4.7 Article

Drosophila Homeodomain-Interacting Protein Kinase (Hipk) Phosphorylates the Hippo/Warts Signalling Effector Yorkie

Journal

Publisher

MDPI
DOI: 10.3390/ijms22041862

Keywords

homeodomain-interacting protein kinase (Hipk); serine; threonine kinase; Hippo; Warts signalling; Yorkie (Yki)

Funding

  1. Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)
  2. Saarland University

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The study identified Hipk as a kinase that phosphorylates Yki, mapping several phosphorylation sites of Yki. These sites potentially provide additional regulation for Yki in vivo, with transgenic flies exhibiting notable phenotypes. Hipk is therefore an additional upstream regulator of Yki working in conjunction with Wts.
Developmental growth and patterning are regulated by an interconnected signalling network of several pathways. In Drosophila, the Warts (Wts) kinase, a component of the Hippo signalling pathway, plays an essential role in regulating transcription and growth by phosphorylating its substrate Yorkie (Yki). The phosphorylation of Yki critically influences its localisation and activity as a transcriptional coactivator. In this study, we identified the homeodomain-interacting protein kinase (Hipk) as another kinase that phosphorylates Yki and mapped several sites of Yki phosphorylated by Hipk, using in vitro analysis: Ser168, Ser169/Ser172 and Ser255. These sites might provide auxiliary input for Yki regulation in vivo, as transgenic flies with mutations in these show prominent phenotypes; Hipk, therefore, represents an additional upstream regulator of Yki that works in concert with Wts.

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