ArticleThe Biochemical journal2003
dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated kinase in Drosophila.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 45 citations in OpenAlex.
- Phosphoproteomics identifies the DYRK1B protein kinase as a regulator of processing bodies.Journal of cell science · 2026Article
- Proteomic Snapshots of Structural Cross-Linking Rearrangements in CaJournal of proteome research · 2026Article
- Insights from the protein interaction Universe of the multifunctional "Goldilocks" kinase DYRK1A.Frontiers in cell and developmental biology · 2023Review
- Two adjacent phosphorylation sites in the C-terminus of the channel's α-subunit have opposing effects on epithelial sodium channel (ENaC) activity.Pflugers Archiv : European journal of physiology · 2022Article
- Updating dual-specificity tyrosine-phosphorylation-regulated kinase 2 (DYRK2): molecular basis, functions and role in diseases.Cellular and molecular life sciences : CMLS · 2020Review
- RNA Recognition-like Motifs Activate a Mitogen-Activated Protein Kinase.Biochemistry · 2018Article
- Dynamic transcriptomic analysis of Ischemic Injury in a Porcine Pre-Clinical Model mimicking Donors Deceased after Circulatory Death.Scientific reports · 2018Article
- Selective inhibition of the kinase DYRK1A by targeting its folding process.Nature communications · 2016Article
- Identification of DYRK1B as a substrate of ERK1/2 and characterisation of the kinase activity of DYRK1B mutants from cancer and metabolic syndrome.Cellular and molecular life sciences : CMLS · 2016Article
- Genome-wide screen for modifiers of Na (+) /K (+) ATPase alleles identifies critical genetic loci.Molecular brain · 2014Article
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- Transcriptome profiling of sexual maturation and mating in the Mediterranean fruit fly, Ceratitis capitata.PloS one · 2012Article
- Deep evolutionary conservation of an intramolecular protein kinase activation mechanism.PloS one · 2012Article
- Splice variants of the dual specificity tyrosine phosphorylation-regulated kinase 4 (DYRK4) differ in their subcellular localization and catalytic activity.The Journal of biological chemistry · 2011Article
- Direct association of Sprouty-related protein with an EVH1 domain (SPRED) 1 or SPRED2 with DYRK1A modifies substrate/kinase interactions.The Journal of biological chemistry · 2010Article
- The phosphoproteome of bloodstream form Trypanosoma brucei, causative agent of African sleeping sickness.Molecular & cellular proteomics : MCP · 2009Article
- DYRK1A autophosphorylation on serine residue 520 modulates its kinase activity via 14-3-3 binding.Molecular biology of the cell · 2007Article
- dDYRK2 and Minibrain interact with the chromatin remodelling factors SNR1 and TRX.The Biochemical journal · 2006Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
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Abstract
Dual-specificity tyrosine-phosphorylation-regulated kinases (DYRKs) are an emerging family of protein kinases that have been identified in all eukaryotic organisms examined to date. DYRK family members are involved in regulating key developmental and cellular processes such as neurogenesis, cell proliferation, cytokinesis and cellular differentiation. Two distinct subgroups exist, nuclear and cytosolic. In Drosophila, the founding family member minibrain, whose human orthologue maps to the Down syndrome critical region, belongs to the nuclear subclass and affects post-embryonic neurogenesis. In the present paper, we report the isolation of dDYRK2, a cytosolic DYRK and the putative product of the smell-impaired smi35A gene. This is the second such kinase described in Drosophila, but the first to be characterized at the molecular and biochemical level. dDYRK2 is an 81 kDa dual-specificity kinase that autophosphorylates on tyrosine and serine/threonine residues, but appears to phosphorylate exogenous substrates only on serine/threonine residues. It contains a YXY motif in the activation loop of the kinase domain in the same location as the TXY motif in mitogen-activated protein kinases. dDYRK2 is tyrosine-phosphorylated in vivo, and mutational analysis reveals that the activation loop tyrosines are phosphorylated and are essential for kinase activity. Finally, dDYRK2 is active at all stages of fly development, with elevated levels observed during embryogenesis and pupation.
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