Affinage

PTPRK

Receptor-type tyrosine-protein phosphatase kappa · UniProt Q15262

Length
1439 aa
Mass
162.1 kDa
Annotated
2026-06-10
30 papers in source corpus 19 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PTPRK is a receptor-type protein tyrosine phosphatase that couples homophilic cell-cell adhesion to the dephosphorylation of junctional and signaling substrates, thereby restraining epithelial proliferation and Wnt/beta-catenin signaling (PMID:8264577, PMID:30924770, PMID:31934854). Its extracellular domain mediates calcium-independent homophilic adhesion that does not require phosphatase activity or proteolytic cleavage (PMID:8264577), forming a head-to-tail homodimer whose interface depends critically on residue W351 (PMID:36436563); the precursor is additionally processed by furin within its fourth fibronectin type III repeat into two associated fragments (PMID:8474452). Stabilized at cell-cell contacts, PTPRK directly dephosphorylates the junctional substrates Afadin, PARD3, and delta-catenin family members, with substrate selectivity conferred by recruitment to the D2 pseudophosphatase domain through a phosphorylation-independent coiled-coil interaction, as shown for Afadin (PMID:30924770, PMID:36264065). PTPRK suppresses Wnt signaling by maintaining the '4Y' endocytic motif of ZNRF3 in a dephosphorylated state to drive Wnt receptor degradation, an activity antagonized by HGF-stimulated MET kinase in a kinase-phosphatase rheostat, and it lowers nuclear beta-catenin to repress cyclin D1 and c-myc (PMID:31934854, PMID:34590584, PMID:18276111). It further restrains contact-dependent growth and oncogenic signaling by dephosphorylating EGFR and suppressing EGFR/ERK, STAT3, CD133-AKT, and E2F pathways, with some growth- and EMT-related effects occurring independently of catalytic activity, indicating scaffold/adaptor functions alongside its enzymatic role (PMID:36551956, PMID:36611909, PMID:30947381, PMID:30838170, PMID:38904097). Beyond epithelial adhesion, PTPRK is required for CD4 single-positive thymocyte maturation (PMID:17909891) and promotes hepatic glycolysis and de novo lipogenesis via dephosphorylation of fructose-1,6-bisphosphatase 1 (PMID:39496584).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 1993 High

    Established that PTPRK is synthesized as a precursor processed by furin, defining the mature receptor architecture before any signaling role was known.

    Evidence Site-directed mutagenesis of a furin consensus site in the fourth FNIII repeat with antibody detection of cleavage products

    PMID:8474452

    Open questions at the time
    • Functional consequence of cleavage for adhesion or catalysis not resolved
    • Whether the two fragments separate under physiological conditions not addressed
  2. 1994 High

    Answered whether the extracellular domain is an adhesion molecule, showing PTPRK mediates calcium-independent homophilic adhesion independent of phosphatase activity or cleavage.

    Evidence Inducible heterologous expression, purified ECD adhesion substrate, and bead aggregation assays

    PMID:8264577

    Open questions at the time
    • Structural basis of the homophilic interface not defined
    • Link between adhesion and cytoplasmic phosphatase function unestablished
  3. 2007 Medium

    Connected PTPRK to tumor suppression and placed it downstream of TGF-beta signaling, providing the first regulatory context for its expression.

    Evidence Overexpression/siRNA in Hodgkin lymphoma lines, proliferation assays, and Smad2 protein-level analysis with EBV EBNA1

    PMID:17720884

    Open questions at the time
    • Direct phosphatase substrates mediating tumor suppression not identified
    • Single tumor-cell context
  4. 2007 High

    Demonstrated a non-redundant in vivo requirement for PTPRK in CD4 single-positive thymocyte maturation via genetic rescue.

    Evidence LEC rat Ptprk deletion with bone marrow reconstitution by retroviral Ptprk and flow cytometry

    PMID:17909891

    Open questions at the time
    • Molecular substrates in thymocytes not identified
    • Mechanism linking phosphatase activity to DP-to-SP transition unknown
  5. 2008 Medium

    Showed PTPRK negatively regulates beta-catenin transcriptional output, linking the receptor to Wnt-pathway target gene control.

    Evidence Gain/loss-of-function in HEK293 and melanoma cells, beta-catenin immunofluorescence, and cyclin D1/c-myc western blots

    PMID:18276111

    Open questions at the time
    • Direct substrate driving beta-catenin relocalization not defined
    • Catalytic vs scaffold contribution not separated
  6. 2010 Medium

    Refined the thymocyte phenotype by showing Themis co-contributes with Ptprk to the thid immunodeficiency.

    Evidence Lentiviral Themis transduction, bone marrow transplantation, and flow cytometry in LEC rats

    PMID:20203423

    Open questions at the time
    • Biochemical relationship between PTPRK and Themis not established
    • Whether the two act in the same pathway unresolved
  7. 2019 High

    Identified direct junctional substrates of PTPRK, defining its molecular role in maintaining cell-cell adhesion and restraining invasion.

    Evidence Proximity labeling, quantitative tyrosine phosphoproteomics, and dephosphorylation/interaction assays in epithelial cells

    PMID:30924770

    Open questions at the time
    • Recruitment mechanism for each substrate not fully mapped
    • In vivo relevance of substrate dephosphorylation not tested at this stage
  8. 2019 Medium

    Extended PTPRK substrate range to CD133 and STAT3, connecting loss of PTPRK to AKT survival and STAT3 oncogenic signaling.

    Evidence siRNA knockdown in colon and NSCLC cells with phospho-CD133, phospho-STAT3 Tyr705, AKT/Bad readouts and functional assays

    PMID:30838170 PMID:30947381

    Open questions at the time
    • Direct vs indirect dephosphorylation of STAT3 not established
    • Single-lab readouts per cancer type
  9. 2020 High

    Defined a direct mechanism for Wnt suppression: PTPRK keeps the ZNRF3 '4Y' motif dephosphorylated to promote Wnt receptor degradation, validated in vivo.

    Evidence Xenopus morpholino knockdown, ZNRF3 epistasis, dephosphorylation assays, and Wnt reporters with phenotypic analysis

    PMID:31934854

    Open questions at the time
    • How adhesion state gates ZNRF3 dephosphorylation unclear
    • Mammalian developmental requirement not addressed here
  10. 2021 High

    Established a kinase-phosphatase rheostat in which MET phosphorylates the same ZNRF3 motif PTPRK dephosphorylates, tuning Wnt receptor turnover.

    Evidence Reciprocal MET-ZNRF3 Co-IP, MET pharmacological inhibition, siRNA, phosphorylation assays, and Wnt reporters

    PMID:34590584

    Open questions at the time
    • Physiological contexts where the rheostat is engaged not defined
    • Quantitative balance of MET vs PTPRK in tissues unknown
  11. 2022 High

    Provided the structural basis of homophilic adhesion, identifying W351 as the dimerization-determining residue.

    Evidence X-ray crystallography of membrane-distal domains, SAXS of full-length ECD, and W351G dimerization assay

    PMID:36436563

    Open questions at the time
    • Whether dimerization regulates cytoplasmic phosphatase activity not tested
    • Adhesion-coupled conformational signaling not resolved
  12. 2022 High

    Resolved how substrate specificity is achieved, showing Afadin is recruited via the D2 pseudophosphatase domain through a distal coiled-coil interaction.

    Evidence Biochemical interaction mapping, pulldowns, and dephosphorylation assays with domain mutants comparing PTPRK and PTPRM

    PMID:36264065

    Open questions at the time
    • Whether other substrates use the same D2 docking mode not shown
    • Structural detail of the docking interface not determined
  13. 2022 Medium

    Linked PTPRK to contact-dependent growth arrest through suppression of E2F activity and CDK inhibitor induction.

    Evidence Knockdown/overexpression, E2F luciferase reporters, cell cycle analysis, CDK2 activity assays, and domain deletions

    PMID:36551956

    Open questions at the time
    • Direct substrate upstream of E2F not identified
    • Connection to junctional substrate dephosphorylation unclear
  14. 2022 Medium

    Identified EGFR as a PTPRK target in intestinal epithelium, coupling the phosphatase to ERK-driven proliferation control.

    Evidence siRNA and overexpression in control and celiac-disease organoids with pEGFR/pERK westerns and BrdU proliferation

    PMID:36611909

    Open questions at the time
    • Whether EGFR is a direct substrate not biochemically proven here
    • Disease relevance beyond organoids not established
  15. 2024 High

    Revealed catalytic-independent scaffold functions, showing PTPRK regulates EGFR and EMT and supports collective migration without phosphatase activity.

    Evidence Catalytically inactive mutants, invasion/migration assays, EMT markers, and a colitis mouse model

    PMID:38904097

    Open questions at the time
    • Scaffold-binding partners mediating these effects not identified
    • How catalytic and non-catalytic roles are partitioned unclear
  16. 2024 High

    Expanded PTPRK function into hepatic metabolism, identifying FBP1 as a substrate driving glycolysis and de novo lipogenesis.

    Evidence PTPRK knockout mice on high-fat diet, hepatocyte phosphoproteomics, and hepatic metabolomics

    PMID:39496584

    Open questions at the time
    • Direct dephosphorylation of FBP1 site not fully mechanistically dissected
    • Tissue specificity of metabolic role not addressed
  17. 2026 Medium

    Connected disease-associated D1-domain mutations to retained ITGB4 binding but lost catalysis, defining a separation-of-function consequence in CRC.

    Evidence PTPRK-ITGB4 Co-IP, ITGB4 phosphorylation westerns, and xenograft tumor growth with mutant constructs

    PMID:41820225

    Open questions at the time
    • Whether ITGB4 is a direct catalytic substrate not definitively established
    • Single-lab in vivo model
  18. 2025 Low

    Proposed a pro-inflammatory neuronal role via DUSP1/p38 MAPK in postherpetic neuralgia, extending PTPRK beyond epithelial contexts.

    Evidence RTX-induced rat PHN model and PTPRK overexpression in DRG cells with pathway and cytokine readouts

    PMID:41253902

    Open questions at the time
    • Mechanistic link to DUSP1/p38 based on overexpression and correlation without direct dephosphorylation assay
    • No loss-of-function validation
    • Relevance to human neuralgia unestablished

Open questions

Synthesis pass · forward-looking unresolved questions
  • How adhesion state and ECD dimerization are transduced to regulate cytoplasmic phosphatase versus scaffold activity, and which partners mediate catalytic-independent functions, remain unresolved.
  • No structural or biochemical coupling between ECD dimerization and catalytic regulation
  • Scaffold/adaptor partners not identified
  • Substrate docking generality beyond Afadin unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 5 GO:0016787 hydrolase activity 3 GO:0060089 molecular transducer activity 2 GO:0060090 molecular adaptor activity 2 GO:0098631 cell adhesion mediator activity 2
Localization
GO:0005886 plasma membrane 3 GO:0005829 cytosol 2
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-1500931 Cell-Cell communication 3 R-HSA-1430728 Metabolism 1 R-HSA-1640170 Cell Cycle 1 R-HSA-168256 Immune System 1
Partners
CD133EGFRITGB4METMFAP/AFADINPARD3ZNRF3

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1994 R-PTP-kappa (PTPRK) mediates homophilic intercellular adhesion through its extracellular domain in a calcium-independent manner that does not require PTPase activity or proteolytic cleavage. Purified extracellular domain functions as an adhesion substrate and induces aggregation of coated beads. Inducible heterologous expression, purified extracellular domain adhesion assays, bead aggregation assay Molecular and cellular biology High 8264577
1993 PTPRK precursor protein undergoes proteolytic cleavage at a furin consensus sequence located in the fourth fibronectin type III-like repeat, generating two cleavage products that remain associated. Site-directed mutagenesis confirmed the furin cleavage site. Site-directed mutagenesis, antibody detection of cleavage products Molecular and cellular biology High 8474452
2007 PTPRK functions as a tumor suppressor in Hodgkin lymphoma cells; overexpression decreases viability and proliferation while knockdown increases them. PTPRK is a TGF-beta target gene whose expression is reduced by EBV-encoded EBNA1 through degradation of Smad2 protein, thereby disrupting TGF-beta signaling upstream of PTPRK. Overexpression and siRNA knockdown in HL cell lines, cell viability/proliferation assays, western blot for Smad2 protein levels Blood Medium 17720884
2008 PTPRK negatively regulates beta-catenin transcriptional activity by reducing nuclear accumulation of both wild-type and oncogenic beta-catenin, limiting cytosolic tyrosine-phosphorylated beta-catenin, and promoting re-localization of E-cadherin/beta-catenin complexes to the membrane. This results in inhibition of cyclin D1 and c-myc expression. PTPRK expression in HEK293 and melanoma cells, siRNA knockdown, immunofluorescence for beta-catenin localization, western blot for cyclin D1 and c-myc Cellular signalling Medium 18276111
2007 A deletion of the Ptprk gene in the LEC rat causes a defect in CD4 single-positive thymocyte maturation. Reconstitution with bone marrow cells transduced with Ptprk (but not with RGD1560849) rescued CD4 SP cell development, establishing that PTPRK is required for CD4 T cell maturation in the thymus. Genetic linkage analysis, bone marrow reconstitution with retroviral Ptprk expression, flow cytometry for T cell subsets Mammalian genome High 17909891
2010 Both Ptprk and Themis gene deletion contribute to the T-helper immunodeficiency (thid) phenotype in LEC rats; exogenous Themis expression also rescued CD4 SP T cell development, indicating both genes are required for DP-to-SP thymocyte maturation. Lentiviral Themis transduction, bone marrow transplantation, flow cytometry Biomedical research (Tokyo, Japan) Medium 20203423
2019 PTPRK is stabilized at cell-cell contacts in epithelial cells and directly dephosphorylates at least five substrates: Afadin, PARD3, and delta-catenin family members. Loss of PTPRK phosphatase activity disrupts cell junctions and increases invasive characteristics. Proximity labeling, quantitative tyrosine phosphoproteomics, dephosphorylation assays, interaction studies, loss-of-function cell assays eLife High 30924770
2019 PTPRK dephosphorylates CD133, and loss of PTPRK potentiates the CD133-AKT signaling pathway. Knockdown of PTPRK reduces sensitivity to oxaliplatin and is accompanied by upregulation of phosphorylated Bad (a downstream AKT target). siRNA knockdown of PTPRK in colon cancer cells, western blot for CD133 phosphorylation and AKT/Bad pathway, oxaliplatin sensitivity assay FEBS open bio Medium 30947381
2019 Downregulation of PTPRK in NSCLC cells leads to increased STAT3 phosphorylation at Tyr705, enhanced proliferation, invasion, and migration, suggesting PTPRK suppresses NSCLC progression at least in part by negatively regulating STAT3 activation. PTPRK siRNA knockdown in NSCLC cell lines, western blot for phospho-STAT3 Tyr705, migration/invasion/proliferation assays Analytical cellular pathology (Amsterdam) Medium 30838170
2020 PTPRK promotes Wnt inhibition by maintaining the '4Y' endocytic tyrosine motif in ZNRF3 in a dephosphorylated state, thereby promoting ZNRF3 internalization and Wnt receptor degradation. Loss of Ptprk in Xenopus embryos increases Wnt signaling, reduces organizer gene expression, and causes head/axial defects. In vivo Xenopus morpholino knockdown, epistasis with ZNRF3, dephosphorylation assays, Wnt signaling reporters, phenotypic analysis eLife High 31934854
2021 MET kinase phosphorylates the '4Y' endocytic motif in ZNRF3 (stimulated by HGF), antagonizing PTPRK-mediated dephosphorylation. HGF-MET signaling reduces ZNRF3-dependent Wnt receptor degradation, while inhibition of MET promotes ZNRF3 internalization, establishing a MET-PTPRK kinase-phosphatase rheostat controlling Wnt signaling. Co-IP for MET-ZNRF3 binding, pharmacological MET inhibition, siRNA knockdown, phosphorylation assays, Wnt signaling reporters eLife High 34590584
2022 The X-ray crystal structure of the N-terminal membrane-distal domains of PTPRK reveals a head-to-tail homodimer consistent with intermembrane adhesion. Residue W351 in the interaction interface is critical for PTPRK dimer formation; mutation to glycine (the equivalent PTPRM residue) abolishes dimer formation in vitro. Small-angle X-ray scattering showed the full-length ECD is a rigid extended molecule. X-ray crystallography, SAXS, in vitro dimerization assay with W351G mutation The Journal of biological chemistry High 36436563
2022 Afadin is recruited for dephosphorylation by directly binding to the PTPRK D2 pseudophosphatase domain via a coiled-coil domain more than 100 amino acids from the substrate pTyr residue. This interaction is phosphorylation-independent and determines substrate specificity — Afadin is selectively dephosphorylated by PTPRK but not by PTPRM. Biochemical interaction mapping, pulldown assays, dephosphorylation assays with domain mutants eLife High 36264065
2022 R-PTP-kappa suppresses contact-dependent cell growth by suppressing E2F transcriptional activity through the cytoplasmic PTP domain, which induces p21Cip1/WAF-1 and p27Kip1, reduces CDK2 activity, and causes G1 cell cycle arrest. siRNA knockdown and overexpression, luciferase reporter assays for E2F activity, cell cycle analysis, CDK2 activity assay, domain deletion constructs Biomedicines Medium 36551956
2022 PTPRK functions as a phosphatase for EGFR in intestinal epithelial cells; silencing PTPRK in control organoids increases pEGFR and pERK and proliferation, while overexpression in celiac disease organoids reduces pEGFR, pERK and proliferation. siRNA silencing and overexpression in intestinal organoids, western blot for pEGFR and pERK, BrdU incorporation proliferation assay Cells Medium 36611909
2024 PTPRK suppresses invasion and promotes collective directed migration in colorectal cancer cells, and supports recovery from colitis in vivo. Contrary to prevailing notion, PTPRK regulation of EGFR and epithelial-to-mesenchymal transition (EMT) is independent of its catalytic phosphatase activity, indicating PTPRK has scaffold/adaptor functions in addition to catalytic activity. Catalytically inactive PTPRK mutants, invasion assays, migration assays, colitis mouse model, EGFR signaling readouts, EMT markers Journal of cell science High 38904097
2024 In obese mice, PTPRK promotes hepatic glycolysis and de novo lipogenesis. Phosphoproteomic analysis identified fructose-1,6-bisphosphatase 1 as a PTPRK target. Mechanistically, PTPRK-induced glycolysis enhances PPARgamma and lipogenesis. PTPRK knockout mice have lower weight gain and reduced hepatic fat accumulation. PTPRK knockout mice on high-fat diet, phosphoproteomics in primary hepatocytes, hepatic metabolomics, colony-forming assay, carcinogen model Nature communications High 39496584
2026 PTPRK mutant proteins with mutations in the D1 domain retain binding to integrin beta-4 (ITGB4) but show impaired phosphatase activity, resulting in increased ITGB4 phosphorylation in CRC cells expressing the mutants and increased tumor proliferation in vivo. Co-IP for PTPRK-ITGB4 binding, western blot for ITGB4 phosphorylation, xenograft tumor growth assay Journal of biochemistry Medium 41820225
2025 PTPRK promotes postherpetic neuralgia in rats by activating the DUSP1/p38 MAPK signaling pathway in dorsal root ganglia. PTPRK overexpression promotes inflammation via this pathway in DRG cells. RTX-induced rat PHN model, PTPRK overexpression in DRG cells, western blot for DUSP1/p38 MAPK pathway components, ELISA for inflammatory cytokines Scientific reports Low 41253902

Source papers

Stage 0 corpus · 30 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2015 Targeting PTPRK-RSPO3 colon tumours promotes differentiation and loss of stem-cell function. Nature 204 26700806
1994 Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding. Molecular and cellular biology 204 8264577
1993 Cloning and characterization of R-PTP-kappa, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular region. Molecular and cellular biology 141 8474452
2016 Frequent PTPRK-RSPO3 fusions and RNF43 mutations in colorectal traditional serrated adenoma. The Journal of pathology 107 26924569
2007 Down-regulation of the TGF-beta target gene, PTPRK, by the Epstein-Barr virus encoded EBNA1 contributes to the growth and survival of Hodgkin lymphoma cells. Blood 88 17720884
2008 PTPRK negatively regulates transcriptional activity of wild type and mutated oncogenic beta-catenin and affects membrane distribution of beta-catenin/E-cadherin complexes in cancer cells. Cellular signalling 40 18276111
2019 The homophilic receptor PTPRK selectively dephosphorylates multiple junctional regulators to promote cell-cell adhesion. eLife 35 30924770
2020 The tumor suppressor PTPRK promotes ZNRF3 internalization and is required for Wnt inhibition in the Spemann organizer. eLife 33 31934854
2018 MiR-1260b promotes the migration and invasion in non-small cell lung cancer via targeting PTPRK. Pathology, research and practice 30 29628123
1997 Molecular cloning and chromosomal localization of a human gene homologous to the murine R-PTP-kappa, a receptor-type protein tyrosine phosphatase. Gene 25 9047348
2007 A deletion mutation of the protein tyrosine phosphatase kappa (Ptprk) gene is responsible for T-helper immunodeficiency (thid) in the LEC rat. Mammalian genome : official journal of the International Mammalian Genome Society 24 17909891
2024 PTPRK regulates glycolysis and de novo lipogenesis to promote hepatocyte metabolic reprogramming in obesity. Nature communications 18 39496584
2019 PTPRK Expression Is Downregulated in Drug Resistant Ovarian Cancer Cell Lines, and Especially in ALDH1A1 Positive CSCs-Like Populations. International journal of molecular sciences 16 31027318
2018 miRNA-627 inhibits cell proliferation and cell migration, promotes cell apoptosis in prostate cancer cells through upregulating MAP3K1, PTPRK and SRA1. International journal of clinical and experimental pathology 15 31938108
2010 Contiguous gene deletion of Ptprk and Themis causes T-helper immunodeficiency (thid) in the LEC rat. Biomedical research (Tokyo, Japan) 15 20203423
2019 PTPRK suppresses progression and chemo-resistance of colon cancer cells via direct inhibition of pro-oncogenic CD133. FEBS open bio 12 30947381
2023 Multi-ancestry genome-wide meta-analysis of 56,241 individuals identifies LRRC4C, LHX5-AS1 and nominates ancestry-specific loci PTPRK , GRB14 , and KIAA0825 as novel risk loci for Alzheimer's disease: the Alzheimer's Disease Genetics Consortium. medRxiv : the preprint server for health sciences 11 37461624
2021 A MET-PTPRK kinase-phosphatase rheostat controls ZNRF3 and Wnt signaling. eLife 10 34590584
2019 Downregulation of PTPRK Promotes Cell Proliferation and Metastasis of NSCLC by Enhancing STAT3 Activation. Analytical cellular pathology (Amsterdam) 10 30838170
2022 PTPRK, an EGFR Phosphatase, Is Decreased in CeD Biopsies and Intestinal Organoids. Cells 9 36611909
2017 Analysis of PTPRK polymorphisms in association with risk and age at onset of Alzheimer's disease, cancer risk, and cholesterol. Journal of psychiatric research 6 28987514
2021 The Impact of PTPRK and ROS1 Polymorphisms on the Preeclampsia Risk in Han Chinese Women. International journal of hypertension 5 34646579
2025 Protein tyrosine phosphatase receptor type kappa (PTPRK) revisited: evolving insights into structure, function, and pathology. Journal of translational medicine 4 40355891
2024 The receptor protein tyrosine phosphatase PTPRK promotes intestinal repair and catalysis-independent tumour suppression. Journal of cell science 3 38904097
2022 Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains. The Journal of biological chemistry 3 36436563
2022 Investigation of cell signalings and therapeutic targets in PTPRK-RSPO3 fusion-positive colorectal cancer. PloS one 2 36129915
2022 R-PTP-κ Inhibits Contact-Dependent Cell Growth by Suppressing E2F Activity. Biomedicines 2 36551956
2025 PTPRK promotes resiniferatoxin-induced postherpetic neuralgia via activating DUSP1/p38 MAPK signaling pathway in dorsal root ganglia. Scientific reports 1 41253902
2022 Molecular mechanism of Afadin substrate recruitment to the receptor phosphatase PTPRK via its pseudophosphatase domain. eLife 1 36264065
2026 Recurrent Mutations in Protein Tyrosine Phosphatase Receptor Type Kappa (PTPRK) in Depressed-Type Colorectal Carcinomas. Journal of biochemistry 0 41820225

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