Drosophila Homeodomain-Interacting Protein Kinase (Hipk) Phosphorylates the Homeodomain Proteins Homeobrain, Empty Spiracles, and Muscle Segment Homeobox

International Journal of Molecular Sciences

Uwe Walldorf¹  EvaLouise Steinmetz¹  DeniseNicole Dewald²  Nadine Luxem³ 

[1] Developmental Biology, Saarland University, Building 61, 66421 Homburg, Germany;Inter-Faculty Institute for Cell Biology Animal Genetics, Auf der Morgenstelle 15, 72076 Tübingen, Germany;MVZ centre of laboratory medicine, Viktoriastraße 39, 56068 Koblenz, Germany;

关键词: homeodomain-interacting protein kinase (Hipk);    serine/threonine kinase;    homeodomain;    Hbn;    Ems;    Msh;    neurogenesis;   

DOI  :  10.3390/ijms20081931

来源: DOAJ

【 摘 要 】

The Drosophila homeodomain-interacting protein kinase (Hipk) is the fly representative of the well-conserved group of HIPKs in vertebrates. It was initially found through its characteristic interactions with homeodomain proteins. Hipk is involved in a variety of important developmental processes, such as the development of the eye or the nervous system. In the present study, we set Hipk and the Drosophila homeodomain proteins Homeobrain (Hbn), Empty spiracles (Ems), and Muscle segment homeobox (Msh) in an enzyme-substrate relationship. These homeoproteins are transcription factors that function during Drosophila neurogenesis and are, at least in part, conserved in vertebrates. We reveal a physical interaction between Hipk and the three homeodomain proteins in vivo using bimolecular fluorescence complementation (BiFC). In the course of in vitro phosphorylation analysis and subsequent mutational analysis we mapped several Hipk phosphorylation sites of Hbn, Ems, and Msh. The phosphorylation of Hbn, Ems, and Msh may provide further insight into the function of Hipk during development of the Drosophila nervous system.

【 授权许可】

Unknown