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  • Title: Regulation of Dyrk1A kinase activity by 14-3-3.
    Author: Kim D, Won J, Shin DW, Kang J, Kim YJ, Choi SY, Hwang MK, Jeong BW, Kim GS, Joe CO, Chung SH, Song WJ.
    Journal: Biochem Biophys Res Commun; 2004 Oct 15; 323(2):499-504. PubMed ID: 15369779.
    Abstract:
    Dual-specificity tyrosine(Y) regulated kinase 1A (DYRK1A) is a serine/threonine protein kinase implicated in mental retardation resulting from Down syndrome. In this study, we carried out yeast two-hybrid screening to find proteins regulating DYRK1A kinase activity. We identified 14-3-3 as a Dyrk1A interacting protein, which is consistent with the previous finding of the interaction between the yeast orthologues Yak1p and Bmh1/2p. We showed the interaction between Dyrk1A and 14-3-3 in vitro and in vivo. The binding required the N-terminus of Dyrk1A and was independent of the Dyrk1A phosphorylation status. Functionally, 14-3-3 binding increased Dyrk1A kinase activity in a dose dependent manner in vitro. In vivo, a small peptide inhibiting 14-3-3 binding, sc138, decreased Dyrk1A kinase activity in COS7. In summary, these results suggest that DYRK1A kinase activity could be regulated by the interaction of 14-3-3.
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