Kateřina Hanáková(1), David Potěšil(2), Ondřej Bernatík(3), Igor Cervenka(4), Matěj Rádsetoulal(5), Vítězslav Bryja(6), Zbyněk Zdráhal(7*)

(1) National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Brno, 62500, CZECH REPUBLIC; Central European Institute of Technology, Masaryk University, Brno, 62500, CZECH REPUBLIC
(2) Central European Institute of Technology, Masaryk University, Brno, 62500, CZECH REPUBLIC
(3) Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, 62500, CZECH REPUBLIC
(4) Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, 62500, CZECH REPUBLIC
(5) Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, 62500, CZECH REPUBLIC
(6) Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, 62500, CZECH REPUBLIC
(7) National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Brno, 62500, CZECH REPUBLIC; Central European Institute of Technology, Masaryk University, Brno, 62500, CZECH REPUBLIC
(*) Corresponding Author

Semiquantitative Assessment of Dishevelled-3 Phosphorylation Status by Mass Spectrometry


Abstract



The focus of this paper is the human Dishevelled 3 protein (hDvl3), an essential component of the Wnt signalling pathway that contributes to their regulation. Mass spectrometry-based analysis of hDvl3 phosphorylations induced by eight associated kinases was performed revealing several dozens of phosphorylation sites. The main outcome of this study was the description of Dvl phosphorylation “patterns” induced by individual kinases.

Keywords


phosphorylation; Dishevelled 3; mass spectrometry; CK1ε; NEK2

Full Text: PDF