Open AccessTheDrosophila engrailedprotein is phosphorylated by a serine-specific protein kinase
Author(s) -
Stephen J. Poole,
Thomas B. Kornberg
Publication year - 1988
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/16.14.6637
Subject(s) - engrailed , biology , homeobox , akt3 , phosphorylation , drosophila melanogaster , protein kinase a , microbiology and biotechnology , protein phosphorylation , autophagy related protein 13 , imaginal disc , serine , gene , biochemistry , threonine , transcription factor
The engrailed gene is required during embryogenesis of Drosophila melanogaster for normal segmental development and for differentiation of posterior compartments. The protein encoded by the engrailed gene contains a homeodomain, has sequence specific DNA binding activity, and has been proposed as a transcriptional regulator. We show here that the engrailed protein, isolated from both cultured cells and embryos, has been modified by a serine-specific protein kinase. This is the first report that homeobox proteins are post-translationally modified. Phosphorylation of the engrailed protein may directly or allosterically modify its function, and offers the possibility that the engrailed protein becomes phosphorylated in response to extracellular, mitogenic or positional stimuli.