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

Majbrit Hjerrild, Allan Stensballe, Ole N Jensen, Steen Gammeltoft, Thomas E Rasmussen

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 2004-Jun-18
OriginalsprogEngelsk
TidsskriftFEBS Letters
Vol/bind568
Udgave nummer1-3
Sider (fra-til)55-9
Antal sider4
ISSN0014-5793
DOI
StatusUdgivet - 2004

Fingeraftryk

Cyclic AMP-Dependent Protein Kinases
Serine
Phosphorylation
DNA
Homeodomain Proteins
COS Cells
DNA-Binding Proteins
Colforsin
Alanine
Glutamic Acid
Brain
Substitution reactions
Proteins

Citer dette

Hjerrild, Majbrit ; Stensballe, Allan ; Jensen, Ole N ; Gammeltoft, Steen ; Rasmussen, Thomas E. / Protein kinase A phosphorylates serine 267 in the homeodomain of engrailed-2 leading to decreased DNA binding. I: FEBS Letters. 2004 ; Bind 568, Nr. 1-3. s. 55-9.
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title = "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.",
keywords = "Amino Acid Sequence, Animals, COS Cells, Cell Nucleus, Cyclic AMP-Dependent Protein Kinases, DNA, Homeodomain Proteins, Nerve Tissue Proteins, Phosphorylation, Promoter Regions (Genetics), Protein Binding",
author = "Majbrit Hjerrild and Allan Stensballe and Jensen, {Ole N} and Steen Gammeltoft and Rasmussen, {Thomas E}",
year = "2004",
doi = "10.1016/j.febslet.2004.05.009",
language = "English",
volume = "568",
pages = "55--9",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd.",
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Protein kinase A phosphorylates serine 267 in the homeodomain of engrailed-2 leading to decreased DNA binding. / Hjerrild, Majbrit; Stensballe, Allan; Jensen, Ole N; Gammeltoft, Steen; Rasmussen, Thomas E.

I: FEBS Letters, Bind 568, Nr. 1-3, 2004, s. 55-9.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Protein kinase A phosphorylates serine 267 in the homeodomain of engrailed-2 leading to decreased DNA binding

AU - Hjerrild, Majbrit

AU - Stensballe, Allan

AU - Jensen, Ole N

AU - Gammeltoft, Steen

AU - Rasmussen, Thomas E

PY - 2004

Y1 - 2004

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - COS Cells

KW - Cell Nucleus

KW - Cyclic AMP-Dependent Protein Kinases

KW - DNA

KW - Homeodomain Proteins

KW - Nerve Tissue Proteins

KW - Phosphorylation

KW - Promoter Regions (Genetics)

KW - Protein Binding

U2 - 10.1016/j.febslet.2004.05.009

DO - 10.1016/j.febslet.2004.05.009

M3 - Journal article

VL - 568

SP - 55

EP - 59

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1-3

ER -