Context-dependent regulation of Hox protein functions by CK2 phosphorylation sites

  • Ouarda Taghli-Lamallem
  • Cheryl Hsia
  • Matthew Ronshaugen
  • William McGinnis
Original Article

DOI: 10.1007/s00427-008-0224-1

Cite this article as:
Taghli-Lamallem, O., Hsia, C., Ronshaugen, M. et al. Dev Genes Evol (2008) 218: 321. doi:10.1007/s00427-008-0224-1

Abstract

Variations in Hox protein sequences and functions have been proposed to contribute to evolutionary changes in appendage shape and number in crustaceans and insects. One model is that insect Hox proteins of the Ultrabithorax (UBX) ortholog class evolved increased abilities to repress Distal-less (Dll) transcription and appendage development in part through the loss of serine and threonine residues in casein kinase 2 (CK2) phosphorylation sites. To explore this possibility, we constructed and tested the appendage repression function of chimeric proteins with insertions of different CK2 consensus sites or phosphomimetics of CK2 sites in C-terminal regions of Drosophila melanogaster UBX. Our results indicate that CK2 sites C-terminal to the homeodomain can inhibit the appendage repression functions of UBX proteins, but only in the context of specific amino acid sequences. Our results, combined with previous findings on evolutionary changes in Hox protein, suggest how intra-protein regulatory changes can diversify Hox protein function, and thus animal morphology.

Keywords

Ultrabithorax Evolution Phosphorylation Casein kinase 2 Homeotic Transcription factor Hox function Hox modification 

Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  • Ouarda Taghli-Lamallem
    • 2
  • Cheryl Hsia
    • 1
  • Matthew Ronshaugen
    • 3
  • William McGinnis
    • 1
  1. 1.Section in Cell and Developmental Biology, Division of BiologyUniversity of California, San DiegoLa JollaUSA
  2. 2.Neuroscience & Aging Research CenterThe Burnham Institute for Medical ResearchLa JollaUSA
  3. 3.The Healing Foundation Centre, Faculty of Life SciencesUniversity of ManchesterManchesterUK

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