Affinage

DUSP16

Dual specificity protein phosphatase 16 · UniProt Q9BY84

Length
665 aa
Mass
73.1 kDa
Annotated
2026-04-28
38 papers in source corpus 23 papers cited in narrative 23 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DUSP16 (MKP-7) is a dual-specificity MAPK phosphatase that serves as a critical negative regulator of JNK and p38 signaling, thereby controlling inflammatory cytokine production, immune cell differentiation, neural progenitor proliferation, cellular senescence, and apoptotic responses. DUSP16 preferentially dephosphorylates JNK and p38α/β but not ERK, and additionally functions as a catalytic-activity-independent cytoplasmic anchor that sequesters phosphorylated ERK and prevents its nuclear translocation; a key allosteric tyrosine (Y271) in the phosphatase domain is required for both catalytic activity and substrate binding (PMID:11359773, PMID:20122898, PMID:36272649). The protein shuttles between cytoplasm and nucleus via NES/NLS motifs and is regulated at multiple levels: ERK-mediated Ser-446 phosphorylation stabilizes it against FBXL18-directed proteasomal degradation, Mycobacterium tuberculosis Eis acetylates Lys55 to inactivate it, and eNOS-derived S-nitrosylation similarly blocks its activity (PMID:15689616, PMID:22547814, PMID:19307591, PMID:40382593). Dusp16-deficient mice die perinatally with congenital obstructive hydrocephalus caused by neural progenitor overproliferation, and Dusp16-deficient macrophages overproduce TLR-induced cytokines including IL-12 through unrestrained JNK activation (PMID:29170629, PMID:24311790).

Mechanistic history

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

    Identification of DUSP16/MKP-7 as a JNK/p38-selective phosphatase established its substrate specificity and distinguished it from ERK-directed DUSPs, answering the question of which MAPKs it targets.

    Evidence Co-immunoprecipitation and overexpression kinase assays in cultured cells, replicated independently in two labs

    PMID:11359773 PMID:11489891

    Open questions at the time
    • Endogenous substrate preferences not confirmed at physiological expression levels
    • No structural basis for p38α/β vs p38γ/δ selectivity
  2. 2001 High

    Discovery that MKP-7 contains functional NES and NLS and shuttles between cytoplasm and nucleus resolved how a cytoplasmic phosphatase could be dynamically regulated by subcellular compartmentalization.

    Evidence Leptomycin B treatment, NES mutant expression, and subcellular fractionation in transfected cells

    PMID:11489891

    Open questions at the time
    • Physiological signals triggering nuclear import were not identified
    • Whether shuttling changes substrate access in vivo was untested
  3. 2005 High

    Demonstrating that ERK phosphorylates DUSP16 at Ser-446 to stabilize it against proteasomal degradation revealed a cross-MAPK feedback loop and established the first mechanism controlling DUSP16 protein turnover.

    Evidence 35S pulse-labeling, phospho-mimetic/deletion mutants, proteasome inhibitor treatment, and ubiquitin co-expression

    PMID:15689616

    Open questions at the time
    • The E3 ubiquitin ligase responsible was not identified at this time
    • In vivo relevance of the feedback loop was not tested
  4. 2005 High

    Linking DUSP16 to the β-arrestin 2/JNK3 scaffold complex explained how DUSP16 accesses activated JNK3 in a receptor-regulated, spatially organized manner following AT1aR stimulation.

    Evidence Reciprocal Co-IP with domain mapping, receptor stimulation time-course, and immunofluorescence colocalization on endocytic vesicles

    PMID:15888437

    Open questions at the time
    • Whether β-arrestin 2 interaction occurs for JNK1/2 substrates was not tested
    • Structural basis of the MKP7–β-arrestin interface unknown
  5. 2009 High

    Identification of S-nitrosylation by eNOS as an inactivating post-translational modification of DUSP16 established a redox-based regulatory mechanism linking NO signaling to JNK3-dependent endothelial migration.

    Evidence eNOS inhibition/knockdown, biotin-switch nitrosylation assay, and endothelial cell migration assay

    PMID:19307591

    Open questions at the time
    • The specific cysteine residue(s) modified were not identified
    • Whether S-nitrosylation occurs in non-endothelial cell types was not explored
  6. 2010 Medium

    Showing that catalytically dead DUSP16 still sequesters phospho-ERK in the cytoplasm revealed a phosphatase-independent scaffold function, broadening DUSP16's role beyond enzymatic dephosphorylation.

    Evidence Phosphatase-dead mutant overexpression with immunofluorescence and reporter gene assays

    PMID:20122898

    Open questions at the time
    • Physiological stoichiometry of DUSP16 vs ERK for scaffolding not assessed
    • Whether this scaffolding occurs under endogenous expression levels is unknown
  7. 2012 High

    Crystal structure-guided demonstration that Mtb Eis acetylates DUSP16 at Lys55 to suppress JNK-dependent autophagy and phagosome maturation provided a molecular mechanism for Mycobacterium immune evasion through host phosphatase inactivation.

    Evidence Crystal structures of Eis, in vitro acetyltransferase assays, site-directed mutagenesis, macrophage infection models

    PMID:22547814

    Open questions at the time
    • Whether DUSP16 acetylation at Lys55 occurs from endogenous host acetyltransferases unknown
    • Contribution relative to other Eis substrates not quantified
  8. 2013 High

    Gene-trap Dusp16 knockout mice revealed perinatal lethality and selective overproduction of TLR-induced IL-12 in macrophages via JNK1/2, establishing DUSP16 as an essential, non-redundant regulator of innate immune cytokine production in vivo.

    Evidence Gene trap KO mice, LPS challenge, cytokine ELISA, JNK pharmacological inhibition and siRNA rescue, bone marrow reconstitution

    PMID:24311790

    Open questions at the time
    • Cause of perinatal lethality not fully resolved (later attributed to hydrocephalus)
    • Whether other DUSPs compensate partially in specific tissues not determined
  9. 2011 High

    Selective expression of DUSP16 in Th2 cells and functional gain/loss experiments shifting Th1/Th2 balance established DUSP16 as an epigenetically regulated determinant of CD4+ T cell fate decisions.

    Evidence ChIP for histone acetylation at dusp16 promoter, adenoviral transduction with WT and dominant-negative DUSP16, transgenic mouse immunization

    PMID:21613215

    Open questions at the time
    • MAPK substrate specificity in Th2 skewing (JNK vs p38 contribution) not delineated
    • Whether DUSP16 is required for Th2 identity or only promotes it is unclear
  10. 2014 Medium

    Identification of PRAS40 and mTOR as direct DUSP16 substrates (dephosphorylated at Thr246 and Ser2248 respectively) linked DUSP16 to senescence regulation beyond the canonical MAPK pathway.

    Evidence Co-immunoprecipitation, phospho-specific western blots for PRAS40/mTOR, senescence assays in miR-17 transgenic mice

    PMID:25077541

    Open questions at the time
    • Direct in vitro phosphatase assay on PRAS40/mTOR not shown
    • Whether PRAS40/mTOR dephosphorylation is physiologically relevant outside senescence context unknown
  11. 2015 Medium

    Demonstrating that DUSP16 knockdown induces G1/S arrest and activates p53/Rb-dependent senescence, rescued only by catalytically active DUSP16, confirmed a phosphatase-dependent anti-senescence function.

    Evidence shRNA knockdown, BrdU incorporation, SA-β-gal assay, phosphatase-dead mutant rescue

    PMID:26381291

    Open questions at the time
    • Whether the senescence phenotype is JNK/p38-dependent or PRAS40/mTOR-dependent not resolved
    • In vivo relevance to organismal aging not tested
  12. 2017 Medium

    Dusp16 knockout mice developing congenital obstructive hydrocephalus from neural progenitor overproliferation revealed the essential role of DUSP16 in timing cell cycle exit during brain development.

    Evidence Dusp16−/− mouse model, BrdU/EdU incorporation, immunohistochemistry for progenitor and neuron markers, aqueduct histology

    PMID:29170629

    Open questions at the time
    • Which MAPK branch (JNK vs p38) drives progenitor overproliferation not determined
    • Whether this is the primary cause of perinatal lethality or one of multiple defects is uncertain
  13. 2021 High

    Establishing that DUSP16 suppresses chemotherapy-induced apoptosis by preventing BAX mitochondrial accumulation through JNK/p38 inactivation defined a targetable resistance mechanism in cancer cells.

    Evidence Overexpression/knockdown in multiple cancer cell lines, mitochondrial fractionation for BAX, phospho-MAPK western blots, cell death assays

    PMID:33863904

    Open questions at the time
    • Relative contribution of JNK vs p38 to BAX translocation not separated
    • Whether DUSP16 targeting sensitizes tumors in vivo not demonstrated
  14. 2022 High

    Identification of Tyr271 as a critical allosteric residue required for both catalytic activity and p38/JNK binding and cytoplasmic sequestration clarified the structural basis for substrate engagement and anchoring.

    Evidence Site-directed mutagenesis of Y271, in-cell dephosphorylation assays, Co-IP for MAPK binding, immunofluorescence for MAPK localization

    PMID:36272649

    Open questions at the time
    • Full crystal structure of DUSP16 phosphatase domain with bound MAPK substrate not available
    • Whether Y271 phosphorylation regulates activity in vivo unknown
  15. 2025 Medium

    Identification of FBXL18 as the E3 ubiquitin ligase that targets DUSP16 for proteasomal degradation closed a long-standing gap about which ligase controls DUSP16 turnover, connecting ubiquitin-proteasome regulation to JNK/c-JUN activation in cancer.

    Evidence Co-immunoprecipitation, ubiquitination assay, western blot, functional rescue of JNK activation by DUSP16 overexpression in endometrial carcinoma cells

    PMID:40382593

    Open questions at the time
    • Whether FBXL18 recognizes the ERK-phosphorylated Ser-446 degron or an independent motif is unknown
    • In vivo validation of FBXL18–DUSP16 axis in animal models not performed

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the full crystal structure of DUSP16 in complex with MAPK substrates, the identity of the S-nitrosylated cysteine(s), the relative contribution of JNK vs p38 to individual phenotypes (hydrocephalus, senescence, Th2 skewing), and whether the non-canonical substrates PRAS40/mTOR are direct physiological targets.
  • No full-length DUSP16 crystal structure available
  • Cysteine target of S-nitrosylation unidentified
  • JNK vs p38 pathway contributions not genetically separated in most disease models

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 7 GO:0008092 cytoskeletal protein binding 2 GO:0098772 molecular function regulator activity 1
Localization
GO:0005829 cytosol 5 GO:0005634 nucleus 2 GO:0031410 cytoplasmic vesicle 1
Pathway
R-HSA-162582 Signal Transduction 8 R-HSA-392499 Metabolism of proteins 3 R-HSA-168256 Immune System 2 R-HSA-5357801 Programmed Cell Death 2 R-HSA-1266738 Developmental Biology 1
Partners
ARRB2ERK2FBXL18JNK1JNK3MAPK14NR4A1TAK1

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 DUSP16/MKP-7 was identified as a novel dual-specificity phosphatase that binds to and inactivates JNK/SAPK and p38α/β MAPKs but not ERK; it is predominantly cytoplasmic when expressed in cultured cells; substrate specificity toward p38 isoforms was defined (α and β, but not γ or δ); the MAPK-docking site sequence was characterized. Co-immunoprecipitation, in-cell overexpression kinase assays, subcellular localization by immunofluorescence The Journal of biological chemistry High 11359773
2001 DUSP16/MKP-7 contains both a nuclear export signal (NES) and a nuclear localization signal (NLS) in its C-terminal stretch, making it the first leptomycin B-sensitive shuttle MKP; it resides exclusively in the cytoplasm under basal conditions but redistributes to the nucleus upon leptomycin B treatment or NES mutation; co-immunoprecipitation showed MKP-7 retains JNK/p38 in the cytoplasm. Leptomycin B treatment, NES mutant expression, subcellular fractionation/immunofluorescence, Co-IP The Journal of biological chemistry High 11489891
2005 ERK phosphorylates DUSP16/MKP-7 at Ser-446 in the C-terminal stretch (CTS), stabilizing the protein by reducing proteasome-mediated degradation; deletion of the CTS elongates MKP-7 half-life; MKP-7 is polyubiquitinated and degraded via the proteasome pathway. 35S-pulse labeling, proteasome inhibitor treatment, phospho-mimetic/deletion mutant expression, ubiquitin co-expression assay The Journal of biological chemistry High 15689616
2005 DUSP16/MKP-7 binds the JNK3 scaffold protein β-arrestin 2 via MKP7 amino acids 394–443 (same region that interacts with JIP-1); MKP7 dephosphorylates JNK3 bound to β-arrestin 2 following ASK1 overexpression or AT1aR stimulation; AT1aR stimulation causes rapid (within 5 min) dissociation of MKP7 from β-arrestin 2, followed by reassociation on endocytic vesicles at 30–60 min. Co-immunoprecipitation, deletion mapping, receptor stimulation assays, immunofluorescence colocalization The Journal of biological chemistry High 15888437
2009 miR-24 directly downregulates DUSP16/MKP-7, leading to enhanced phosphorylation of JNK and p38, stimulating myeloid cell proliferation and blocking granulocytic differentiation; this pathway is downstream of disrupted Runx1 subnuclear targeting. miRNA overexpression, western blot for phospho-JNK/p38, luciferase reporter, flow cytometry differentiation assays Cancer research Medium 19826043
2009 SDF-1α-induced activation of eNOS leads to S-nitrosylation of DUSP16/MKP7, rendering the phosphatase inactive, which permits JNK3 activation required for endothelial cell migration. eNOS inhibition/knockdown, nitrosylation assay, JNK3 activity assay, endothelial migration assay Proceedings of the National Academy of Sciences of the United States of America High 19307591
2010 MKP-7/DUSP16 blocks ERK-dependent nuclear gene activation by anchoring phosphorylated ERK in the cytoplasm, independent of its phosphatase catalytic activity toward ERK; a phosphatase-dead MKP-7 mutant similarly prolongs mitogen-induced ERK phosphorylation and prevents nuclear accumulation of phospho-ERK. Phosphatase-dead mutant overexpression, immunofluorescence colocalization, reporter gene assay, time-course ERK phosphorylation assays Biochemical and biophysical research communications Medium 20122898
2010 DUSP16 expression is silenced by CpG island methylation in Burkitt's lymphoma (BL), which abrogates a negative feedback loop limiting JNK activity; in BL cell lines with DUSP16 methylation, JNK activation is increased, and cells show enhanced sensitivity to JNK-activating agents. Bisulfite sequencing, methylation-specific PCR, western blot with phospho-JNK antibody, siRNA knockdown British journal of cancer Medium 20551953
2011 DUSP16 is selectively expressed in Th2 cells via histone H3/H4 acetylation at the dusp16 promoter; adenoviral overexpression of DUSP16 in naïve CD4+ T cells increased IL-4 and GATA-3 in Th2 and decreased IFNγ and T-bet in Th1 differentiation; dominant-negative DUSP16 had opposite effects; phosphatase activity is required for Th1/Th2 balance. ChIP, adenoviral transduction, dominant-negative mutant, cytokine ELISA, transgenic mouse immunization The Journal of biological chemistry High 21613215
2011 MKP-7/DUSP16 silencing by siRNA increased phospho-JNK and inhibited VCAM-1 (but not ICAM-1) expression in TNF-α-stimulated endothelial cells; this regulation was mediated via IRF-1 binding to the VCAM-1 promoter, as confirmed by ChIP assay. siRNA knockdown, western blot, ChIP assay, flow cytometry Cellular signalling Medium 22182512
2012 Mtb Eis protein acetylates Lys55 of DUSP16/MKP-7 (Nε-acetylation), which inhibits LPS-induced JNK phosphorylation; crystal structures of both Mtb and Msm Eis proteins explain the differential selectivity; this acetylation suppresses JNK-dependent autophagy, phagosome maturation, and ROS generation in macrophages. Biochemical acetyltransferase assay, crystal structure determination, site-directed mutagenesis, western blot for phospho-JNK, macrophage infection models Proceedings of the National Academy of Sciences of the United States of America High 22547814
2013 In a rat cerebral ischemia/reperfusion model, MKP-7 is upregulated at 4 h reperfusion; MKP-7 nuclear export is required for cytoplasmic JNK inactivation (leptomycin B blocking nuclear export upregulated JNK activity); MKP-7 regulates JNK independently of the PI3K/Akt pathway. siRNA knockdown, cycloheximide treatment, leptomycin B treatment, subcellular fractionation, western blot for phospho-JNK in rat ischemia model BMC neuroscience Medium 23280045
2013 PPARδ activation stabilizes DUSP16/MKP-7 mRNA (post-transcriptional mRNA stabilization), leading to suppression of JNK signaling and reduced UVB-induced MMP-1 secretion in human dermal fibroblasts and hairless mice. PPARδ siRNA knockdown, specific ligand treatment, western blot, mRNA stability assay, in vivo mouse model The Journal of investigative dermatology Medium 23639976
2013 Dusp16-deficient macrophages show selective overproduction of a subset of TLR-induced cytokines (including IL-12), mediated through enhanced JNK1/2 activation; JNK1/2 pharmacological inhibition or siRNA knockdown normalizes IL-12p40 secretion; Dusp16-deficient fibroblasts show enhanced p38 and JNK MAPK activation; homozygous Dusp16-deficient mice die perinatally. Gene trap mouse model, LPS challenge, cytokine ELISA, siRNA knockdown, pharmacological JNK inhibition, bone marrow reconstitution The Journal of biological chemistry High 24311790
2014 miR-17 upregulates DUSP16/MKP7 expression (by repressing ADCY5, causing RGS2 nuclear translocation that promotes MKP7 promoter activity); MKP7 inhibits cellular senescence by dephosphorylating PRAS40 at Thr246 and mTOR at Ser2248, facilitating their interaction and loss of function. miRNA transgenic mice, co-immunoprecipitation, western blot for phospho-PRAS40/mTOR, senescence assays, promoter-reporter assay Cell death & disease Medium 25077541
2015 DUSP16 ablation by shRNA causes G1/S transition arrest, cellular senescence (increased SA-β-gal, SAHF), and activates tumor suppressors p53 and Rb; the phosphatase catalytic activity of DUSP16 is required to antagonize cellular senescence. shRNA knockdown, cell cycle analysis (BrdU incorporation), SA-β-gal assay, phosphatase-dead mutant rescue The FEBS journal Medium 26381291
2017 Dusp16 knockout mice develop congenital obstructive hydrocephalus and brain overgrowth; Dusp16 deficiency causes delayed cell cycle exit of neural progenitors in the midbrain aqueduct, leading to progenitor overproliferation and subsequent neuron overproduction and aqueduct obstruction. Dusp16−/− mouse model, BrdU/EdU incorporation, immunohistochemistry for progenitor/neuron markers, histological analysis of aqueduct Frontiers in molecular neuroscience Medium 29170629
2018 HIF-1 (hypoxia-inducible factor 1) decreases DUSP16 expression in response to chemotherapy in triple-negative breast cancer cells; reduced DUSP16 leads to p38 activation, which stabilizes Nanog and Klf4 mRNA via inactivating phosphorylation of ZFP36L1, promoting breast cancer stem cell enrichment. HIF1 siRNA knockdown, western blot, flow cytometry for BCSC markers, p38 inhibitor treatment Cancer research Medium 29880481
2020 DUSP16 can directly interact with TAK1 in human hepatocytes; DUSP16 negatively regulates JNK, TAK1, and NF-κB signaling in response to palmitate; DUSP16 knockdown accelerates lipid deposition and inflammatory response, while DUSP16 overexpression has opposite effects; DUSP16 knockout in mice aggravates HFD-induced metabolic disorder. Co-immunoprecipitation (DUSP16–TAK1 interaction), siRNA knockdown, overexpression in primary hepatocytes, DUSP16-KO mouse model, western blot for phospho-JNK/TAK1/NF-κB Biochemical and biophysical research communications Medium 31982140
2021 DUSP16 overexpression inhibits JNK and p38 activation, reducing BAX accumulation in mitochondria and decreasing chemotherapy-induced apoptosis; DUSP16 knockdown sensitizes cancer cells to chemotherapy-induced cell death via the mitochondrial apoptosis pathway. DUSP16 overexpression/knockdown, western blot for phospho-JNK/p38/BAX, mitochondrial fractionation, cell death assays Nature communications High 33863904
2021 NR4A1 transcriptionally enhances MKP7/DUSP16 expression by physically associating with two putative binding sites on the MKP7 promoter; MKP7 knockdown increases phospho-JNK in pancreatic β cells upon ER stress or ROS; NR4A1-KO mice show reduced MKP7 in pancreatic islets. NR4A1 KO mouse islets, promoter reporter assay with NR4A1 binding site mutations, siRNA knockdown, western blot for phospho-JNK Cell death discovery Medium 34088892
2022 Tyrosine 271 (Y271) in the phosphatase domain of MKP7/DUSP16 is critical for catalytic activity and for binding to p38 MAPK and JNK1/2; Y271 mutants fail to dephosphorylate p38/JNK in cells and show reduced MAPK binding; WT MKP7 sequesters p38/JNK in the cytoplasm, but Y271 mutants fail to do so, resulting in greater nuclear accumulation of phospho-p38/JNK; this allosteric site is analogous to Y435 in MKP5. Site-directed mutagenesis, in-cell dephosphorylation assays, Co-IP for MAPK binding, immunofluorescence for MAPK localization The Journal of biological chemistry High 36272649
2025 FBXL18 physically interacts with DUSP16 and promotes its ubiquitination and proteasome-mediated degradation, thereby activating JNK/c-JUN signaling and promoting endometrial carcinoma cell proliferation, migration, and invasion; DUSP16 overexpression rescues FBXL18-mediated JNK activation. Co-immunoprecipitation, ubiquitination assay, western blot, loss/gain-of-function cell assays, rescue experiment Cancer cell international Medium 40382593

Source papers

Stage 0 corpus · 38 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Mycobacterium tuberculosis Eis protein initiates suppression of host immune responses by acetylation of DUSP16/MKP-7. Proceedings of the National Academy of Sciences of the United States of America 172 22547814
2001 A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs. The Journal of biological chemistry 136 11359773
2001 MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein. The Journal of biological chemistry 126 11489891
2009 Altered Runx1 subnuclear targeting enhances myeloid cell proliferation and blocks differentiation by activating a miR-24/MKP-7/MAPK network. Cancer research 100 19826043
2018 Reciprocal Regulation of DUSP9 and DUSP16 Expression by HIF1 Controls ERK and p38 MAP Kinase Activity and Mediates Chemotherapy-Induced Breast Cancer Stem Cell Enrichment. Cancer research 73 29880481
2009 SDF-1alpha stimulates JNK3 activity via eNOS-dependent nitrosylation of MKP7 to enhance endothelial migration. Proceedings of the National Academy of Sciences of the United States of America 68 19307591
2021 DUSP16 promotes cancer chemoresistance through regulation of mitochondria-mediated cell death. Nature communications 63 33863904
2005 Phosphorylation of Ser-446 determines stability of MKP-7. The Journal of biological chemistry 55 15689616
2011 Flagellin administration protects gut mucosal tissue from irradiation-induced apoptosis via MKP-7 activity. Gut 54 21199832
2014 miR-17 extends mouse lifespan by inhibiting senescence signaling mediated by MKP7. Cell death & disease 53 25077541
2005 Dynamic interaction between the dual specificity phosphatase MKP7 and the JNK3 scaffold protein beta-arrestin 2. The Journal of biological chemistry 51 15888437
2003 MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for chromosome region 12p12-13, reduces BCR-ABL-induced transformation. Oncogene 45 14586399
2013 PI3K/Akt-independent negative regulation of JNK signaling by MKP-7 after cerebral ischemia in rat hippocampus. BMC neuroscience 40 23280045
2020 Photobiomodulation suppresses JNK3 by activation of ERK/MKP7 to attenuate AMPA receptor endocytosis in Alzheimer's disease. Aging cell 34 33336891
2018 MicroRNA-27a-3p inhibits cell viability and migration through down-regulating DUSP16 in hepatocellular carcinoma. Journal of cellular biochemistry 33 29143999
2021 Exosomal transfer of miR-769-5p promotes osteosarcoma proliferation and metastasis by targeting DUSP16. Cancer cell international 28 34663350
2013 PPARδ inhibits UVB-induced secretion of MMP-1 through MKP-7-mediated suppression of JNK signaling. The Journal of investigative dermatology 28 23639976
2010 DUSP16 is an epigenetically regulated determinant of JNK signalling in Burkitt's lymphoma. British journal of cancer 28 20551953
2015 DUSP16 ablation arrests the cell cycle and induces cellular senescence. The FEBS journal 24 26381291
2013 Gene trap mice reveal an essential function of dual specificity phosphatase Dusp16/MKP-7 in perinatal survival and regulation of Toll-like receptor (TLR)-induced cytokine production. The Journal of biological chemistry 24 24311790
2011 Functional involvement of dual specificity phosphatase 16 (DUSP16), a c-Jun N-terminal kinase-specific phosphatase, in the regulation of T helper cell differentiation. The Journal of biological chemistry 23 21613215
2010 MKP-7, a JNK phosphatase, blocks ERK-dependent gene activation by anchoring phosphorylated ERK in the cytoplasm. Biochemical and biophysical research communications 18 20122898
2016 Upregulation of MKP-7 in response to rosiglitazone treatment ameliorates lipopolysaccharide-induced destabilization of SIRT1 by inactivating JNK. Pharmacological research 17 27771463
2022 circRNA_0001679/miR-338-3p/DUSP16 axis aggravates acute lung injury. Open medicine (Warsaw, Poland) 16 35291714
2021 NR4A1 enhances MKP7 expression to diminish JNK activation induced by ROS or ER-stress in pancreatic β cells for surviving. Cell death discovery 16 34088892
2020 Targeting DUSP16/TAK1 signaling alleviates hepatic dyslipidemia and inflammation in high fat diet (HFD)-challenged mice through suppressing JNK MAPK. Biochemical and biophysical research communications 15 31982140
2017 Dusp16 Deficiency Causes Congenital Obstructive Hydrocephalus and Brain Overgrowth by Expansion of the Neural Progenitor Pool. Frontiers in molecular neuroscience 15 29170629
2011 MKP-7, a negative regulator of JNK, regulates VCAM-1 expression through IRF-1. Cellular signalling 15 22182512
2023 Mettl3 induced miR-338-3p expression in dendritic cells promotes antigen-specific Th17 cell response via regulation of Dusp16. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 13 37878342
2021 CircRNA DUSP16 Knockdown Suppresses Colorectal Cancer Progression by Regulating the miR-432-5p/E2F6 Axis. Cancer management and research 13 34456589
2014 Discovery of novel DUSP16 phosphatase inhibitors through virtual screening with homology modeled protein structure. Journal of biomolecular screening 9 25245988
2022 A novel site on dual-specificity phosphatase MKP7/DUSP16 is required for catalysis and MAPK binding. The Journal of biological chemistry 8 36272649
2013 A docking study of enhanced intracellular survival protein from Mycobacterium tuberculosis with human DUSP16/MKP-7. Journal of synchrotron radiation 7 24121342
2024 Deficiency of smooth muscle cell ILF3 alleviates intimal hyperplasia via HMGB1 mRNA degradation-mediated regulation of the STAT3/DUSP16 axis. Journal of molecular and cellular cardiology 5 38583797
2024 Suppressing DUSP16 overexpression induced by ELK1 promotes neural progenitor cell differentiation in mouse models of Alzheimer's disease. Aging cell 3 39434411
2025 FBXL18 promotes endometrial carcinoma progression via destabilizing DUSP16 and thus activating JNK signaling pathway. Cancer cell international 0 40382593
2025 SBEM confers paclitaxel resistance in breast cancer via DUSP16-mediated MAPK/AMPK pathway activation. Oncology letters 0 41181635
2025 Regulatory roles of MKP7/DUSP16 in cancer. Medical oncology (Northwood, London, England) 0 41320681