Protein kinase A phosphorylates serine 267 in the homeodomain of engrailed-2 leading to decreased DNA binding

被引:8
作者
Hjerrild, M [1 ]
Stensballe, A
Jensen, ON
Gammeltoft, S
Rasmussen, TE
机构
[1] Glostrup Cty Hosp, Dept Clin Biochem, DK-2600 Glostrup, Denmark
[2] Univ So Denmark, Dept Biochem & Mol Biol, DK-5230 Odense M, Denmark
来源
FEBS LETTERS | 2004年 / 568卷 / 1-3期
关键词
engrailed-2; homeodomain; protein kinase A; protein phosphorylation; DNA binding;
D O I
10.1016/j.febslet.2004.05.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Engrailed-2 (En-2) belongs to an evolutionarily conserved family of DNA binding homeodomain-containing proteins that are expressed in mammalian brain during development. Here, we demonstrate that serine 267 in the homeodomain of En-2 is phosphorylated by protein kinase A (PKA) in forskolin-treated COS-7 cells. Furthermore, we analyze the physiological function of En-2 phosphorylation by PKA. The nuclear localization of En-2 is not influenced by the phosphorylation of serine 267. However, substitution of serine 267 with alanine resulted in increased binding of En-2 to DNA, while replacing serine 267 with glutamic acid resulted in decreased En-2 DNA binding. These results suggest that the transcriptional activity of En-2 is regulated by PKA. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:55 / 59
页数:5
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