A phosphorylation site in the ftz homeodomain is required for activity

The EMBO Journal
J DongH M Krause

Abstract

The Drosophila homeodomain-containing protein Fushi tarazu (Ftz) is expressed sequentially in the embryo, first in alternate segments, then in specific neuroblasts and neurons in the central nervous system, and finally in parts of the gut. During these different developmental stages, the protein is heavily phosphorylated on different subsets of Ser and Thr residues. This stage-specific phosphorylation suggests possible roles for signal transduction pathways in directing tissue-specific Ftz activities. Here we show that one of the Ftz phosphorylation sites, T263 in the N-terminus of the Ftz homeodomain, is phosphorylated in vitro by Drosophila embryo extracts and protein kinase A. In the embryo, mutagenesis of this site to the non-phosphorylatable residue Ala resulted in loss of ftz-dependent segments. Conversely, substitution of T263 with Asp, which is also non-phosphorylatable, but which successfully mimics phosphorylated residues in a number of proteins, rescued the mutant phenotype. This suggests that T263 is in the phosphorylated state when functioning normally in vivo. We also demonstrate that the T263 substitutions of Ala and Asp do not affect Ftz DNA-binding activity in vitro, nor do they affect stability or transcriptio...Continue Reading

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Citations

Oct 14, 2000·Annual Review of Cell and Developmental Biology·R S Mann, G Morata
Mar 21, 2001·Evolution & Development·M P DevenportP Eggleston
Dec 29, 2010·Progress in Biophysics and Molecular Biology·Yoram Schiffmann
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May 10, 2000·The Journal of Biological Chemistry·H L FordD C Seldin
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Mar 4, 2011·Molecular Biology Reports·Cinzia PuppinGiuseppe Damante
Jan 14, 2020·PloS One·Anirban Banerjee, Anthony Percival-Smith
Jan 11, 2000·Genetics·W D TraceyJ P Gergen

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