Affinage

VRK1

Serine/threonine-protein kinase VRK1 · UniProt Q99986

Length
396 aa
Mass
45.5 kDa
Annotated
2026-06-11
100 papers in source corpus 38 papers cited in narrative 38 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 10/10 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

VRK1 is a nuclear serine/threonine chromatin kinase that couples mitogenic and genotoxic signals to cell cycle entry, chromatin dynamics, nuclear envelope organization, and DNA damage responses (PMID:10951572, PMID:18286197, PMID:25923214). It was originally cloned as a kinase distantly related to vaccinia virus B1R (PMID:9344656) and shown to autophosphorylate and phosphorylate p53 at Thr18 within the MDM2-binding loop, with a C-terminal nuclear localization signal directing it to the nucleus (PMID:10951572). As an early-response gene induced by serum, VRK1 drives the G0/G1 transition: its loss blocks cells in G1 with reduced phospho-Rb, cyclin D1, and PCNA (PMID:16547155, PMID:18286197), and it activates cyclin D1 expression by phosphorylating CREB at Ser133 and promoting its recruitment to the CCND1 promoter (PMID:18713830). VRK1 stabilizes and activates the transcription factors ATF2 and c-Jun through phosphorylation, paralleling JNK targeting (PMID:15105425, PMID:15378002). In the DNA damage response, VRK1 acts upstream of and independently of ATM, phosphorylating histone H2AX (Ser139/γH2AX), NBS1 (Ser343), and 53BP1 to support damage focus formation, and phosphorylating Tip60/KAT5 at T158 to license its acetyltransferase activity toward histones and ATM (PMID:22621922, PMID:25923214, PMID:26869104, PMID:33076429, PMID:36280132). Structural work defined a C-terminal tail that folds onto the catalytic site and an arginine-rich tail that engages linker DNA and the nucleosome acidic patch for histone H3T3 phosphorylation; disease-associated mutations in this motif disrupt nucleosome binding and mitotic localization (PMID:21543316, PMID:35390161). VRK1 regulates nuclear envelope assembly and mitotic chromosome segregation by phosphorylating BAF/BANF1, controlling its dynamic dissociation from chromatin (PMID:17170708, PMID:24430874), and maintains Cajal bodies by phosphorylating coilin at Ser184 to prevent its degradation (PMID:26068304). Its kinase activity is negatively regulated by RanGDP, macroH2A1.2, SIRT2, and reciprocal cross-inhibition with Aurora B (PMID:18617507, PMID:22194607, PMID:29340707, PMID:36902348). VRK1 and its paralog VRK2 are synthetic-lethal, rendering VRK2-deficient cancers selectively dependent on VRK1 via BAF phosphorylation (PMID:36069976). Beyond its core nuclear roles, VRK1 also acts in a Plk3-driven Golgi fragmentation cascade (PMID:19103756), gluconeogenic signaling via PXR (PMID:28911860), AMPK activation and longevity (PMID:32937443), cGAS-STING interferon signaling (PMID:38536553), and EMT through a CHD1L-SNAI1 axis (PMID:40234378).

Mechanistic history

Synthesis pass · year-by-year structured walk · 28 steps
  1. 1997 Medium

    Established VRK1 as a distinct serine/threonine kinase family member, providing the molecular identity needed to study its function.

    Evidence cDNA cloning and sequence analysis against vaccinia B1R kinase

    PMID:9344656

    Open questions at the time
    • No in vitro kinase activity or substrate demonstrated
    • No subcellular localization or cellular role defined
  2. 2000 High

    Demonstrated VRK1 is a catalytically active nuclear kinase with p53 Thr18 as a defined substrate, opening the link to the p53 stress-response axis.

    Evidence In vitro kinase assays with GST substrates, autophosphorylation, GFP localization and domain mapping

    PMID:10951572

    Open questions at the time
    • Functional consequence of p53 Thr18 phosphorylation not resolved in cells
    • Physiological substrate repertoire still unknown
  3. 2004 High

    Extended VRK1 substrate scope to AP-1 transcription factors, showing it stabilizes and activates ATF2 and c-Jun in parallel with the JNK pathway.

    Evidence In vitro kinase assays, Co-IP, site mutagenesis, and transcriptional reporters

    PMID:15105425 PMID:15378002

    Open questions at the time
    • In vivo physiological context of these phosphorylations unclear
    • Relative contribution versus JNK not quantified
  4. 2006 Medium

    Defined VRK1 as a serum-induced early-response gene required for the G0/G1 transition, framing it as a proliferation driver.

    Evidence Serum stimulation, siRNA knockdown, flow cytometry, cell-cycle marker western blots

    PMID:16547155 PMID:18286197

    Open questions at the time
    • Direct kinase substrates mediating G1 arrest not identified here
    • Single-lab phenotype
  5. 2006 High

    Established the conserved nuclear-envelope role of VRK1 via BAF phosphorylation using a genetically tractable in vivo model.

    Evidence RNAi and temperature-sensitive mutants with live imaging in C. elegans

    PMID:17170708

    Open questions at the time
    • Direct BAF phosphosite not defined in this study
    • Mammalian conservation not yet shown at this stage
  6. 2008 High

    Mechanistically connected VRK1 to cyclin D1 induction through CREB Ser133 phosphorylation and promoter recruitment, downstream of Myc.

    Evidence In vitro kinase assay, ChIP, kinase-dead mutant, luciferase reporter

    PMID:18713830

    Open questions at the time
    • How serum/Myc signal activates VRK1 not resolved
    • Endogenous CREB occupancy dynamics not fully mapped
  7. 2008 High

    Identified upstream regulatory inputs: Plk3 phosphorylates VRK1 at Ser342 to drive Golgi fragmentation, and RanGDP inhibits VRK1 activity, revealing signal-dependent control.

    Evidence Reciprocal Co-IP, in vitro kinase assays, site-mutant epistasis, pulldown with Ran mutants

    PMID:18617507 PMID:19103756

    Open questions at the time
    • Physiological trigger linking Ran nucleotide state to VRK1 in vivo unclear
    • Golgi role mechanism downstream of Ser342 incomplete
  8. 2008 Medium

    Showed a feedback loop in which p53 downregulates VRK1 via DRAM-dependent autophagy, defining reciprocal regulation between VRK1 and p53.

    Evidence DRAM/Beclin1 siRNA, leptomycin B, autophagy marker western blots

    PMID:21386980

    Open questions at the time
    • Direct mechanism of VRK1 autophagic targeting not defined
    • Single-lab pathway tracing
  9. 2009 Medium

    Demonstrated physiological requirement for VRK1 in proliferating germline tissue through a hypomorphic mouse with spermatogenesis failure.

    Evidence Gene-trap mouse genetics, histology, expression analysis

    PMID:19696012

    Open questions at the time
    • Molecular substrate underlying spermatogonial defect not identified here
    • Hypomorph rather than null
  10. 2010 Medium

    Placed VRK1 genetically upstream of p53 in controlling germ cell proliferation, reinforcing a conserved VRK1–p53 antagonism.

    Evidence Genome-wide RNAi and double-mutant epistasis in C. elegans

    PMID:20599896

    Open questions at the time
    • Direct biochemical link to CEP-1/p53 not established
    • Mechanism of negative regulation unclear
  11. 2011 High

    Provided the structural basis of VRK1 catalysis, showing the C-terminal tail is integral to activity, and identified macroH2A1.2 as a cell-cycle-dependent inhibitor.

    Evidence NMR solution structure, deletion-mutant kinase assays, NMR binding of macroH2A1.2

    PMID:21543316 PMID:22194607

    Open questions at the time
    • Full-length structure including arginine-rich tail not resolved here
    • How macroH2A1.2 occludes catalysis structurally unknown
  12. 2011 Medium

    Extended VRK1's developmental requirement to female meiosis, with chromosome segregation defects independent of p53.

    Evidence Gene-trap hypomorph, meiotic chromosome spreads, p53-knockout epistasis

    PMID:21277975

    Open questions at the time
    • Substrate driving meiotic defect not identified
    • Hypomorphic rather than null
  13. 2012 High

    Established VRK1 as an ATM-independent apical DNA damage response kinase that phosphorylates 53BP1 and supports damage signaling and telomere maintenance via hnRNP A1.

    Evidence In vitro kinase assays, siRNA with focus quantification, siRNA-resistant rescue, EMSA and telomerase assays

    PMID:22621922 PMID:22740652

    Open questions at the time
    • How VRK1 is activated by double-strand breaks unresolved
    • Direct 53BP1 phosphosite not defined
  14. 2014 High

    Quantified VRK1's control of BAF mobility in mammalian cells, linking BAF phosphorylation to nuclear envelope architecture and faithful mitosis.

    Evidence siRNA knockdown, GFP-BAF FRAP, live-cell imaging, mitotic phenotype scoring

    PMID:24430874

    Open questions at the time
    • Direct BAF phosphosite in mammalian cells not mapped here
    • Spatial coordination of BAF phosphorylation cycle incomplete
  15. 2014 Medium

    Showed VRK1 forms a basal complex with p53 via its DNA-binding domain and rapidly phosphorylates Thr18 upon UV damage before p53 accumulation.

    Evidence Co-IP, in vitro kinase assay, UV treatment, phospho-p53 western blot

    PMID:24492002

    Open questions at the time
    • Stoichiometry and dynamics of the preassembled complex unclear
    • Reciprocal validation limited
  16. 2015 High

    Defined VRK1 as a nucleosomal chromatin kinase required for histone acetylation and γH2AX formation, and as a regulator of Cajal body integrity and neuronal development.

    Evidence Chromatin fractionation, histone Co-IP, kinase-dead rescue, coilin phosphosite mapping, in utero electroporation shRNA

    PMID:25609612 PMID:25923214 PMID:26068304

    Open questions at the time
    • Mechanism linking VRK1 to H3/H4 acetylation machinery only partly defined
    • Non-catalytic migration function mechanism unknown
  17. 2016 High

    Identified NBS1 Ser343 as a VRK1 substrate within a preassembled complex, contributing to NBS1 stability and ATM-independent damage focus formation.

    Evidence Co-IP, in vitro kinase assay in ATM-/- cells, focus imaging, proteasome inhibition, RNF8 knockdown

    PMID:26869104

    Open questions at the time
    • Integration with canonical MRN/ATM signaling not fully resolved
    • Single-lab
  18. 2017 Medium

    Expanded VRK1 into metabolic signaling, phosphorylating PXR Ser350 to control a gluconeogenic cascade gated by CDK2 and glucose status.

    Evidence In vitro kinase assay, Co-IP, glucose-dependent assays, fasting mouse liver

    PMID:28911860

    Open questions at the time
    • Tissue-specificity and physiological magnitude unclear
    • Single-lab pathway
  19. 2018 High

    Revealed mutual cross-inhibition between VRK1 and Aurora B over histone H3 phosphorylation, coupling VRK1 to mitotic survivin/centromere function.

    Evidence Co-IP, in vitro cross-inhibition kinase assays, kinase-active vs dead rescue, mitotic imaging

    PMID:29340707

    Open questions at the time
    • Spatiotemporal regulation of the antagonism in mitosis unclear
    • Structural basis of cross-inhibition unknown
  20. 2020 High

    Mechanistically dissected VRK1 control of Tip60/KAT5, showing T158 phosphorylation licenses Tip60 acetyltransferase activity toward ATM and histones in a sequential code with DNA-PK.

    Evidence In vitro kinase assays, ATM-/- context, phosphomutants, chromatin fractionation, DNA-PK inhibition

    PMID:33076429 PMID:36280132

    Open questions at the time
    • Ordering of VRK1 versus DNA-PK inputs across damage types incomplete
    • Single-lab
  21. 2020 High

    Demonstrated a conserved VRK1 role in activating AMPK to promote longevity, broadening its substrate range beyond chromatin.

    Evidence In vitro kinase assay, C. elegans lifespan and epistasis, human cell corroboration

    PMID:32937443

    Open questions at the time
    • AMPK phosphosite and mammalian physiological role not defined
    • Link to nuclear functions unclear
  22. 2021 Medium

    Showed vaccinia B12 pseudokinase targets VRK1 to block its inactivation of BAF, defining a host-pathogen control point at the VRK1–BAF interface.

    Evidence Proteomic interactome, VRK1 KD/OE, viral replication assays, imaging

    PMID:33177193

    Open questions at the time
    • Direct biochemical mechanism of B12 inhibition unresolved
    • Single-lab
  23. 2022 High

    Provided the structural mechanism of nucleosome engagement, showing an arginine-rich C-terminal tail binds the acidic patch and linker DNA, with disease mutations disrupting this and mitotic localization.

    Evidence Cryo-EM, nucleosome binding assays, disease-mutant localization tests

    PMID:35390161

    Open questions at the time
    • Functional consequence of disrupted acidic-patch binding on substrate phosphorylation in vivo incomplete
    • Disease genotype-phenotype not mapped here
  24. 2022 High

    Established VRK1–VRK2 synthetic lethality through BAF phosphorylation, defining a therapeutic dependency in VRK2-deficient cancers.

    Evidence CRISPR knockdown, VRK2 rescue, phospho-BAF blots, imaging, flow cytometry, xenografts

    PMID:36069976

    Open questions at the time
    • Determinants of selectivity beyond BAF unclear
    • Resistance mechanisms not addressed
  25. 2022 Medium

    Challenged the assignment of mitotic H3T3/S10 phosphorylation to VRK1, attributing mitotic H3T3ph to Haspin and constraining VRK1's interphase chromatin role.

    Evidence In vitro kinase assays, KiPIK screening, RNAi, CRISPR knockout

    PMID:35778595

    Open questions at the time
    • Reconciliation with VRK1 H3T3 activity reported elsewhere unresolved
    • Context-dependence of H3 phosphorylation not settled
  26. 2023 Medium

    Identified SIRT2 as a direct inhibitor of VRK1 controlling H4K16 acetylation and chromatin accessibility during the damage response.

    Evidence In vitro pull-down and kinase inhibition, Co-IP, H4K16ac western blot, imaging

    PMID:36902348

    Open questions at the time
    • Whether inhibition is allosteric or steric unclear
    • Single-lab
  27. 2024 Medium

    Linked VRK1 to innate immune signaling, showing it potentiates cGAS-STING-dependent type I interferon production at the STING level.

    Evidence siRNA, VRK-IN-1 inhibition, qPCR and reporter assays in human/murine cells and BMDMs

    PMID:38536553

    Open questions at the time
    • Direct STING-pathway substrate not identified
    • Mechanism of STING-level potentiation unresolved
  28. 2025 Medium

    Defined a VRK1–CHD1L–SNAI1 axis driving EMT in hepatocellular carcinoma, extending VRK1's oncogenic reach.

    Evidence Co-IP/MS, in vitro kinase assay with phosphosite, RNA-seq, KD/OE functional assays

    PMID:40234378

    Open questions at the time
    • In vivo tumor relevance not fully established
    • Single-lab

Open questions

Synthesis pass · forward-looking unresolved questions
  • How VRK1 kinase activity is switched on by distinct mitogenic versus genotoxic upstream signals, and how its many substrate engagements are spatially and temporally prioritized, remains unresolved.
  • No unified model of VRK1 activation upstream of DNA damage
  • Substrate selection logic across cell-cycle phases undefined
  • Context dependence of H3T3 phosphorylation unsettled

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 12 GO:0098772 molecular function regulator activity 4 GO:0016740 transferase activity 3 GO:0042393 histone binding 2 GO:0003677 DNA binding 1
Localization
GO:0000228 nuclear chromosome 3 GO:0005634 nucleus 3 GO:0005635 nuclear envelope 2 GO:0005794 Golgi apparatus 2 GO:0005829 cytosol 1
Pathway
R-HSA-1640170 Cell Cycle 5 R-HSA-4839726 Chromatin organization 5 R-HSA-73894 DNA Repair 5 R-HSA-74160 Gene expression (Transcription) 4 R-HSA-1852241 Organelle biogenesis and maintenance 3
Partners
ATF2AURKBBANF1JUNKAT5NBS1PLK3TP53

Evidence

Reading pass · 38 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 VRK1 was identified as a novel serine/threonine kinase with 40% amino acid identity to vaccinia virus B1R kinase over 305 residues, establishing it as a member of a new kinase family related to, but distinct from, casein kinase 1. cDNA cloning, sequence analysis, Northern blotting Genomics Medium 9344656
2000 VRK1 phosphorylates p53 specifically at threonine-18 (within the mdm-2 binding site/hydrophobic loop), has strong autophosphorylating activity, and phosphorylates acidic substrates (phosvitin, casein) and basic substrates (histone H2B, myelin basic protein). The C-terminal domain (residues 268–396) contains a nuclear localization signal that targets VRK1 to the nucleus. In vitro kinase assay with GST-fusion substrates, autophosphorylation assay, GFP-fusion subcellular localization Oncogene High 10951572
2004 VRK1 phosphorylates ATF2 at Thr-73 and Ser-62, stabilizing ATF2 protein and increasing its intracellular level. VRK1 colocalizes with ATF2 in the nucleus and forms a stable complex. A kinase-dead VRK1 (K179E) or T73A ATF2 substitution prevents ATF2 accumulation and transcriptional activation. VRK1 and JNK have additive effects on ATF2-dependent transcription at suboptimal doses. In vitro kinase assay, co-immunoprecipitation, mutagenesis, transcriptional reporter assay, immunofluorescence colocalization The Journal of biological chemistry High 15105425
2004 VRK1 phosphorylates c-Jun at Ser63 and Ser73 in vitro (the same residues targeted by JNK), stabilizes and accumulates c-Jun protein, activates c-Jun-dependent transcription, and interacts with c-Jun but not with JNK. VRK1 and JNK have additive effects on c-Jun transcriptional activation at suboptimal doses. In vitro kinase assay, immunoprecipitation, transcriptional reporter assay, western blot for endogenous phospho-c-Jun Oncogene High 15378002
2006 In C. elegans, VRK-1 (the VRK1 ortholog) phosphorylates BAF-1 and regulates BAF localization. VRK-1 localizes to the nuclear envelope and chromatin in a cell-cycle-dependent manner. Depletion of VRK-1 causes mitotic defects including impaired nuclear envelope formation and BAF delocalization. RNAi depletion, temperature-sensitive mutant analysis, live imaging, immunofluorescence in C. elegans embryos The EMBO journal High 17170708
2006 VRK1 is an early-response gene: its expression is induced upon serum addition to starved cells (paralleling MYC, FOS, CCND1), and its loss via siRNA causes G1 block in cell division with loss of phosphorylated-Rb and cyclin D1. Serum stimulation of starved cells, siRNA knockdown, flow cytometry cell cycle analysis, western blot for proliferation markers Molecular cancer research : MCR Medium 16547155
2007 Most intracellular VRK1 protein is nuclear, but a subpopulation localizes to the cytosol and Golgi apparatus depending on cell type. A T355 phosphomimetic substitution near the nuclear localization signal alters antibody reactivity, suggesting post-translational modification regulates VRK1 subcellular distribution. Immunofluorescence in cell lines, immunohistochemistry of human biopsies, phosphomimetic mutagenesis Archives of biochemistry and biophysics Low 17617371
2008 VRK1 phosphorylates CREB at Ser133 in vitro and in cells. VRK1 facilitates recruitment of phospho-CREB to the CRE element in the CCND1 promoter to drive cyclin D1 expression. Kinase-dead VRK1 or VRK1 siRNA knockdown fails to activate CREB or CRE-driven transcription. VRK1 is a critical link in the CCND1 expression pathway downstream of Myc overexpression. In vitro kinase assay, ChIP, siRNA knockdown, luciferase reporter assay, western blot Journal of cell science High 18713830
2008 VRK1 downregulation by p53 occurs through the autophagic/lysosomal pathway and requires DRAM (a p53-induced gene in the endosomal-lysosomal compartment). DNA damage (UV, IR, etoposide, doxorubicin) stabilizes p53, induces DRAM, and leads to VRK1 downregulation; this process requires nuclear export of VRK1 (blocked by leptomycin B) and Beclin1, and results in reduced p53 Thr18 phosphorylation. siRNA knockdown of DRAM, leptomycin B treatment, LC3/p62 western blot, Beclin1 RNAi, overexpression assays PloS one Medium 21386980
2008 Plk3 interacts with VRK1, forming a stable complex. Plk3 phosphorylates the C-terminal region of VRK1 at Ser342 but VRK1 does not phosphorylate Plk3. Phosphorylation of VRK1 at Ser342 is required for Golgi fragmentation: VRK1 with S342 substitutions is catalytically active but blocks Golgi fragmentation. VRK1 and Plk3 represent consecutive steps in the MEK1-Plk3-VRK1 Golgi fragmentation cascade. Reciprocal immunoprecipitation, pull-down assay, in vitro kinase assay, siRNA knockdown, immunofluorescence (Golgi marker giantin), dominant-negative approaches Molecular and cellular biology High 19103756
2008 Ran GTPase interacts with and inhibits VRK1 kinase activity. RanGDP (inactive form, especially RanT24N) strongly inhibits VRK1 autophosphorylation and VRK1-mediated histone H3 phosphorylation; active RanGTP or RanL43E relieves this inhibition. Ran does not interact with RCC1 directly through VRK1, but can form a ternary complex. VRK1 does not phosphorylate Ran or RCC1. Pulldown of endogenous proteins, reciprocal immunoprecipitation, mass spectrometry, in vitro kinase assay with Ran mutants Molecular & cellular proteomics : MCP High 18617507
2008 VRK1 is an early-response gene required for cell cycle entry at G0/G1. siRNA-mediated VRK1 loss results in G1 block, loss of phosphorylated-Rb, cyclin D1, and PCNA, and reduced cell proliferation. VRK1 expression is induced by serum and correlates inversely with p27. siRNA knockdown, serum stimulation, flow cytometry, western blot for cell cycle markers, reporter assay PloS one Medium 18286197
2009 VRK1 hypomorphic mice (GT3/GT3, ~15% wild-type VRK1) are viable but infertile. VRK1 is expressed in Sertoli cells and spermatogonia, and its loss results in a progressive defect in spermatogonial proliferation/differentiation, ultimately eliminating mitotic and meiotic cells from adult testis. Gene-trap mouse genetics, histology, in situ expression analysis Biology of reproduction Medium 19696012
2010 In C. elegans, VRK-1 is required for normal germ cell proliferation, and acts in part by negatively regulating CEP-1 (p53) activity. Loss of cep-1 significantly rescues vrk-1 proliferation defects, placing VRK-1 upstream of CEP-1/p53 in germline proliferation control. Genome-wide RNAi screen, genetic epistasis (double mutant rescue), gene expression profiling Developmental biology Medium 20599896
2011 NMR solution structure of catalytically active human VRK1 (residues 1–361) revealed that the C-terminal tail orients toward the catalytic site and forms interactions critical for structural stability and catalysis. Deletion of the C-terminal tail dramatically reduces autocatalytic activity. ATP binding involves the hinge region, catalytic loop, and DYG motif, with additional contacts from C-terminal tail residues. NMR solution structure determination, deletion mutant kinase assays, NMR titration with ATP/ATP analogs The Journal of biological chemistry High 21543316
2011 MacroH2A1.2 directly interacts with VRK1 and suppresses VRK1-mediated histone H3 phosphorylation during interphase. MacroH2A1.2 levels are markedly reduced in mitosis, thereby relieving VRK1 inhibition. VRK1-macroH2A1.2 interaction was confirmed by NMR spectroscopy. Co-immunoprecipitation, NMR spectroscopy (binding characterization), cell cycle synchronization, western blot for H3 phosphorylation The Journal of biological chemistry High 22194607
2011 The kinase VRK1 is required for normal meiotic progression in female mouse oogenesis. VRK1 reduction (gene-trap hypomorph) causes delayed meiotic progression, lagging chromosomes at the metaphase plate, and failure of oocyte fertilization. These defects are independent of p53 activity. Gene-trap mouse hypomorph, histology, meiotic chromosome spreads, p53 knockout epistasis Mechanisms of development Medium 21277975
2012 VRK1 directly phosphorylates 53BP1 in serum-starved cells in response to ionizing radiation-induced double-strand breaks. VRK1 knockdown causes defective 53BP1 foci formation (reduced number and size) after IR; this effect is p53- and ATM-independent and is rescued by siRNA-resistant VRK1 mutants. VRK1 knockdown also prevents activating phosphorylation of ATM, CHK2, and DNA-PK in response to IR. In vitro kinase assay, siRNA knockdown, immunofluorescence for 53BP1 foci, western blot for ATM/CHK2/DNA-PK phosphorylation, siRNA-resistant rescue constructs The Journal of biological chemistry High 22621922
2012 VRK1 phosphorylates hnRNP A1, and this phosphorylation potentiates hnRNP A1 binding to telomeric ssDNA and telomerase RNA in vitro, and enhances telomerase activity. VRK1 deficiency in mouse male germ cells causes telomere shortening with abnormal telomere arrangement and activation of DNA-damage signaling. In vitro kinase assay, EMSA (ssDNA binding), telomerase activity assay, mouse VRK1 hypomorph analysis Nucleic acids research Medium 22740652
2014 VRK1 depletion in MCF10a and MDA-MB-231 cells causes aberrant nuclear envelope architecture. GFP-BAF FRAP analysis shows elevated immobile fraction at the nuclear envelope in VRK1-depleted cells, indicating prolonged BAF-partner interactions. In VRK1-depleted cells, BAF does not disperse at mitosis onset but remains chromosome-bound throughout mitosis. VRK1 depletion also increases anaphase bridges and multipolar spindles. siRNA knockdown, FRAP of GFP-BAF, live-cell imaging, immunofluorescence for mitotic phenotypes Molecular biology of the cell High 24430874
2014 VRK1 forms a basal stable complex with p53 through the p53 DNA-binding domain. UV-induced DNA damage activates VRK1 and triggers phosphorylation of p53 at Thr-18 before p53 accumulates. Frequent DNA-contact p53 mutants (R273H, R248H, R280K) do not disrupt the VRK1-p53 complex. Co-immunoprecipitation, in vitro kinase assay, UV treatment, western blot for phospho-p53 Thr18 FEBS letters Medium 24492002
2015 VRK1 is a nucleosomal chromatin kinase that directly and stably interacts with histones H2AX and H3. VRK1 depletion causes loss of H3 and H4 acetylation (required for chromatin relaxation) in basal conditions and after DNA damage, independently of ATM. In response to ionizing radiation, VRK1 phosphorylates histone H2AX at Ser139 (γH2AX); VRK1 depletion prevents γH2AX foci formation, which is rescued by kinase-active but not kinase-dead VRK1. Chromatin fractionation, Co-immunoprecipitation with histones, siRNA knockdown, ionizing radiation, immunofluorescence for γH2AX foci, kinase-dead rescue Epigenetics High 25923214
2015 VRK1 directly interacts with and phosphorylates coilin at Ser184. Phosphorylation of coilin by VRK1 occurs during mitosis and regulates coilin stability: VRK1 knockdown or inactivation causes loss of coilin phosphorylation and Cajal body (CB) disassembly, leading to coilin ubiquitination (partly mediated by mdm2) and proteasomal degradation in the cytosol (after nuclear export). Kinase-active but not kinase-dead VRK1 rescues CB formation. Co-immunoprecipitation, in vitro kinase assay, siRNA knockdown, immunofluorescence, proteasome inhibitor (MG132), nuclear export inhibitor Scientific reports High 26068304
2015 VRK1 regulates neuronal migration and neuronal stem cell proliferation. In utero electroporation shRNA knockdown of Vrk1 in mice impairs cortical neuronal migration and affects cell cycle of neuronal progenitors; wild-type human VRK1 rescues both phenotypes. Kinase-dead VRK1 rescues migration but not proliferation, indicating the migration role is partly non-catalytic. VRK1 deficiency reduces amyloid-β precursor protein (APP) levels, and APP overexpression rescues the Vrk1 knockdown neuronal migration phenotype. In utero electroporation shRNA, cortical migration assay, kinase-dead rescue, western blot for APP, APP overexpression rescue The Journal of neuroscience Medium 25609612
2016 VRK1 phosphorylates NBS1 at Ser343, forming a basal preassembled complex with NBS1 in non-damaged cells. VRK1 knockdown causes loss of NBS1 foci after ionizing radiation (also in cell-cycle arrested and ATM−/− cells). NBS1 phosphorylation by VRK1 (induced by doxorubicin or IR) contributes to NBS1 stability: loss of this phosphorylation can be prevented by MG132 proteasome inhibitor or RNF8 knockdown. Co-immunoprecipitation, in vitro kinase assay (ATM−/− cells), siRNA knockdown, immunofluorescence for NBS1 foci, proteasome inhibitor treatment Biochimica et biophysica acta High 26869104
2017 VRK1 phosphorylates pregnane X receptor (PXR) at Ser350 in response to low glucose conditions, enabling PXR to scaffold PP2Cα, which dephosphorylates SGK2 at Thr193, releasing SGK2 repression of the PCK1 gluconeogenesis gene. CDK2 inhibits VRK1 activity toward PXR under high glucose conditions, forming a VRK1-CDK2-PXR-PP2Cα-SGK2 pathway regulating gluconeogenesis. In vitro kinase assay, co-immunoprecipitation, cell-based phosphorylation assays, CDK2 inhibition, fasting mouse liver analysis Cellular signalling Medium 28911860
2018 VRK1 and Aurora B (AURKB) form a stable protein complex (minor subpopulation, detected after nocodazole release). Each kinase inhibits the kinase activity of the other, and each inhibits the other's phosphorylation of histone H3 (VRK1 on Thr3, AURKB on Ser10). VRK1 depletion downregulates BIRC5 (survivin) expression and is rescued by kinase-active but not kinase-dead VRK1; loss of the H3-Thr3ph–survivin complex prevents AURKB localization to centromeres. Co-immunoprecipitation, in vitro kinase assay (cross-inhibition), siRNA knockdown, immunofluorescence, kinase-active vs. kinase-dead rescue Cellular and molecular life sciences : CMLS High 29340707
2020 In C. elegans, VRK-1 directly phosphorylates and activates AMPK, promoting longevity. VRK-1 overexpression increases lifespan and inhibition decreases lifespan; vrk-1 is required for longevity conferred by inhibited mitochondrial respiration (which requires AMPK). VRK-1 directly phosphorylates and upregulates AMPK in both C. elegans and human cultured cells. In vitro kinase assay (direct phosphorylation of AMPK), C. elegans lifespan assays, genetic epistasis with AMPK mutants, overexpression in cultured human cells Science advances High 32937443
2020 VRK1 directly phosphorylates Tip60/KAT5 in the chromatin fraction in response to DNA damage (doxorubicin). VRK1 depletion causes loss of Tip60 phosphorylation in both ATM+/+ and ATM−/− cells; kinase-active but not kinase-dead VRK1 rescues Tip60 phosphorylation. VRK1-mediated Tip60 phosphorylation is necessary for Tip60 acetyltransferase activity toward ATM (activating acetylation) and subsequent ATM autophosphorylation; both are lost by VRK1 depletion. In vitro kinase assay, Co-immunoprecipitation, siRNA knockdown (ATM+/+ and ATM−/− cells), Tip60 inhibitor (MG149), kinase-active/dead rescue Cancers High 33076429
2021 Vaccinia virus B12 pseudokinase directly interacts with VRK1 (as the most enriched B12 interactor by proteomics), and B12 interferes with VRK1's ability to phospho-inactivate BAF. VRK1 is required for rescue of B1-deleted virus; VRK1 overexpression overcomes B12-mediated repression of viral replication. B12 promotes VRK1 colocalization with cellular DNA during mitosis. Protein interactome (mass spectrometry), VRK1 knockdown and overexpression assays, viral replication assays, immunofluorescence Journal of virology Medium 33177193
2022 VRK1 interacts with both linker DNA and the nucleosome acidic patch to phosphorylate histone H3T3. Acidic patch binding is mediated by a C-terminal arginine-rich flexible tail. Disease-associated missense and nonsense mutations in this C-terminal acidic patch recognition motif disrupt nucleosome acidic patch binding and cause VRK1 mislocalization during mitosis. Cryo-electron microscopy, biochemical binding assays (chromatin/nucleosome), cellular localization assays (mitosis), analysis of disease-associated mutants Nucleic acids research High 35390161
2022 VRK1 and VRK2 are synthetic-lethal paralogs. In VRK2-null/methylated glioblastoma cells, VRK1 knockdown reduces phosphorylation of BAF, causing nuclear lobulation, blebbing, and micronucleation, followed by G2-M arrest and DNA damage. The synthetic-lethal interaction requires VRK1 kinase activity and is rescued by ectopic VRK2 expression. CRISPR/Cas9 knockdown, VRK2 ectopic expression rescue, phospho-BAF western blot, live-cell imaging (nuclear morphology), flow cytometry (G2-M arrest), xenograft models Cancer research High 36069976
2022 The VRK1 chromatin kinase regulates Tip60/KAT5 through sequential phosphorylation events: VRK1 phosphorylates Tip60 at T158 (early, transient), which protects Tip60 from ubiquitin-mediated degradation, promotes its recruitment from nucleoplasm to chromatin, and is necessary for full trans-acetylase activity. DNA-PK subsequently phosphorylates Tip60 at S199, enabling Tip60 autoacetylation; however, full trans-acetylation of H4 and ATM requires both T158 and S199 phosphorylation. In vitro kinase assay, phosphomimetic and phosphonull mutants, Co-immunoprecipitation, chromatin fractionation, DNA-PK inhibitor treatment Biochimica et biophysica acta. Gene regulatory mechanisms High 36280132
2022 Using in vitro kinase assays, KiPIK screening, RNAi, and CRISPR/Cas9 approaches, VRK1 and its paralog VRK2 could NOT be substantiated as the kinases responsible for histone H3 Thr3 or Ser10 phosphorylation during mitosis; Haspin is the kinase responsible for H3T3ph in mitosis. Loss of VRK1 did slow cell proliferation. In vitro kinase assays, KiPIK screening, RNA interference, CRISPR/Cas9 knockout Scientific reports Medium 35778595
2022 In zebrafish, Ankle2 deficiency causes microcephaly and spermatogenesis defects through dysregulated BAF phosphorylation. Heterozygous deletion of vrk1 or vrk1 morpholino knockdown rescues the Ankle2-deficient microcephaly and partially rescues spermatogenesis defects, placing VRK1 downstream of ANKLE2 in the BAF phosphorylation pathway regulating neurogenesis. Zebrafish genetic knockout and morpholino knockdown, genetic epistasis, brain size measurement, cell proliferation assays Biochemical and biophysical research communications Medium 35940133
2023 VRK1 kinase activity is inhibited by direct interaction with SIRT2 deacetylase through VRK1's N-terminal kinase domain. VRK1-SIRT2 interaction causes loss of H4K16 acetylation (similar to VRK1 inhibitor VRK-IN-1 or VRK1 depletion). SIRT2 inhibitors increase H4K16ac, cooperating with VRK1 in chromatin accessibility in response to DNA damage. In vitro interaction/pull-down assay, in vitro kinase assay, Co-immunoprecipitation, immunofluorescence, H4K16ac western blot International journal of molecular sciences Medium 36902348
2024 VRK1 promotes DNA-induced type I interferon production through the cGAS-STING pathway. VRK1 knockdown attenuates induction of type I IFNs and ISGs following HTDNA and Poly(dA:dT) stimulation; VRK-IN-1 (VRK1 inhibitor) similarly suppresses IFN-I induction. VRK1 potentiates the cGAS-STING-IFN-I axis at the level of STING. siRNA knockdown, pharmacological inhibition (VRK-IN-1), real-time PCR, dual-luciferase reporter assay in human and murine cell lines and primary BMDMs Molecular biology reports Medium 38536553
2025 VRK1 directly interacts with and phosphorylates CHD1L at serine 122. VRK1-CHD1L-SNAI1 forms an axis by which VRK1 promotes EMT in hepatocellular carcinoma: VRK1 phosphorylation of CHD1L upregulates SNAI1 expression (identified by RNA-seq as a key downstream target). Immunoprecipitation combined with mass spectrometry, in vitro kinase assay (phosphosite identification), RNA-seq, VRK1 overexpression/knockdown functional assays Cell death & disease Medium 40234378

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in post-mitotic nuclear envelope assembly. The EMBO journal 183 17170708
2009 Spinal muscular atrophy with pontocerebellar hypoplasia is caused by a mutation in the VRK1 gene. American journal of human genetics 130 19646678
1997 Identification of two novel human putative serine/threonine kinases, VRK1 and VRK2, with structural similarity to vaccinia virus B1R kinase. Genomics 122 9344656
2000 The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressor protein. Oncogene 118 10951572
2004 Human vaccinia-related kinase 1 (VRK1) activates the ATF2 transcriptional activity by novel phosphorylation on Thr-73 and Ser-62 and cooperates with JNK. The Journal of biological chemistry 103 15105425
2004 c-Jun phosphorylation by the human vaccinia-related kinase 1 (VRK1) and its cooperation with the N-terminal kinase of c-Jun (JNK). Oncogene 94 15378002
2008 Human VRK1 is an early response gene and its loss causes a block in cell cycle progression. PloS one 90 18286197
2008 VRK1 phosphorylates CREB and mediates CCND1 expression. Journal of cell science 84 18713830
2014 Depletion of the protein kinase VRK1 disrupts nuclear envelope morphology and leads to BAF retention on mitotic chromosomes. Molecular biology of the cell 78 24430874
2006 VRK1 signaling pathway in the context of the proliferation phenotype in head and neck squamous cell carcinoma. Molecular cancer research : MCR 74 16547155
2011 Roles of VRK1 as a new player in the control of biological processes required for cell division. Cellular signalling 71 21514377
2013 Mutations in VRK1 associated with complex motor and sensory axonal neuropathy plus microcephaly. JAMA neurology 61 24126608
2017 Circular RNA profile indicates circular RNA VRK1 is negatively related with breast cancer stem cells. Oncotarget 58 29221160
2015 VRK1 chromatin kinase phosphorylates H2AX and is required for foci formation induced by DNA damage. Epigenetics 57 25923214
2008 Plk3 interacts with and specifically phosphorylates VRK1 in Ser342, a downstream target in a pathway that induces Golgi fragmentation. Molecular and cellular biology 52 19103756
2012 Vaccinia-related kinase 1 (VRK1) is an upstream nucleosomal kinase required for the assembly of 53BP1 foci in response to ionizing radiation-induced DNA damage. The Journal of biological chemistry 51 22621922
2011 Downregulation of VRK1 by p53 in response to DNA damage is mediated by the autophagic pathway. PloS one 50 21386980
2019 Ginsenoside Rg3 regulates DNA damage in non-small cell lung cancer cells by activating VRK1/P53BP1 pathway. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 49 31629252
2021 The human VRK1 chromatin kinase in cancer biology. Cancer letters 46 33516791
2009 Mice deficient in the serine/threonine protein kinase VRK1 are infertile due to a progressive loss of spermatogonia. Biology of reproduction 44 19696012
2007 Identification of a dominant epitope in human vaccinia-related kinase 1 (VRK1) and detection of different intracellular subpopulations. Archives of biochemistry and biophysics 44 17617371
2018 Implication of the VRK1 chromatin kinase in the signaling responses to DNA damage: a therapeutic target? Cellular and molecular life sciences : CMLS 42 29679095
2018 VRK1 and AURKB form a complex that cross inhibit their kinase activity and the phosphorylation of histone H3 in the progression of mitosis. Cellular and molecular life sciences : CMLS 41 29340707
2008 Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities. Molecular & cellular proteomics : MCP 41 18617507
2014 VRK1 interacts with p53 forming a basal complex that is activated by UV-induced DNA damage. FEBS letters 39 24492002
2014 Vaccinia-related kinase 1 (VRK1) confers resistance to DNA-damaging agents in human breast cancer by affecting DNA damage response. Oncotarget 38 24731990
2011 Differential inhibitor sensitivity between human kinases VRK1 and VRK2. PloS one 38 21829721
2007 Alteration of the VRK1-p53 autoregulatory loop in human lung carcinomas. Lung cancer (Amsterdam, Netherlands) 38 17689819
2011 NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for its structural stability and autocatalytic activity. The Journal of biological chemistry 36 21543316
2011 Macro histone H2A1.2 (macroH2A1) protein suppresses mitotic kinase VRK1 during interphase. The Journal of biological chemistry 36 22194607
2015 VRK1 regulates Cajal body dynamics and protects coilin from proteasomal degradation in cell cycle. Scientific reports 34 26068304
2013 Molecular genetic analysis of VRK1 in mammary epithelial cells: depletion slows proliferation in vitro and tumor growth and metastasis in vivo. Oncogenesis 34 23732708
2012 HnRNP A1 phosphorylated by VRK1 stimulates telomerase and its binding to telomeric DNA sequence. Nucleic acids research 34 22740652
2016 Novel motor phenotypes in patients with VRK1 mutations without pontocerebellar hypoplasia. Neurology 33 27281532
2015 The spinal muscular atrophy with pontocerebellar hypoplasia gene VRK1 regulates neuronal migration through an amyloid-β precursor protein-dependent mechanism. The Journal of neuroscience : the official journal of the Society for Neuroscience 33 25609612
2022 VRK1 Is a Synthetic-Lethal Target in VRK2-Deficient Glioblastoma. Cancer research 32 36069976
2019 Olaparib and ionizing radiation trigger a cooperative DNA-damage repair response that is impaired by depletion of the VRK1 chromatin kinase. Journal of experimental & clinical cancer research : CR 31 31101118
2016 VRK1 phosphorylates and protects NBS1 from ubiquitination and proteasomal degradation in response to DNA damage. Biochimica et biophysica acta 30 26869104
2015 Expanding Phenotype of VRK1 Mutations in Motor Neuron Disease. Journal of clinical neuromuscular disease 30 26583493
2011 The kinase VRK1 is required for normal meiotic progression in mammalian oogenesis. Mechanisms of development 29 21277975
2021 HNRNP A1 Promotes Lung Cancer Cell Proliferation by Modulating VRK1 Translation. International journal of molecular sciences 28 34071140
2017 Expression of VRK1 and the downstream gene BANF1 in esophageal cancer. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 28 28298069
2020 VRK-1 extends life span by activation of AMPK via phosphorylation. Science advances 27 32937443
2020 VRK1 Phosphorylates Tip60/KAT5 and Is Required for H4K16 Acetylation in Response to DNA Damage. Cancers 27 33076429
2019 VRK1 functional insufficiency due to alterations in protein stability or kinase activity of human VRK1 pathogenic variants implicated in neuromotor syndromes. Scientific reports 27 31527692
2021 Circular RNA VRK1 facilitates pre-eclampsia progression via sponging miR-221-3P to regulate PTEN/Akt. Journal of cellular and molecular medicine 26 33738906
2017 VRK1 promotes cisplatin resistance by up-regulating c-MYC via c-Jun activation and serves as a therapeutic target in esophageal squamous cell carcinoma. Oncotarget 25 29029460
2017 Glucose elicits serine/threonine kinase VRK1 to phosphorylate nuclear pregnane X receptor as a novel hepatic gluconeogenic signal. Cellular signalling 24 28911860
2019 A novel mutation in VRK1 associated with distal spinal muscular atrophy. Journal of human genetics 23 30617279
2018 Overexpression of the VRK1 kinase, which is associated with breast cancer, induces a mesenchymal to epithelial transition in mammary epithelial cells. PloS one 23 30180179
2010 Genome-wide analysis of germ cell proliferation in C.elegans identifies VRK-1 as a key regulator of CEP-1/p53. Developmental biology 23 20599896
2008 The C/H3 domain of p300 is required to protect VRK1 and VRK2 from their downregulation induced by p53. PloS one 23 18612383
2022 Multivalent DNA and nucleosome acidic patch interactions specify VRK1 mitotic localization and activity. Nucleic acids research 22 35390161
2022 VRK1 as a synthetic lethal target in VRK2 promoter-methylated cancers of the nervous system. JCI insight 22 36040810
2019 Loss of Cajal bodies in motor neurons from patients with novel mutations in VRK1. Human molecular genetics 22 31090908
2015 High VRK1 expression contributes to cell proliferation and survival in hepatocellular carcinoma. Pathology, research and practice 20 26706601
2018 A novel VRK1 mutation associated with recessive distal hereditary motor neuropathy. Annals of clinical and translational neurology 19 30847374
2020 Identification of VRK1 as a New Neuroblastoma Tumor Progression Marker Regulating Cell Proliferation. Cancers 18 33233777
2019 Motor neuron diseases caused by a novel VRK1 variant - A genotype/phenotype study. Annals of clinical and translational neurology 18 31560180
2021 VRK1 Depletion Facilitates the Synthetic Lethality of Temozolomide and Olaparib in Glioblastoma Cells. Frontiers in cell and developmental biology 16 34195200
2020 Downregulation of VRK1 reduces the expression of BANF1 and suppresses the proliferative and migratory activity of esophageal cancer cells. Oncology letters 15 32724356
2019 Novel VRK1 Mutations in a Patient with Childhood-onset Motor Neuron Disease. Internal medicine (Tokyo, Japan) 15 31178479
2009 Protein kinase VRK-1 regulates cell invasion and EGL-17/FGF signaling in Caenorhabditis elegans. Developmental biology 15 19679119
2020 Identification of a homozygous VRK1 mutation in two patients with adult-onset distal hereditary motor neuropathy. Muscle & nerve 14 31837156
2020 VRK1 (Y213H) homozygous mutant impairs Cajal bodies in a hereditary case of distal motor neuropathy. Annals of clinical and translational neurology 14 32365420
2018 Vrk1 partial Knockdown in Mice Results in Reduced Brain Weight and Mild Motor Dysfunction, and Indicates Neuronal VRK1 Target Pathways. Scientific reports 14 30050127
2022 Ankle2 deficiency-associated microcephaly and spermatogenesis defects in zebrafish are alleviated by heterozygous deletion of vrk1. Biochemical and biophysical research communications 13 35940133
2017 Comparative Interactomes of VRK1 and VRK3 with Their Distinct Roles in the Cell Cycle of Liver Cancer. Molecules and cells 13 28927264
2023 The pattern of histone H3 epigenetic posttranslational modifications is regulated by the VRK1 chromatin kinase. Epigenetics & chromatin 12 37179361
2022 The VRK1 chromatin kinase regulates the acetyltransferase activity of Tip60/KAT5 by sequential phosphorylations in response to DNA damage. Biochimica et biophysica acta. Gene regulatory mechanisms 12 36280132
2016 Oncogenic Sox2 regulates and cooperates with VRK1 in cell cycle progression and differentiation. Scientific reports 12 27334688
2023 VRK1 Kinase Activity Modulating Histone H4K16 Acetylation Inhibited by SIRT2 and VRK-IN-1. International journal of molecular sciences 11 36902348
2023 VRK1 variants at the cross road of Cajal body neuropathogenic mechanisms in distal neuropathies and motor neuron diseases. Neurobiology of disease 11 37257665
2021 Adult-Onset Spinal Muscular Atrophy due to Mutations in the VRK1 Gene. Neurology. Genetics 11 34169149
2020 VRK1 variants in two Portuguese unrelated patients with childhood-onset motor neuron disease. Amyotrophic lateral sclerosis & frontotemporal degeneration 11 32242460
2022 Dissecting the roles of Haspin and VRK1 in histone H3 phosphorylation during mitosis. Scientific reports 10 35778595
2022 Distal spinal muscular atrophy featured by predominant calf muscle involvement in VRK1 associated disease - Case series and review. Neuromuscular disorders : NMD 9 35641352
2021 Dysfunctional Homozygous VRK1-D263G Variant Impairs the Assembly of Cajal Bodies and DNA Damage Response in Hereditary Spastic Paraplegia. Neurology. Genetics 9 34504951
2025 Histone Lactylation-Driven Upregulation of VRK1 Expression Promotes Stemness and Proliferation of Glioma Stem Cells. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 7 40990975
2021 The Vaccinia Virus B12 Pseudokinase Represses Viral Replication via Interaction with the Cellular Kinase VRK1 and Activation of the Antiviral Effector BAF. Journal of virology 7 33177193
2021 VRK1 promotes proliferation, migration, and invasion of gastric carcinoma cells by activating β-catenin. Neoplasma 7 34374295
2024 ALS-associated VRK1 R321C mutation causes proteostatic imbalance and mitochondrial defects in iPSC-derived motor neurons. Neurobiology of disease 6 38806131
2016 Expression of vaccinia-related kinase 1 (VRK1) accelerates cell proliferation but overcomes cell adhesion mediated drug resistance (CAM-DR) in multiple myeloma. Hematology (Amsterdam, Netherlands) 6 27319807
2023 Behavioral and neurological effects of Vrk1 deficiency in zebrafish. Biochemical and biophysical research communications 5 37429068
2023 Downregulation of VRK1 Inhibits Progression of Lung Squamous Cell Carcinoma through DNA Damage. Canadian respiratory journal 5 37547297
2024 Loss of VRK1 alters the nuclear phosphoproteome in the DNA damage response to doxorubicin. Chemico-biological interactions 4 38367682
2024 VRK1 promotes DNA-induced type I interferon production. Molecular biology reports 4 38536553
2022 Inhibition of VRK1 suppresses proliferation and migration of vascular smooth muscle cells and intima hyperplasia after injury via mTORC1/β-catenin axis. BMB reports 4 35410639
2022 Dysregulation of Cellular VRK1, BAF, and Innate Immune Signaling by the Vaccinia Virus B12 Pseudokinase. Journal of virology 4 35543552
2024 VRK1 Regulates Sensitivity to Oxidative Stress by Altering Histone Epigenetic Modifications and the Nuclear Phosphoproteome in Tumor Cells. International journal of molecular sciences 3 38732093
2019 Ras-PI3K pathway promotes osteosarcoma progression via regulating VRK1-mediated H2A phosphorylation at threonine 120. Artificial cells, nanomedicine, and biotechnology 3 31810390
2025 Lentinan suppresses the progression of neuroblastoma by inhibiting FOS-mediated transcription activation of VRK1 to stabilize p53 protein. Cell death discovery 2 40089488
2025 VRK1 promotes epithelial-mesenchymal transition in hepatocellular carcinoma mediated by SNAI1 via phosphorylating CHD1L. Cell death & disease 2 40234378
2025 VRK1/BANF1/GLI1 Axis Regulates Tumor Development and Progression of Colorectal Cancer. International journal of biological sciences 2 40384864
2024 Pathogenic effects of Leu200Pro and Arg387His VRK1 protein variants on phosphorylation targets and H4K16 acetylation in distal hereditary motor neuropathy. Journal of molecular medicine (Berlin, Germany) 2 38554151
2024 Nuclear functions regulated by the VRK1 kinase. Nucleus (Austin, Tex.) 2 38753965
2024 CMT2 and distal hereditary motor neuropathy associated with VRK1 variants: Case series. Neuromuscular disorders : NMD 2 39693713
2024 Inactivation of VRK1 sensitizes ovarian cancer to PARP inhibition through regulating DNA-PK stability. Experimental cell research 1 38614421
2023 Circ VRK1/microRNA-17/PTEN axis modulates the angiogenesis of human brain microvascular endothelial cells to affect injury induced by oxygen-glucose deprivation/reperfusion. BMC neuroscience 1 36707796
2025 VRK1 Is a Novel Therapeutic Target for Small Cell Neuroendocrine Carcinoma of the Cervix. Cancer science 0 41111449

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