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DCAF7/WDR68 is required for normal levels of DYRK1A and DYRK1B
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DYRK1B mutations associated with metabolic syndrome interfere with the maturation of DYRK1B by tyrosine autophosphorylation and compromise the conformational stability of the catalytic domain, which renders the kinase susceptible to misfolding.
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Through the activation of DYRK1B, Hedgehog signaling facilitates microtubule-dependent processes such as intracellular mitochondrial transport, mesenchymal cell polarization or directed cell migration.
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Dyrk1B was overexpressed in breast cancer tissues and cells and correlates with FoxO1 phosphorylation and cell proliferation.
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High DYRK1B expression is associated with pancreatic and skin cancers.
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The study shows that DYRK1B is a novel ERK2 substrate, uncovering new links between two kinases involved in cell fate decisions.
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Data reveal a novel role for miR-9 in regulation of the NFAT pathway by targeting KPNB1 and DYRK1B.
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NKX3.1 and DYRK1B were shown to interact via the DYRK1B kinase domain. In vitro kinase assay showed that DYRK1B phosphorylated NKX3.1 at serine 185, a residue critical for NKX3.1 steady-state turnover.
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Upregulation of Mirk mRNA expression is mediated by CREB binding to two sites in the Mirk promoter upstream of the transcription start site and one site within exon 4.
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A founder mutation was identified in DYRK1B, substituting cysteine for arginine at position 102 in 3 families with metabolic syndrome.
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DYRK1B is a novel Thr(286)-CCND1 kinase that acts independently of GSK3beta to promote CCND1 degradation.
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Mirk/Dyrk1B plays an important role in ovarian cancer cell survival through modulating FoxO translocation.
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In line with a redirection of autocrine toward paracrine HH signaling by a KRAS-DYRK1B network, we find high levels of GLI1 expression restricted to the stromal compartment and not to SHH-expressing tumor cells in pancreatic adenocarcinoma.
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the kinase Mirk is essential for the growth and survival of osteosarcoma cells.
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activation by MKK2 and role as transcriptional activator of HNF1alpha
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p38 MAP Kinase suppresses the function of Mirk as a transcriptional activator only when cells are proliferating
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Mirk is anti-apoptotic in myoblasts
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Mirk is a survival factor for pancreatic ductal adenocarcinoma. Because knockout of Mirk does not cause embryonic lethality, Mirk is not essential for normal cell growth.
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This review summarizes the known regulators and functions of Mirk kinase and outlines opportunities for future studies of Mirk in the fields of muscle and tumor biology.
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GSK-3beta but also DYRK1B modulates cyclin D1 subcellular localization by the phosphorylation of Thr(288). These results suggest that DIF-3 induces degradation of cyclin D1 through the GSK-3beta- and DYRK1B-mediated threonine phosphorylation in HeLa cells
