| 1999 |
DYRK1B (MIRK) is a nuclear-localized serine/threonine kinase predominantly expressed in muscle and testis; a GFP fusion protein localizes mainly to the nucleus of transfected COS-7 cells, consistent with a bipartite nuclear localization motif in its sequence. |
GFP fusion protein transfection and fluorescence microscopy; sequence analysis |
Biochemical and biophysical research communications |
Medium |
9918863
|
| 2000 |
DYRK1B (MIRK) is a downstream substrate of the MAPK pathway; activated ERKs down-regulate MIRK protein levels in vivo, and blocking MEK with PD98059 increases MIRK levels ~20-fold in colon carcinoma cells. Kinase-active MIRK (but not kinase-dead mutant) enables colon carcinoma cells to survive in serum-free medium. |
MEK inhibitor treatment, stable overexpression of wild-type vs. kinase-dead MIRK, serum-free growth assays |
Cancer research |
Medium |
10910078
|
| 2002 |
DYRK1B (MIRK) functions as a transcriptional co-activator of HNF1α by binding DCoHm (a dimerization cofactor of HNF1α), forming a MIRK–DCoHm–HNF1α complex; MIRK directly phosphorylates HNF1α at Ser249 within its CBP-binding domain. MKK3, an upstream stress-activated kinase, co-immunoprecipitates with MIRK and enhances its kinase activity and HNF1α transactivation. |
Yeast two-hybrid, GST pulldown, co-immunoprecipitation, in vitro kinase assay, reporter assays with kinase-dead mutants |
The Journal of biological chemistry |
High |
11980910
|
| 2002 |
p38α and p38β (but not γ or δ) isoforms sequester DYRK1B (MIRK) in nuclear subnuclear complexes (~500–700 kDa) in a kinase-independent manner, preventing MIRK association with MKK3 and inhibiting its function as a transcriptional activator of HNF1α. |
Co-immunoprecipitation, size-exclusion FPLC fractionation, reporter assays, dominant-negative p38 constructs |
The Journal of biological chemistry |
High |
12384504
|
| 2003 |
DYRK1B (MIRK) is induced by Rho-family GTPases (RhoA, Cdc42, and to a lesser extent Rac1) during skeletal muscle differentiation, and is required for myoblast fusion and induction of differentiation markers (myogenin, troponin T, myosin heavy chain); depletion by siRNA blocks these events. |
Promoter-reporter assays, transient expression of constitutively active GTPases, siRNA knockdown with differentiation marker readouts |
The Journal of biological chemistry |
High |
12902328
|
| 2003 |
DYRK1B (MIRK) was identified as a binding partner of the Met adaptor protein RanBPM by yeast two-hybrid, confirmed by GST pulldown, Co-IP, and in vivo cross-linking; RanBPM inhibits MIRK kinase activity. Induction of MIRK inhibits cell migration and invasion, an effect attenuated by HGF or overexpressed RanBPM. |
Yeast two-hybrid, GST pulldown, Co-IP, in vivo cross-linking, stable inducible MIRK cell line, wounding and Transwell migration assays |
The Journal of biological chemistry |
High |
14500717
|
| 2003 |
Stable overexpression of DYRK1B (MIRK) enhances proteasome-dependent turnover of p27Kip1, cyclin D1, and p21Cip1 at the protein level without affecting p27 mRNA or promoter activity, indicating post-transcriptional regulation. |
Stable transfectants (wild-type vs. kinase-dead), proteasome inhibitor experiments, mRNA and promoter assays |
International journal of cancer |
Medium |
12455049
|
| 2004 |
DYRK1B (MIRK) directly phosphorylates p27Kip1 at Ser10 in G0, stabilizing p27 and maintaining G0 arrest; phosphomimetic p27-S10D is more stable than wild-type, and non-phosphorylatable p27-S10A is less stable. MIRK co-localizes with nuclear p27 in G0 and does not induce p27 nuclear export. Depletion of MIRK by RNAi decreases p27 phosphorylation at Ser10 and increases G0→G1 entry. |
In vitro kinase assay, phosphomimetic/non-phosphorylatable mutants, RNAi knockdown, PCNA and p27 protein/stability assays, co-localization |
The Journal of biological chemistry |
High |
15010468
|
| 2004 |
DYRK1B (MIRK) binds cyclin D1 and phosphorylates it at Thr288 (in vivo and in vitro), promoting cyclin D1 destabilization; cyclin D1-T288A is more stable than wild-type. MIRK and GSK3β phosphorylate cyclin D1 additively at distinct sites. RNAi depletion of MIRK increases cyclin D1 protein without affecting mRNA. |
Co-immunoprecipitation, in vitro kinase assay, stable inducible MIRK transfectants, cyclin D1-T288A mutant, RNAi knockdown, GSK3β inhibitor LiCl |
The Journal of biological chemistry |
High |
15075324
|
| 2004 |
DYRK1B (MIRK) phosphorylates class II HDACs (HDAC5, MITR) at a conserved site within their nuclear localization region, reducing their nuclear accumulation in a dose- and kinase-dependent manner, thereby enabling MEF2C to activate the myogenin promoter during muscle differentiation. MIRK does not directly phosphorylate MEF2; the effect is indirect via HDAC phosphorylation. |
Co-expression studies, kinase-dead mutants, phosphomimetic MITR construct, reporter assays, subcellular localization of GFP-HDAC fusions, siRNA knockdown |
The Journal of biological chemistry |
High |
15546868
|
| 2005 |
DYRK1B (MIRK) phosphorylates p21Cip1 at Ser153 within its nuclear localization domain, causing a fraction of nuclear p21 to relocalize to the cytoplasm; cytoplasmic p21 blocks caspase 3 activation and promotes myoblast survival. Phosphomimetic p21-S153D localizes pan-cellularly and is more effective than wild-type at blocking caspase 3; non-phosphorylatable p21-S153A remains nuclear and has no survival effect. |
Overexpression and RNAi, GFP-p21 localization (fluorescence microscopy), phosphomimetic/non-phosphorylatable mutants, caspase 3 activation assays, colony-forming assays |
The Journal of biological chemistry |
High |
15851482
|
| 2005 |
DYRK1B (MIRK) is activated by signaling from Rac1 to MKK3; constitutively active Rac1QL activates MIRK through MKK3, which phosphorylates MIRK. Dominant-negative Rac1, dominant-negative MKK3, and MKK3 siRNA inhibit MIRK kinase activity. Endogenous Rac1 activates MIRK following E-cadherin ligation in confluent MDCK cells. |
Kinase activity assays, dominant-negative constructs, RNAi knockdown of MKK3, E-cadherin/Fc chimera engagement, Rac1 inhibitor treatment |
The Journal of biological chemistry |
High |
16257974
|
| 2007 |
DYRK1B (MIRK) is a novel downstream effector of oncogenic K-RAS in pancreatic cancer; K-RAS activates MIRK through Rac1→MKK3 signaling. Knockdown of K-RAS by three independent RNAi sequences, or of Rac1 by two independent RNAi sequences, or pharmacological Rac1 inhibition, or dominant-negative K-rasS17N all blocked MIRK activation. |
Reporter assays, RNAi knockdown (K-RAS, Rac1), dominant-negative K-ras, Rac1 inhibitor, kinase activity assays |
Cancer research |
High |
17671193
|
| 2008 |
BCL2 and BCL-xL stabilize p27 in G0 via MIRK-mediated phosphorylation of p27 at Ser10; this G0 function requires BAX and BAK, as the effect is lost in bax−/−bak−/− cells. Re-expression of BAX in double-knockout cells restores Ser10-p27 phosphorylation, demonstrating that BAX/BAK modulate MIRK-dependent p27 stabilization. |
Genetic knockout cells (bax−/−bak−/−), BAX re-expression, phospho-specific p27 Ser10 immunoblotting, cell cycle analysis |
The Journal of biological chemistry |
Medium |
18818203
|
| 2009 |
DYRK1B (MIRK) maintains viability of quiescent pancreatic cancer cells by increasing transcription of antioxidant genes (ferroxidase, SOD2, SOD3), thereby reducing intracellular ROS levels. Depletion of MIRK via inducible shRNA increases ROS, decreases colony-forming ability, and reduces viability; ectopic expression of SOD2 and ferroxidase rescues ROS levels in MIRK-depleted cells. |
Inducible shRNA knockdown, ROS measurement, antioxidant gene expression analysis, ectopic expression rescue, colony-forming assays, dye exclusion viability |
Cancer research |
High |
19351855
|
| 2010 |
Mutant RAS activates DYRK1B as part of a KRAS–DYRK1B network that mediates cell-autonomous negative regulation (antagonism) of autocrine Hedgehog (HH) signaling, interfering with Gli2 function and Gli3 processing, while simultaneously redirecting HH signaling toward a paracrine mode in pancreatic cancer. |
Genetic and cell biological studies in mutant RAS-expressing cells; RAS effector pathway analysis; Gli2/Gli3 processing assays |
Nature structural & molecular biology |
Medium |
20512148
|
| 2010 |
DYRK1B (MIRK) regulates colon cancer cell exit from quiescence by destabilizing cyclin D1 and cyclin D3, reducing CDK4/cyclin D activity and p130/Rb2 phosphorylation, thereby maintaining the quiescent state. Depletion of MIRK increases cyclin D1/D3 protein via slower turnover and allows cells to escape G0. Cyclin D1-T288A (Mirk phosphorylation site mutant), but not wild-type cyclin D1, shortens 5-FU-induced G1, confirming site-specific mechanism. |
RNAi knockdown, cyclin D1-T288A mutant expression, CDK4 activity assays, p130 phosphorylation, Hoechst/Pyronin Y G0 staining |
The Journal of biological chemistry |
High |
19542220
|
| 2012 |
Cold-inducible RNA-binding protein CIRP directly binds DYRK1B/MIRK and inhibits its interaction with p27, resulting in decreased phosphorylation and destabilization of p27. CIRP does not affect DYRK1B binding to cyclin D1 but inhibits DYRK1B-mediated phosphorylation of cyclin D1, leading to cyclin D1 stabilization. CIRP and DYRK1B co-localize in the nucleus of undifferentiated spermatogonia. |
Co-immunoprecipitation (direct CIRP–DYRK1B binding), siRNA knockdown, protein stability assays, G0 fraction analysis, immunofluorescence co-localization in spermatogonia |
Proceedings of the National Academy of Sciences of the United States of America |
High |
22711815
|
| 2014 |
DYRK1B inhibits SHH and Wnt signaling pathways and enhances adipogenesis; the disease-associated R102C allele shows gain-of-function activity, potentiating these effects. DYRK1B also promotes expression of glucose-6-phosphatase (a key gluconeogenic enzyme). |
Functional characterization in patient-derived cell lines and model systems; pathway reporter assays; gene expression analysis; R102C gain-of-function mutant characterization |
The New England journal of medicine |
Medium |
24827035
|
| 2014 |
Using the selective DYRK1B inhibitor AZ191, it was demonstrated that DYRK1B phosphorylates cyclin D1 at Thr286 (not Thr288 as previously reported) in vitro and in cells, and this is independent of GSK3β. In PANC-1 and HEK293 cells, DYRK1B drives Thr286 phosphorylation and proteasome-dependent cyclin D1 turnover; AZ191 or DYRK1B RNAi abolishes this, while GSK3β inhibitors or GSK3β RNAi do not. DYRK1B also promotes p21CIP1 and p27KIP1 expression. |
In vitro kinase assay, phospho-specific immunoblot, mass spectrometry, selective small-molecule inhibitor (AZ191), DYRK1B RNAi, GSK3β RNAi and inhibitors |
The Biochemical journal |
High |
24134204
|
| 2014 |
DYRK1B (MIRK) is upregulated several-fold by mTOR inhibitors (RAD001, WYE354, rapamycin) via CREB-mediated transcription; CREB binds two sites in the MIRK promoter and one site in exon 4. Depletion of CREB reduces MIRK expression; depletion of mTOR increases it. Activated Akt–ER construct blocks the mTOR-inhibitor-induced increase in MIRK mRNA. |
mTOR inhibitor treatment, CREB ChIP/reporter assays, siRNA knockdown of CREB and mTOR, inducible Akt-ER construct |
Carcinogenesis |
Medium |
24590896
|
| 2014 |
DYRK1B (MIRK) in differentiated skeletal muscle (fast-twitch fibers) and cycling myoblasts reduces ROS by maintaining expression of antioxidant genes; pharmacological MIRK kinase inhibition or depletion increases ROS in both C2C12 myoblasts and differentiated myotubes. MIRK protein translocates from nucleus (cycling myoblasts) to cytoplasm (differentiating myoblasts and mature fast-twitch fibers). |
MIRK kinase inhibitor treatment, inducible shRNA, ROS measurement, immunofluorescence and cell fractionation for localization, antioxidant gene expression |
Genes & cancer |
Medium |
24955215
|
| 2015 |
DYRK1B is a substrate of ERK2: ERK2 phosphorylates DYRK1B at Ser421 in vitro; selective ERK1/2 pathway activation increases p-S421 in cells. DYRK1B also trans-autophosphorylates at S421 in vitro and in cells. A catalytically inactive DYRK1B(D239A) mutant has very low p-S421 in cells, increased by KRAS(G12V). S421 phosphorylation contributes to DYRK1B kinase activity. DYRK1B is activated by cis-autophosphorylation on Y273 during translation. |
In vitro kinase assay with recombinant ERK2, phospho-specific immunoblot, selective MEK inhibitors, pathway-selective activation constructs, kinase-dead DYRK1B mutants, KRAS(G12V) expression |
Cellular and molecular life sciences : CMLS |
High |
26346493
|
| 2015 |
DYRK1B interacts with the tumor suppressor NKX3.1 via the DYRK1B kinase domain and phosphorylates NKX3.1 at Ser185 in vitro, promoting NKX3.1 degradation; this residue is critical for NKX3.1 steady-state turnover. Small-molecule DYRK1B inhibitors prolonged NKX3.1 half-life. |
siRNA kinase screen, Co-IP (kinase domain interaction), in vitro kinase assay, phospho-specific site (S185) mutagenesis, protein stability/half-life assays, small-molecule inhibitors |
Molecular cancer research : MCR |
High |
25777618
|
| 2017 |
DYRK1B mediates Hedgehog (Hh)-induced mTOR/AKT activation: Hh signaling induces DYRK1B protein expression in fibroblasts, which then activates the mTOR/AKT kinase signaling arm. DYRK1B exerts negative feedback on canonical SMO-mediated Hh/GLI signaling while providing positive feed-forward regulation by promoting AKT-mediated GLI stability. |
Genetic and pharmacological inhibition of DYRK1B, Hh pathway stimulation, AKT/mTOR phosphorylation readouts, GLI1 expression assays |
Oncotarget |
Medium |
27903983
|
| 2017 |
DYRK1B missense mutations (H90P and R102C) affecting the DYRK homology (DH) box do not alter the specific catalytic activity of mature DYRK1B but cause accumulation of the mutant protein in detergent-insoluble cytoplasmic aggregates in an underphosphorylated (on tyrosine) form. Mutant DYRK1B shows enhanced binding to co-chaperone CDC37 and greater sensitivity to the HSP90 inhibitor ganetespib, indicating impaired chaperone-dependent maturation. |
Cellular kinase activity assays, detergent fractionation, phospho-tyrosine immunoblotting, HSP90 inhibitor sensitivity, Co-IP with CDC37 |
Scientific reports |
Medium |
28743892
|
| 2018 |
DYRK1B mediates Hedgehog-induced microtubule (MT) acetylation by inhibiting GSK3β through phosphorylation of GSK3β Serine 9, which suppresses HDAC6 activity (a major tubulin deacetylase), resulting in increased acetylated MTs. This DYRK1B-dependent MT acetylation facilitates mitochondrial transport, mesenchymal cell polarization, and directed cell migration. |
Hh pathway stimulation, DYRK1B knockdown/inhibition, GSK3β S9 phospho-specific immunoblot, HDAC6 activity assay, MT acetylation assays, mitochondrial transport and migration assays |
Cellular and molecular life sciences : CMLS |
Medium |
30317528
|
| 2018 |
WDR68 (DCAF7) is required for normal protein levels of DYRK1B (and DYRK1A); WDR68 knockout in C2C12 and HeLa cells reduces DYRK1B protein levels without affecting mRNA, and proteasome inhibition does not restore DYRK1B, suggesting WDR68 is required for proper kinase stabilization/maturation rather than preventing proteasomal degradation. |
Engineered knockout cell lines, Western blotting, RT-PCR, proteasome inhibitor treatment, WDR68 overexpression |
PloS one |
Medium |
30496304
|
| 2020 |
DYRK1B is recruited to laser-microirradiated DNA double-strand break (DSB) sites, and its kinase activity is required for DSB-induced transcriptional silencing on active chromatin and for efficient DNA repair. DYRK1B phosphorylates the histone methyltransferase EHMT2, enforcing its DSB accumulation, establishing a DYRK1B–EHMT2 axis. Genetic inactivation of DYRK1B or its kinase activity attenuates DSB-induced gene silencing and impairs DNA repair. |
Kinome-wide chemical screen, laser micro-irradiation, live-cell imaging of DYRK1B recruitment, genetic inactivation (knockout/kinase-dead), global transcription shutdown rescue, EHMT2 phosphorylation assays |
Proceedings of the National Academy of Sciences of the United States of America |
High |
32611815
|
| 2021 |
DYRK1B is required for full suppression of rDNA (ribosomal DNA) transcription following DSBs, exhibiting robust nucleolar accumulation after laser micro-irradiation. DYRK1B inactivation leads to sustained nucleolar transcription after DSBs, impaired rDNA DSB repair, and reduced rDNA copy number maintenance. This nucleolar DSB response can be uncoupled from ATM-mediated DSB signaling. |
Targeted rDNA DSBs, laser micro-irradiation, chemical inhibition and genetic inactivation of DYRK1B, rRNA synthesis assays, rDNA copy number analysis, cell sensitivity assays |
Nucleic acids research |
High |
33469661
|
| 2022 |
DYRK1B promotes hepatic lipogenesis by activating mTORC2 in a kinase-independent fashion. Dyrk1b overexpression in mouse liver enhanced de novo lipogenesis, fatty acid uptake, triacylglycerol secretion, and caused NASH; the Dyrk1b-induced NASH was fully rescued when mTORC2 was genetically disrupted. The resulting elevated diacylglycerol activated PKCε and led to IRKT1150 phosphorylation, impairing hepatic insulin signaling. |
Liver-specific AAV-mediated overexpression, genetic mTORC2 disruption (rescue experiment), Dyrk1b knockdown, lipogenesis assays, PKCε and IR phosphorylation assays, in vivo mouse models |
The Journal of clinical investigation |
High |
34855620
|
| 2022 |
DYRK1B directly binds STAT3 and increases its phosphorylation and nuclear accumulation, contributing to downregulation of PGC-1α and impaired mitochondrial bioenergetics in cardiac hypertrophy and heart failure. Cardiac-specific DYRK1B overexpression causes cardiac dysfunction; DYRK1B knockout mitigates TAC-induced cardiac hypertrophy and heart failure. |
Transgenic and knockout mice (TAC model), Co-IP (DYRK1B–STAT3 binding), STAT3 phosphorylation and nuclear accumulation assays, PGC-1α expression, mitochondrial functional analysis, specific inhibitors |
Circulation |
High |
35235343
|
| 2022 |
DYRK1B maturation requires the CMGC insert and adjacent sequences; human DYRK1B autophosphorylation is severely compromised in bacterial cell-free systems (unlike DYRK1A or zebrafish/Xenopus DYRK1B orthologs), and the differential folding is largely due to divergent C-terminal lobe sequences. DYRK1B's mature kinase domain has lower thermal stability than DYRK1A. |
Bacterial expression systems (cell-free), autophosphorylation assays, thermal stability assays, domain comparison across species, heat challenge in vitro and in cells |
Scientific reports |
Medium |
35165364
|
| 2023 |
DYRK1B phosphorylates FOXO1 at Ser329 to regulate its cytoplasmic/nuclear localization; DYRK1B inhibition enhances nuclear FOXO1 retention (by blocking Ser329 phosphorylation), promoting Treg differentiation and suppressing Th1/Th17 differentiation in CD4+ T cells. |
DYRK1B inhibitor treatment, FOXO1 phospho-specific assays (Ser329), T cell differentiation assays (FACS), Treg/Th1/Th17 marker analysis, murine CHS model |
Scientific reports |
Medium |
37120440
|
| 2024 |
DYRK1B downregulates the phagocytosis checkpoint 'don't eat me' signal CD24 on pancreatic cancer cells; genetic ablation or pharmacological inhibition of DYRK1B strongly attracts tumoricidal macrophages and enhances tumor cell phagocytosis. Tumor cells lacking DYRK1B barely expand in vivo despite growing rapidly in culture. |
Transplantation and autochthonous mouse PDAC models, genetic Dyrk1b loss, pharmacological inhibition, co-culture experiments, CD24 surface expression analysis, phagocytosis assays, bulk mRNA sequencing and proteomics (secretomics) |
Gut |
High |
38834297
|
| 2024 |
DYRK1B is a novel substrate of and negative feedback regulator on the transcription factor RFX7: DYRK1B is induced by cytostatic drugs (Actinomycin D, Doxorubicin) via p53-dependent activation of RFX7; DYRK1B physically interacts with RFX7 and counteracts its p53-mediated activation in a catalytic-activity-dependent manner, establishing a negative feedback loop. |
Drug treatment in multiple cancer cell lines, p53-dependent induction assays, Co-IP (DYRK1B–RFX7 interaction), kinase-dead DYRK1B mutants, DYRK1 small-molecule inhibitors |
Cell death & disease |
Medium |
41888523
|
| 2025 |
DYRK1B promotes hepatic gluconeogenesis and glucose intolerance by interacting with and phosphorylating FOXO1 primarily at Thr467/Ser468, which is essential for FOXO1 nuclear localization; additionally, DYRK1B inhibits AKT-mediated FOXO1 phosphorylation at Thr24 and Ser256, enhancing FOXO1 nuclear retention and gluconeogenic gene expression. Liver-specific Dyrk1b conditional knockout mice are protected from diet-induced hyperglycemia. |
In vivo/in vitro kinase assays, liver-specific Dyrk1b cKO mice, Co-IP (DYRK1B–FOXO1), phospho-specific immunoblotting at FOXO1 sites, gluconeogenesis gene expression assays, AZ191 pharmacological inhibitor |
Nucleic acids research |
High |
40287828
|
| 2025 |
The CMGC insert sequence and two adjacent proline residues (P332/P333 in DYRK1B) are critical for DYRK1B tyrosine autophosphorylation and maturation; mutation of either proline impairs autophosphorylation and nuclear localization. Substitution of the DYRK1B CMGC insert with that of DYRK1A rescues the maturation defect. The pathogenic R349W mutation associated with monogenic obesity/type 2 diabetes also disrupts autophosphorylation. |
Domain swaps, point mutations, autophosphorylation assays, nuclear localization studies, X-ray crystallography structural context |
Scientific reports |
High |
41444824
|
| 2025 |
DYRK1B crystal structure was solved in complex with the inhibitor AZ191, revealing features in the hinge-binding region and differential accessibility of the catalytic lysine compared to DYRK1A that are pivotal for kinase selectivity. |
X-ray crystallography, quantum-mechanical and molecular-dynamics analyses, enzyme inhibition assays, cellular target engagement |
International journal of biological macromolecules |
High |
41061777
|
| 2025 |
DYRK1B inhibition reduces STAT3 phosphorylation in leukocytes, leading to decreased integrin activation, reduced leukocyte adhesion/migration, suppression of pro-inflammatory cytokines and eicosanoids, induction of apoptosis in neutrophils, and increased efferocytosis; this DYRK1B/STAT3 axis is identified as a regulator of inflammatory resolution. |
Small-molecule DYRK1B inhibitor (C81), STAT3 phosphorylation assays, leukocyte adhesion/migration assays, cytokine measurements, murine psoriasis and choroidal neovascularization models |
Cellular and molecular life sciences : CMLS |
Medium |
39985685
|
| 2024 |
DYRK1B promotes proteasomal degradation of WBP2 through enhanced WBP2 ubiquitylation (kinase-activity-dependent), thereby impairing hepatic insulin signaling; restoration of WBP2 partially rescues DYRK1B overexpression-induced glucose intolerance in vivo. |
Dyrk1b overexpression/knockout in mice, quantitative proteomics, ubiquitylation assays, WBP2 rescue experiments, kinase-dead mutant controls |
Heliyon |
Medium |
39296215
|
| 2021 |
DYRK1B upregulates 4E-BP1 (a translational inhibitor) in C2C12 myofibers as a post-transcriptional target; CRISPR/Cas9 knockout of Dyrk1b in zebrafish also identifies 4E-BP1 as a downstream target in vivo. 4E-BP1 enhances autophagy and mediates Dyrk1b's effects on skeletal muscle differentiation. The disease-associated Dyrk1bR102C mutation impairs muscle differentiation via excessive 4E-BP1/autophagy activation, rescued by reduction of autophagic flux. |
Untargeted proteomics (C2C12), CRISPR/Cas9 zebrafish knockout, siRNA knockdown and overexpression in C2C12, autophagy flux assays, rescue experiments |
Cellular signalling |
Medium |
34752933
|
| 2025 |
DYRK1B kinase inhibition by AZ191 reduces total small extracellular vesicle (EV) number and alters intracellular distribution of the EV marker CD63, suggesting DYRK1B plays a role in EV trafficking. DYRK1B knockdown confirms the EV reduction effect. |
High-throughput nanoscale flow cytometry, kinase inhibitor screen (AZ191), siRNA knockdown, CD63 intracellular distribution imaging |
Nanoscale |
Low |
40063071
|