proliferation and migration in small cell lung cancer. Life sciences 14 38851418
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
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
2020 Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases. International journal of molecular sciences 10 33053837
2015 Expression of the chemokine receptor gene, CCR8, is associated With DUSP22 rearrangements in anaplastic large cell lymphoma. Applied immunohistochemistry & molecular morphology : AIMM 10 25390351
2007 Quinoxalinylurea derivatives as a novel class of JSP-1 inhibitors. Bioorganic & medicinal chemistry letters 10 17303416
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
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
2024 DUSP22 Ameliorates Endothelial-to-Mesenchymal Transition in HUVECs through Smad2/3 and MAPK Signaling Pathways. Cardiovascular therapeutics 7 38495810
2024 DUSP22 inhibits lung tumorigenesis by suppression of EGFR/c-Met signaling. Cell death discovery 7 38877005
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
2025 Modulating phosphatase DUSP22 with BML-260 ameliorates skeletal muscle wasting via Akt independent JNK-FOXO3a repression. EMBO molecular medicine 6 40263624
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
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
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 4 31594044
2023 DUSP22 suppresses tumor progression by directly dephosphorylating AKT in non-small cell lung cancer. Molecular carcinogenesis 3 37937915
2021 DUSP22 promotes senescence of HS-1 skin cancer cells through triggering MAPK signaling pathway. European review for medical and pharmacological sciences 3 33629281
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
2026 DUSP22 dephosphorylates LGALS1 to enhance T cell-driven antitumor immunity. Journal for immunotherapy of cancer 1 41611244
2026 The dual-specificity phosphatase JSP1 regulates neutrophil adhesion via integrin-SRC signaling in vascular inflammation. The Journal of biological chemistry 1 41850398
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 Lymphomatoid Papulosis With DUSP22 Rearrangement in a Patient With a Historical Diagnosis of Primary Cutaneous Anaplastic Large Cell Lymphoma. Cureus 1 39221352
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 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 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

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