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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hjerrild M,Stensballe A,Jensen ON,Gammeltoft S,Rasmussen TE

doi

10.1016/j.febslet.2004.05.009

keywords:

subject

Has Abstract

pub_date

2004-06-18 00:00:00

pages

55-9

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579304006076

journal_volume

568

pub_type

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