Affinage

STK17B

Serine/threonine-protein kinase 17B · UniProt O94768

Length
372 aa
Mass
42.3 kDa
Annotated
2026-06-10
47 papers in source corpus 21 papers cited in narrative 21 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

STK17B (DRAK2) is a calcium-responsive serine/threonine kinase best characterized as a negative regulator that raises the threshold for lymphocyte activation and as a stress-responsive kinase controlling cell survival and metabolism across multiple tissues (PMID:15589167, PMID:21148796). In T cells its activation is driven by TCR ligation through Orai1/CRAC-dependent Ca2+ influx, a PKD-mediated phosphorylation step, and mitochondrial ROS, and it autophosphorylates at Ser12 in a calcium-dependent manner required for optimal suppression of T cell activation (PMID:17182616, PMID:21148796). Rather than dampening proximal TCR signaling, STK17B limits IL-2 sensitivity by inhibiting STAT5A phosphorylation, thereby restraining regulatory T cell development (PMID:36773294); loss of the kinase sensitizes activated T cells to intrinsic mitochondrial apoptosis that is rescued by Bcl-xL (PMID:19017949). STK17B also phosphorylates myosin light chain 2 to support actin polymerization, TCR microcluster formation, and myosin-dependent T cell migration and conjugation (PMID:39421891, PMID:39502695). Its subcellular distribution is governed by a functional NLS whose adjacent Ser350 is phosphorylated by PKC-gamma to drive cytoplasmic accumulation, while nuclear localization is required for UV-induced apoptosis (PMID:16462023, PMID:18084041). Beyond immunity, STK17B acts through defined substrates: it phosphorylates ULK1 at Ser56 to trigger its ubiquitylation and suppress autophagy in pancreatic beta cells (PMID:38324636), binds the splicing factor SRSF6 and blocks its phosphorylation by SRPK1 to reprogram mitochondrial-gene splicing during NASH progression (PMID:34614409), and phosphorylates IREB2 (Ser157) and HSPB1 (Ser15) to suppress ferroptosis in multiple myeloma (PMID:40953235). Kinase activity is inhibited in a calcium-dependent manner by the calcium-binding protein CHP, and expression is transcriptionally repressed by MYB (PMID:12966074, PMID:23398943). A crystal structure with the selective inhibitor SGC-STK17B-1 defined a distinctive P-loop conformation involving an R41 salt bridge that confers selectivity over STK17A (PMID:33215924).

Mechanistic history

Synthesis pass · year-by-year structured walk · 20 steps
  1. 2003 Medium

    Established the first negative regulator of STK17B catalytic output, linking its kinase activity to calcium signaling at the biochemical level.

    Evidence In vitro kinase assay with CHP and MLC substrate, plus interaction studies

    PMID:12966074

    Open questions at the time
    • Single in vitro study with exogenous substrate
    • Cellular relevance of CHP inhibition not tested in primary cells
  2. 2004 High

    Defined the core physiological role by showing STK17B sets the activation threshold of T cells, distinguishing it from an apoptotic or selection function.

    Evidence Drak2-/- knockout mouse with T cell functional assays

    PMID:15589167

    Open questions at the time
    • Molecular target downstream of the kinase not identified
    • Mechanism of threshold-raising left open
  3. 2005 Medium

    Connected STK17B to calcium-tuned thymocyte selection and showed its expression is induced by TCR signaling via PKC and MAP kinase.

    Evidence Drak2-/- thymocyte assays and retroviral transduction with TCR stimulation

    PMID:16172133

    Open questions at the time
    • Direct transcriptional inducers not mapped
    • Substrate mediating threshold control unknown
  4. 2006 Medium

    Identified Ser12 autophosphorylation as a calcium-dependent activation mark required for suppressive function, providing a molecular readout of activity.

    Evidence Mass spectrometry, phospho-specific antibody, and calcium perturbation in T and B cells

    PMID:17182616

    Open questions at the time
    • Upstream kinase/sensor coupling calcium to Ser12 not defined at this stage
  5. 2006 Medium

    Showed overexpression promotes apoptosis of activated T cells in the presence of IL-2, linking kinase dosage to survival and memory T cell numbers.

    Evidence Transgenic Drak2-overexpressing mice with IL-2 apoptosis assays

    PMID:16517594

    Open questions at the time
    • Direct apoptotic substrate not identified
    • Overexpression may not reflect endogenous stoichiometry
  6. 2006 Medium

    Demonstrated nuclear localization is required for apoptotic function, establishing subcellular compartmentalization as a control point.

    Evidence GFP-fusion localization, NLS mutagenesis, siRNA, UV apoptosis assay

    PMID:16462023

    Open questions at the time
    • Nuclear substrates driving apoptosis not identified
    • Single lab
  7. 2007 Medium

    Identified PKC-gamma phosphorylation of Ser350 flanking the NLS as the switch controlling nucleocytoplasmic shuttling.

    Evidence GFP-fusion mutagenesis, PKC-gamma expression, PMA stimulation, S350D mutant

    PMID:18084041

    Open questions at the time
    • Physiological stimuli triggering PKC-gamma-dependent relocation in vivo not established
  8. 2008 High

    Resolved the survival phenotype by showing Drak2-/- T cells are hypersensitive to intrinsic mitochondrial apoptosis, rescuable by Bcl-xL.

    Evidence Drak2-/- mice, Bcl-xL transgenic rescue, adoptive transfer, EAE model

    PMID:19017949

    Open questions at the time
    • Direct kinase link to mitochondrial apoptotic machinery not defined
  9. 2009 Medium

    Proposed p70S6 kinase as a direct substrate in beta cell apoptosis, situating STK17B within an iNOS-caspase-9 axis.

    Evidence In vitro kinase assay, siRNA, overexpression, epistasis

    PMID:19342653

    Open questions at the time
    • Phosphosite on p70S6K not mapped
    • Single lab; not validated in vivo
  10. 2009 Medium

    Placed STK17B in a TGF-beta negative-feedback loop through interaction with TbRI that blocks R-Smad recruitment.

    Evidence Co-IP with TbRI, siRNA, TGF-beta reporter assays in tumor cells

    PMID:23122956

    Open questions at the time
    • Later contradicted in primary T cells (#12)
    • Direct phosphorylation of receptor not shown
  11. 2010 High

    Defined the activation module by showing PKD, Orai1-dependent Ca2+ influx, and mitochondrial ROS are required and sufficient for STK17B activation downstream of TCR.

    Evidence PKD inhibitor, kinase-dead/constitutively active mutants, knockdown, Co-IP, calcium influx assays

    PMID:21148796

    Open questions at the time
    • PKD phosphosite on STK17B not pinpointed
    • Connection to Ser12 autophosphorylation not directly bridged
  12. 2013 Medium

    Identified MYB as a direct transcriptional repressor of STK17B, linking its expression to apoptotic control in leukemia cells.

    Evidence siRNA of MYB and DRAK2, ChIP at the promoter, caspase-9 assay

    PMID:23398943

    Open questions at the time
    • Whether this regulation operates in normal lymphocytes unknown
  13. 2015 Medium

    Corrected the TGF-beta model by showing STK17B does not regulate TGF-beta/Smad signaling in primary T cells, narrowing the receptor-interaction finding to specific contexts.

    Evidence TGF-beta signaling and Smad phosphorylation assays in WT vs Drak2-/- primary T cells

    PMID:25951457

    Open questions at the time
    • Reconciliation with the tumor-cell TbRI finding (#9) not resolved mechanistically
  14. 2020 High

    Delivered a structural basis for selective inhibition, defining a unique P-loop conformation distinguishing STK17B from STK17A.

    Evidence X-ray crystallography with SGC-STK17B-1, selectivity profiling, MD simulation

    PMID:33215924

    Open questions at the time
    • No substrate-bound or active-state structure
    • Apo conformational dynamics not fully resolved
  15. 2021 High

    Identified SRSF6 as a direct binding partner whose SRPK1-mediated phosphorylation STK17B blocks, linking the kinase to mitochondrial-gene splicing and NASH.

    Evidence Co-IP/pulldown, phosphoproteomics, transcriptomics, conditional liver KO

    PMID:34614409

    Open questions at the time
    • Whether STK17B phosphorylates SRSF6 directly versus only sequestering it not fully resolved
  16. 2021 Medium

    Extended the PKC-effector role to neurons, showing STK17B mediates PKC-driven Purkinje cell dendritic remodeling.

    Evidence Overexpression, pharmacological inhibition, phospho-mimetic mutant in primary Purkinje cultures

    PMID:34536317

    Open questions at the time
    • Neuronal substrates not identified
    • In vivo dendritic phenotype not shown
  17. 2023 Medium

    Reframed the immune mechanism: STK17B limits IL-2 sensitivity by inhibiting STAT5A rather than dampening TCR signaling, controlling Treg development and autoimmunity.

    Evidence Drak2-/- NOD mice, STAT5A phosphorylation assays, Treg-depletion adoptive transfer

    PMID:36773294

    Open questions at the time
    • Direct phosphorylation target linking STK17B to STAT5A inhibition not defined
  18. 2024 High

    Established a direct ULK1 Ser56 phosphorylation-ubiquitylation axis through which STK17B suppresses autophagy and impairs beta cell mitochondrial function.

    Evidence Islet phosphoproteomics, in vitro kinase assay, ULK1-S56A rescue, conditional beta cell KO

    PMID:38324636

    Open questions at the time
    • E3 ligase coupling Ser56 phosphorylation to ULK1 ubiquitylation not identified
  19. 2024 Medium

    Identified MLC2 as a cytoskeletal substrate, explaining STK17B control of actomyosin dynamics, T cell migration, and immune synapse formation.

    Evidence Drak2-/- T cell functional assays, actin and MLC2 phosphorylation analysis, conjugation and microcluster imaging; phosphosite mapped by companion phosphoproteomics

    PMID:39421891 PMID:39502695

    Open questions at the time
    • Direct in vitro phosphorylation of MLC2 by purified STK17B not shown in these reports
  20. 2026 Medium

    Identified IREB2 (Ser157) and HSPB1 (Ser15) as direct substrates through which STK17B suppresses ferroptosis in multiple myeloma, linking it to iron handling and STAT3.

    Evidence Proximity labeling plus phosphoproteomics, site-specific validation, ferroptosis assays, xenografts, selective inhibitor

    PMID:40953235

    Open questions at the time
    • Mechanism by which STK17B maintains STAT3 phosphorylation indirect/unmapped
    • Single lab

Open questions

Synthesis pass · forward-looking unresolved questions
  • How STK17B selects among its diverse substrates (STAT5A pathway, ULK1, SRSF6, MLC2, IREB2/HSPB1) in different tissues, and how upstream calcium/PKD/PKC-gamma inputs are integrated to direct context-specific outputs, remains unresolved.
  • No unifying determinant of substrate choice identified
  • Cross-tissue regulatory logic uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 6 GO:0016740 transferase activity 5 GO:0140110 transcription regulator activity 1
Localization
GO:0005634 nucleus 2 GO:0005829 cytosol 1
Pathway
R-HSA-168256 Immune System 5 R-HSA-5357801 Programmed Cell Death 3 R-HSA-162582 Signal Transduction 2 R-HSA-8953854 Metabolism of RNA 1 R-HSA-9612973 Autophagy 1
Partners
CHPMYBPKDSRSF6TGFBR1ULK1

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 DRAK2 raises the threshold for T cell activation by negatively regulating signals through the TCR. Drak2-/- T cells showed enhanced sensitivity to TCR-mediated stimulation with a reduced requirement for costimulation, but no defects in apoptosis or negative selection. Genetic knockout mouse model (Drak2-/- mice), functional T cell assays Immunity High 15589167
2003 The calcium-binding protein CHP (calcineurin homologous protein) inhibits DRAK2 kinase activity (approximately 85% inhibition of both autophosphorylation and phosphorylation of myosin light chain substrate) in a calcium-dependent manner, while the CHP-DRAK2 physical interaction itself is not calcium-dependent. In vitro kinase assay, protein interaction studies Journal of biochemistry Medium 12966074
2006 Nuclear localization of DRAK2 is required for UV-induced apoptosis. DRAK2 accumulates in the nucleus following UV irradiation, and nuclear-targeted DRAK2 (NLS fusion) causes cell death, while cytoplasmic DRAK2 does not. siRNA knockdown of DRAK2 partially suppressed UV-induced apoptosis. GFP-fusion localization, NLS mutagenesis, siRNA knockdown, UV irradiation apoptosis assay Biological & pharmaceutical bulletin Medium 16462023
2007 DRAK2 contains a functional nuclear localization signal (NLS); phosphorylation of Ser350 (flanking the NLS) by PKC-gamma drives cytoplasmic localization. PMA induced cytoplasmic accumulation via PKC-gamma-mediated Ser350 phosphorylation, and the Ser350Asp mutant failed to accumulate in the nucleus upon UV irradiation. GFP-fusion NLS mutagenesis, ectopic PKC-gamma expression, PMA stimulation, site-directed mutagenesis (S350D) Journal of biochemistry Medium 18084041
2006 DRAK2 autophosphorylates at Ser12, and this autophosphorylation is induced by antigen receptor stimulation in T and B cells in a calcium-dependent manner (blocked by BAPTA-AM, promoted by thapsigargin). Ser12 phosphorylation is necessary for optimal suppression of T cell activation. Mass spectrometry identification of autophosphorylation site, phospho-specific antibody, calcium chelation/mobilization experiments The Journal of biological chemistry Medium 17182616
2005 DRAK2 controls the threshold for calcium signaling during thymocyte selection; Drak2-deficient positively selected thymocytes displayed a reduced requirement for TCR cross-linking. DRAK2 expression in DP thymocytes is induced by TCR stimulation in a PKC- and MAP kinase-dependent manner. Drak2-/- mouse thymocyte functional assays, retroviral transduction, TCR stimulation assays International immunology Medium 16172133
2006 Transgenic Drak2 overexpression leads to enhanced apoptosis of activated T cells in the presence of IL-2, with lower increases in anti-apoptotic factors (Bcl-2, Bcl-xL) during activation, resulting in reduced memory T cell numbers. Transgenic mouse model (human beta-actin promoter-driven Drak2), IL-2 apoptosis assays, immunophenotyping The Journal of biological chemistry Medium 16517594
2008 In Drak2-/- mice, T cells require greater tonic signaling for maintenance during clonal expansion and are more sensitive to intrinsic (mitochondrial) apoptosis following stimulation, which is prevented by CD28 ligation, homeostatic cytokines, or enforced Bcl-xL expression. T cell-specific Bcl-xL expression restored susceptibility to EAE in Drak2-/- mice. Drak2-/- mice, Bcl-xL transgenic rescue, adoptive transfer, apoptosis assays Journal of immunology High 19017949
2009 DRAK2 is upstream of p70S6 kinase (S6K) in beta cell apoptosis signaling; inducible NO synthase is upstream of DRAK2 and caspase-9 is downstream. Purified DRAK2 directly phosphorylates p70S6 kinase in an in vitro kinase assay. DRAK2 overexpression enhanced p70S6K phosphorylation in cells, and DRAK2 knockdown reduced it. In vitro kinase assay with purified proteins, siRNA knockdown, transgenic overexpression, epistasis analysis Journal of immunology Medium 19342653
2009 DRAK2 participates in a negative feedback loop controlling TGF-β signaling: TGF-β1 stimulation induces DRAK2 expression and promotes endogenous interaction of DRAK2 with the type I TGF-β receptor (TβRI), thereby blocking R-Smads recruitment. DRAK2 depletion markedly augmented TGF-β1 responses. Co-immunoprecipitation of DRAK2 with TβRI, siRNA knockdown, TGF-β signaling reporter assays, tumor cell line functional studies Cell reports Medium 23122956
2010 Protein kinase D (PKD) is an essential upstream activator of DRAK2 following TCR ligation, requiring Ca2+ influx through Orai1 (CRAC channels). PKD physically interacts with DRAK2, phosphorylates it, and a constitutively active PKD mutant promoted DRAK2 function while kinase-dead PKD or PKD knockdown blocked DRAK2 activation. Mitochondrial reactive oxygen species generation was necessary and sufficient for DRAK2 activation in response to Ca2+ influx. PKD inhibitor (Gö6976), kinase-dead and constitutively active PKD mutants, PKD knockdown, Co-IP of DRAK2-PKD interaction, Orai1-dependent calcium influx assays Journal of immunology High 21148796
2013 The MYB oncogene transcriptionally represses DRAK2 expression by binding to a conserved element upstream of the DRAK2 transcription start site. MYB knockdown upregulates DRAK2, activates caspase-9, and promotes apoptosis; DRAK2 siRNA knockdown rescues cells from this apoptosis. siRNA knockdown of MYB and DRAK2, ChIP assay showing MYB binding to DRAK2 promoter, caspase-9 activity assay Leukemia research Medium 23398943
2015 DRAK2 does NOT regulate TGF-β/Smad signaling in primary T cells. Smad2/Smad3 activation, TGF-β-mediated effects on naïve T cell proliferation, CD8+ T cell survival, Treg induction, and enhanced T cell death in Drak2-/- mice were all independent of TGF-β signaling. In vitro TGF-β signaling assays in wildtype vs Drak2-/- primary T cells, Smad phosphorylation assays, proliferation and survival assays PloS one Medium 25951457
2020 X-ray crystallography of STK17B with inhibitor SGC-STK17B-1 (thieno[3,2-d]pyrimidine) revealed a unique P-loop conformation characterized by a salt bridge between R41 and the carboxylic acid of the inhibitor, explaining selectivity over closely related STK17A. The compound is an ATP-competitive inhibitor. X-ray crystallography, kinase selectivity profiling, molecular dynamics simulation Journal of medicinal chemistry High 33215924
2021 DRAK2 directly binds the splicing factor SRSF6 and inhibits its phosphorylation by SRPK1, thereby regulating alternative splicing of mitochondrial function-related genes and driving NAFLD/NASH progression. Hepatic deletion of DRAK2 suppressed hepatic steatosis progression to NASH. Phosphoproteome and transcriptome analyses, Co-IP/pulldown identifying SRSF6 as direct DRAK2 binding partner, DRAK2 conditional liver knockout mice, RNA splicing analysis Cell metabolism High 34614409
2021 STK17B is strongly expressed in cerebellar Purkinje cells and functions as a downstream effector of PKC. STK17B overexpression potentiates PKC-induced morphological changes in Purkinje cell dendritic trees; a phosphorylation-mimetic STK17B variant caused marked reduction in dendritic tree size; and STK17B inhibition partially rescued PKC activation-induced dendritic changes. Overexpression and pharmacological inhibition in primary Purkinje cell cultures, phospho-mimetic mutant (STK17B-S350D equivalent), morphological quantification The European journal of neuroscience Medium 34536317
2023 DRAK2 regulates IL-2 signaling by inhibiting STAT5A phosphorylation, not by limiting TCR signaling as previously hypothesized. Enhanced sensitivity to IL-2 in Drak2-/- mice augments thymic regulatory T cell (Treg) development, and resistance to T1D requires Treg presence. Drak2-/- NOD mice, T cell-specific conditional approaches, adoptive transfer with/without Tregs, STAT5A phosphorylation assays, Treg development analysis Cell reports Medium 36773294
2024 DRAK2 directly phosphorylates ULK1 at Ser56, leading to ULK1 ubiquitylation and suppression of autophagy. In pancreatic β cells, this DRAK2-ULK1 axis impairs mitochondrial function and insulin secretion upon lipotoxic stress. Conditional β cell-specific DRAK2 knockout preserved autophagy and mitochondrial function under high-fat diet. Phosphoproteome analysis of primary mouse islets, ULK1-S56A point mutant rescue, DRAK2 conditional KO mice, in vitro kinase assay (direct phosphorylation), autophagy and mitochondrial function assays Science translational medicine High 38324636
2024 DRAK2 phosphorylates myosin light chain 2 (MLC2) in T cells. In the absence of DRAK2, polymerized actin is decreased, and myosin-dependent T cell functions including migration, TCR microcluster accumulation, and conjugation to antigen-presenting cells are impaired. Drak2-/- T cell functional assays, actin polymerization assay, phosphorylation analysis of MLC2, T cell-APC conjugation assay, TCR microcluster imaging Journal of cell science Medium 39421891
2024 Pharmacological STK17B inhibitors identify Ser19 on myosin light chain 2 (MLC2) as a STK17B substrate by mass spectrometry-based phosphoproteomics. In mouse T cell activation assays, STK17B inhibitors enhanced IL-2 production and enhanced T cell priming (CD69, IL-2, IFN-γ upregulation) in vivo. MS-based phosphoproteomics with selective kinase inhibitors, flow cytometry pharmacodynamic assay, in vivo T cell activation assay Frontiers in immunology Medium 39502695
2026 STK17B phosphorylates IREB2 at Ser157 and HSPB1 at Ser15, identified by proximity labeling combined with phosphoproteomic analysis. This modulates the balance between proferroptotic transferrin receptor and antiferroptotic ferritin heavy chain, suppressing ferroptosis in multiple myeloma cells. STK17B also indirectly maintains activating phosphorylation of STAT3. Proximity labeling (BioID or similar) combined with phosphoproteomics, site-specific phosphorylation validation, ferroptosis assays (labile iron pool, lipid peroxidation), xenograft mouse model, selective STK17B inhibitor Blood Medium 40953235

Source papers

Stage 0 corpus · 47 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2021 DRAK2 aggravates nonalcoholic fatty liver disease progression through SRSF6-associated RNA alternative splicing. Cell metabolism 79 34614409
2004 A deficiency in Drak2 results in a T cell hypersensitivity and an unexpected resistance to autoimmunity. Immunity 58 15589167
2008 Drak2 contributes to West Nile virus entry into the brain and lethal encephalitis. Journal of immunology (Baltimore, Md. : 1950) 55 18641347
2018 STK17B promotes carcinogenesis and metastasis via AKT/GSK-3β/Snail signaling in hepatocellular carcinoma. Cell death & disease 49 29445189
2012 DRAK2 participates in a negative feedback loop to control TGF-β/Smads signaling by binding to type I TGF-β receptor. Cell reports 33 23122956
2017 Discovery of benzofuran-3(2H)-one derivatives as novel DRAK2 inhibitors that protect islet β-cells from apoptosis. European journal of medicinal chemistry 32 28249207
2006 Transgenic drak2 overexpression in mice leads to increased T cell apoptosis and compromised memory T cell development. The Journal of biological chemistry 30 16517594
2003 The apoptosis-inducing protein kinase DRAK2 is inhibited in a calcium-dependent manner by the calcium-binding protein CHP. Journal of biochemistry 29 12966074
2007 Nuclear localization signal and phosphorylation of Serine350 specify intracellular localization of DRAK2. Journal of biochemistry 28 18084041
2006 Nuclear localization of the serine/threonine kinase DRAK2 is involved in UV-induced apoptosis. Biological & pharmaceutical bulletin 27 16462023
2009 Drak2 is upstream of p70S6 kinase: its implication in cytokine-induced islet apoptosis, diabetes, and islet transplantation. Journal of immunology (Baltimore, Md. : 1950) 25 19342653
2008 Drak2 overexpression results in increased beta-cell apoptosis after free fatty acid stimulation. Journal of cellular biochemistry 25 18777517
2008 Enhanced T cell apoptosis within Drak2-deficient mice promotes resistance to autoimmunity. Journal of immunology (Baltimore, Md. : 1950) 25 19017949
2024 DRAK2 suppresses autophagy by phosphorylating ULK1 at Ser56 to diminish pancreatic β cell function upon overnutrition. Science translational medicine 24 38324636
2010 Knobbed acrosome defect is associated with a region containing the genes STK17b and HECW2 on porcine chromosome 15. BMC genomics 23 21143916
2005 DRAK2, a lymphoid-enriched DAP kinase, regulates the TCR activation threshold during thymocyte selection. International immunology 23 16172133
2008 Drak2 regulates the survival of activated T cells and is required for organ-specific autoimmune disease. Journal of immunology (Baltimore, Md. : 1950) 22 19017948
2020 A Chemical Probe for Dark Kinase STK17B Derives Its Potency and High Selectivity through a Unique P-Loop Conformation. Journal of medicinal chemistry 21 33215924
2013 The MYB oncogene can suppress apoptosis in acute myeloid leukemia cells by transcriptional repression of DRAK2 expression. Leukemia research 21 23398943
2006 Modulation of DRAK2 autophosphorylation by antigen receptor signaling in primary lymphocytes. The Journal of biological chemistry 20 17182616
2016 Discovery of indirubin derivatives as new class of DRAK2 inhibitors from high throughput screening. Bioorganic & medicinal chemistry letters 19 27106709
2014 Synthesis and structure-activity relationship studies of 2-(1,3,4-oxadiazole-2(3H)-thione)-3-amino-5-arylthieno[2,3-b]pyridines as inhibitors of DRAK2. ChemMedChem 19 25146684
2009 Regulation of the apoptosis-inducing kinase DRAK2 by cyclooxygenase-2 in colorectal cancer. British journal of cancer 19 19638987
2010 Protein kinase D orchestrates the activation of DRAK2 in response to TCR-induced Ca2+ influx and mitochondrial reactive oxygen generation. Journal of immunology (Baltimore, Md. : 1950) 15 21148796
2007 Anti-viral effector T cell responses and trafficking are not dependent upon DRAK2 signaling following viral infection of the central nervous system. Autoimmunity 15 17364498
2021 STK17B promotes the progression of ovarian cancer. Annals of translational medicine 14 33850872
2021 Serine/threonine kinase 17b (STK17B) signalling regulates Purkinje cell dendritic development and is altered in multiple spinocerebellar ataxias. The European journal of neuroscience 14 34536317
2015 Drak2 is not required for tumor surveillance and suppression. International immunology 13 25568303
2022 Understanding the P-Loop Conformation in the Determination of Inhibitor Selectivity Toward the Hepatocellular Carcinoma-Associated Dark Kinase STK17B. Frontiers in molecular biosciences 11 35620482
2009 Altered thymic selection and increased autoimmunity caused by ectopic expression of DRAK2 during T cell development. Journal of immunology (Baltimore, Md. : 1950) 11 19542440
2020 DAP Kinase-Related Apoptosis-Inducing Protein Kinase 2 (DRAK2) Is a Key Regulator and Molecular Marker in Chronic Lymphocytic Leukemia. International journal of molecular sciences 10 33081245
2015 Drak2 Does Not Regulate TGF-β Signaling in T Cells. PloS one 10 25951457
2012 Loss of DRAK2 signaling enhances allogeneic transplant survival by limiting effector and memory T cell responses. American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons 10 22494341
2008 A role for DRAK2 in the germinal center reaction and the antibody response. Autoimmunity 10 18568639
2007 DRAK2 regulates memory T cell responses following murine coronavirus infection. Autoimmunity 10 17966037
2013 An epistatic interaction between the PAX8 and STK17B genes in papillary thyroid cancer susceptibility. PloS one 9 24086368
2023 DRAK2 contributes to type 1 diabetes by negatively regulating IL-2 sensitivity to alter regulatory T cell development. Cell reports 8 36773294
2026 Targeting STK17B kinase activates ferroptosis and suppresses drug resistance in multiple myeloma. Blood 6 40953235
2022 New insights into the characteristics of DRAK2 and its role in apoptosis: From molecular mechanisms to clinically applied potential. Frontiers in pharmacology 6 36386181
2024 Evaluation of STK17B as a cancer immunotherapy target utilizing highly potent and selective small molecule inhibitors. Frontiers in immunology 5 39502695
2022 Mechanistic Insights into the Mechanism of Inhibitor Selectivity toward the Dark Kinase STK17B against Its High Homology STK17A. Molecules (Basel, Switzerland) 5 35889528
2024 DRAK2 regulates myosin light chain phosphorylation in T cells. Journal of cell science 4 39421891
2024 Methionine deprivation inhibits glioma proliferation and EMT via the TP53TG1/miR-96-5p/STK17B ceRNA pathway. NPJ precision oncology 4 39572759
2024 Bicyclic polyprenylated acylphloroglucinol-related meroterpenoids as potent DRAK2 inhibitors from Hypericum patulum. Phytochemistry 3 39733941
2026 Tanshinone IIA alleviates chronic endometritis via DRAK2 inhibition to restore mitochondrial function and suppress KDM3A-SLC2A3-driven NETs formation. Journal of molecular histology 0 42141237
2026 Design, synthesis, and evaluation of novel thieno[2,3-b]pyridine derivatives as DRAK2 inhibitors. European journal of medicinal chemistry 0 42251818
2025 Novel thieno[2,3-b]pyridine derivatives protect islet through DRAK2 kinase inhibition. European journal of medicinal chemistry 0 41109008

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