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PMID: 2899884 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The Drosophila engrailed protein is phosphorylated by a serine-specific protein kinase.

Nucleic acids research ·Vol. 16 ·No. 14A ·1988-07-25 ·Pages 6637-47

Gay NJ, Poole SJ, Kornberg TB

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals DNA-Binding Proteins/physiology Drosophila melanogaster/physiology Genes, Homeobox Hot Temperature Molecular Sequence Data Molecular Weight Nuclear Proteins/physiology Phosphoproteins/physiology Phosphoserine/metabolism Protein Processing, Post-Translational Transcription Factors/physiology
Chemicals
DNA-Binding Proteins Nuclear Proteins Phosphoproteins Transcription Factors Phosphoserine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Gay N J
Department of Biochemistry, University of California, San Francisco 94143.
Poole S J
Kornberg T B
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/16.14.6637
Published
1988-07-25
Pages
6637-47
Language
English
Region
England
NLM ID
0411011
PMCID
PMC338319
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/16.14.6637 PMC Full Text View journal details
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