Dual specificity tyrosine-phosphorylation-regulated kinase 1A

Definition:

Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Plays an important role in double-strand breaks (DSBs) repair following DNA damage. Mechanistically, phosphorylates RNF169 and increases its ability to block accumulation of TP53BP1 at the DSB sites thereby promoting homologous recombination repair (HRR). Also acts as a positive regulator of transcription by acting as a CTD kinase that mediates phosphorylation of the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A. May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Has pro-survival function and negatively regulates the apoptotic process (By similarity). Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1 (By similarity). This in turn inhibits p53/TP53 activity and apoptosis (By similarity). Phosphorylates SEPTIN4, SEPTIN5 and SF3B1 at 'Thr-434' (By similarity).

References:

[1]. Steven E Guard, et al. The nuclear interactome of DYRK1A reveals a functional role in DNA damage repair. Sci Rep. 2019 Apr 25;9(1):6539. [Content Brief]

[2]. Yasushi Ogawa, et al. Development of a novel selective inhibitor of the Down syndrome-related kinase Dyrk1A. Nat Commun. 2010 Oct 5;1:86. [Content Brief]

[3]. Huasong Lu, et al. Phase-separation mechanism for C-terminal hyperphosphorylation of RNA polymerase II. Nature. 2018 Jun;558(7709):318-323. [Content Brief]

[4]. Chiara Di Vona, et al. Chromatin-wide profiling of DYRK1A reveals a role as a gene-specific RNA polymerase II CTD kinase. Mol Cell. 2015 Feb 5;57(3):506-20. [Content Brief]

[5]. Vijay R Menon, et al. DYRK1A regulates the recruitment of 53BP1 to the sites of DNA damage in part through interaction with RNF169. Cell Cycle. 2019 Mar;18(5):531-551. [Content Brief]

[6]. Meera Soundararajan, et al. Structures of Down syndrome kinases, DYRKs, reveal mechanisms of kinase activation and substrate recognition. Structure. 2013 Jun 4;21(6):986-96. [Content Brief]

[7]. N Shindoh, et al. Cloning of a human homolog of the Drosophila minibrain/rat Dyrk gene from "the Down syndrome critical region" of chromosome 21. Biochem Biophys Res Commun. 1996 Aug 5;225(1):92-9. [Content Brief]

[8]. Yonglong Zou, et al. Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M. J Biol Chem. 2003 Dec 5;278(49):49573-81. [Content Brief]

[9]. Chrisovalantis Papadopoulos, et al. Splice variants of the dual specificity tyrosine phosphorylation-regulated kinase 4 (DYRK4) differ in their subcellular localization and catalytic activity. J Biol Chem. 2011 Feb 18;286(7):5494-505. [Content Brief]

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