DYRK1A

DYRK1A

A gene on chromosome 21q22.13 that encodes a member of the dual-specificity tyrosine-phosphorylation-regulated kinase (DYRK) family, which catalyses its autophosphorylation on serine/threonine and tyrosine residues. DYRK1A may play a key role in a signalling pathway that regulates cell proliferation and may be involved in brain development. 

Molecular pathology
DYRK1A is a candidate gene for learning defects associated with Down syndrome.
References in periodicals archive ?
Another therapeutic topic of interest resides on [beta]-carbolines' action upon DATs, since these alkaloids inhibit DYRK1A, a kinase found in the striatum which act as an important modulator of dopaminergic transmission and in dopamine vesicles' endocytosis (Brierley and Davidson, 2012).
2013) NGF Upregulates the Plasminogen Activation Inhibitor-1 in Neurons via the Calcineurin/NFAT Pathway and the Down Syndrome Related Proteins DYRK1A and RCAN1 Attenuate this Effect.
Moreover, in the limbic lobe, the highest expression values were registered at DG for DYRK1A and KCNJ6 and in the CA1 and CA2 for DSCR3 and KCNJ6 (Fig.
In Ts65Dn mice, green tea extract (Epi-Gallo-Catechin Gallate/EGCG) blocked the harmful effects of DYRK1A and restored normal physiology, learning, and behavior.
pl-carboline compounds, including harmine, inhibit DYRK1A and tau phosphorylation at multiple Alzheimer's disease-related sites.
Other innovative projects currently in development include SEL141, an early stage discovery program of DYRK1A kinase inhibitors with therapeutic potential in the treatment targeting Alzheimer's disease and Down syndrome, SEL201-novel small molecule MNK1/2 inhibitors in oncology, cancer metabolism platform and inflammasome platform.
DYRK1A phosphorylates NFAT, thereby mediating its nuclear export (27).
The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site.
One of these alkaloids, called harmine, inhibits a protein known as DYRK1A, which has been implicated by this and other studies in the formation of tau phosphorylation.
5-fold increase in dosage of RCAN1 and DYRK1A cooperatively destabilizes a regulatory circuit, leading to reduced NFATc activity and many of the features of Down syndrome.