Functional Analysis of Dishevelled-3 Phosphorylation Identifies Distinct Mechanisms Driven by Casein Kinase 1ϵ and Frizzled5*

@inproceedings{Bernatk2014FunctionalAO,
  title={Functional Analysis of Dishevelled-3 Phosphorylation Identifies Distinct Mechanisms Driven by Casein Kinase 1ϵ and Frizzled5*},
  author={Ondřej Bernat{\'i}k and Kateřina {\vS}eďov{\'a} and Carolin Schille and Ranjani Sri Ganji and Igor {\vC}ervenka and Luk{\'a}{\vs} Trant{\'i}rek and Alexandra Schambony and Zbyněk Zdr{\'a}hal and V{\'i}tězslav Bryja},
  booktitle={The Journal of biological chemistry},
  year={2014}
}
Dishevelled-3 (Dvl3), a key component of the Wnt signaling pathways, acts downstream of Frizzled (Fzd) receptors and gets heavily phosphorylated in response to pathway activation by Wnt ligands. Casein kinase 1ϵ (CK1ϵ) was identified as the major kinase responsible for Wnt-induced Dvl3 phosphorylation. Currently it is not clear which Dvl residues are phosphorylated and what is the consequence of individual phosphorylation events. In the present study we employed mass spectrometry to analyze in… CONTINUE READING

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Semiquantitative Assessment of Dishevelled-3 Phosphorylation Status by Mass Spectrometry

Kateřina Hamáková, David Potěšil, +4 authors Zbyněk Zdráhal
  • 2018
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