Anti-DYRK3 antibody

Target data

Dual-specificity protein kinase that promotes disassembly of several types of membraneless organelles during mitosis, such as stress granules, nuclear speckles and pericentriolar material (PubMed : 29973724). Dual-specificity tyrosine-regulated kinases (DYRKs) autophosphorylate a critical tyrosine residue in their activation loop and phosphorylate their substrate on serine and threonine residues (PubMed : 29634919, PubMed : 9748265). Acts as a central dissolvase of membraneless organelles during the G2-to-M transition, after the nuclear-envelope breakdown : acts by mediating phosphorylation of multiple serine and threonine residues in unstructured domains of proteins, such as SRRM1 and PCM1 (PubMed : 29973724). Does not mediate disassembly of all membraneless organelles : disassembly of P-body and nucleolus is not regulated by DYRK3 (PubMed : 29973724). Dissolution of membraneless organelles at the onset of mitosis is also required to release mitotic regulators, such as ZNF207, from liquid-unmixed organelles where they are sequestered and keep them dissolved during mitosis (PubMed : 29973724). Regulates mTORC1 by mediating the dissolution of stress granules : during stressful conditions, DYRK3 partitions from the cytosol to the stress granule, together with mTORC1 components, which prevents mTORC1 signaling (PubMed : 23415227). When stress signals are gone, the kinase activity of DYRK3 is required for the dissolution of stress granule and mTORC1 relocation to the cytosol : acts by mediating the phosphorylation of the mTORC1 inhibitor AKT1S1, allowing full reactivation of mTORC1 signaling (PubMed : 23415227). Also acts as a negative regulator of EPO-dependent erythropoiesis : may place an upper limit on red cell production during stress erythropoiesis (PubMed : 10779429). Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells (PubMed : 10779429). Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1 : this in turn inhibits p53/TP53 activity and apoptosis (PubMed : 20167603).