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Regulation of Dyrk1A kinase activity by 14-3-3

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...

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Published in:Biochemical and biophysical research communications 2004-10, Vol.323 (2), p.499-504
Main Authors: Kim, Doyeun, Won, Jungyeon, Shin, Dong Wook, Kang, Junghee, Kim, Yeon Ju, Choi, Su Young, Hwang, Mi-Kyung, Jeong, Byeong-Woo, Kim, Gun Soo, Joe, Cheol O., Chung, Sul-Hee, Song, Woo-Joo
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Language:English
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2004.08.102