Two putative protein kinase CK2 phosphorylation sites are important for Myf-5 activity.

B Winter, I Kautzner, O G Issinger, H H Arnold

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 1997-Dec
OriginalsprogEngelsk
TidsskriftBiological Chemistry
Vol/bind378
Udgave nummer12
Sider (fra-til)1445-56
Antal sider11
ISSN1431-6730
DOI
StatusUdgivet - 1. dec. 1997

Fingeraftryk

Casein Kinase II
Phosphorylation
Dimerization
Reporter Genes
Serine
Muscle
Cell Differentiation
Glutamic Acid
Proteins
Transcription Factors
Genes
Muscles
Mutation
DNA
Substrates

Citer dette

Winter, B ; Kautzner, I ; Issinger, O G ; Arnold, H H. / Two putative protein kinase CK2 phosphorylation sites are important for Myf-5 activity. I: Biological Chemistry. 1997 ; Bind 378, Nr. 12. s. 1445-56.
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title = "Two putative protein kinase CK2 phosphorylation sites are important for Myf-5 activity.",
abstract = "Myf-5, a member of a family of muscle-specific transcription factors, is important for myogenic cell determination and differentiation. Here, we report that Myf-5 protein constitutes a substrate for phosphorylation in vitro by protein kinase CK2. We identified two potential phosphorylation sites at serine49 and serine133, both of which seem to be necessary for Myf-5 activity. Mutants which can no longer be phosphorylated fail to transactivate E-box-dependent reporter genes and act as trans-dominant repressors of wild-type Myf-5. Normal activity can be restored by replacing the serine residues with glutamate suggesting that a negative charge at these sites is obligatory for Myf-5 activity. Although serine133 is part of helix 2 which mediates dimerization, we find no evidence for impaired DNA-binding or heterodimerization of the Ser-Ala133 mutant. Some serine49 mutations exhibit reduced nuclear localization and/or protein stability. Our data suggest that CK2-mediated phosphorylation of Myf-5 is required for Myf-5 activity.",
keywords = "Animals, Binding Sites, Casein Kinase II, Cell Line, Cell Nucleus, DNA, DNA-Binding Proteins, Humans, Muscle Proteins, Mutagenesis, Site-Directed, Myogenic Regulatory Factor 5, Phosphorylation, Protein-Serine-Threonine Kinases, Rats, Recombinant Fusion Proteins, Serine, Trans-Activators, Transcription Factors",
author = "B Winter and I Kautzner and Issinger, {O G} and Arnold, {H H}",
year = "1997",
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Two putative protein kinase CK2 phosphorylation sites are important for Myf-5 activity. / Winter, B; Kautzner, I; Issinger, O G; Arnold, H H.

I: Biological Chemistry, Bind 378, Nr. 12, 01.12.1997, s. 1445-56.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Two putative protein kinase CK2 phosphorylation sites are important for Myf-5 activity.

AU - Winter, B

AU - Kautzner, I

AU - Issinger, O G

AU - Arnold, H H

PY - 1997/12/1

Y1 - 1997/12/1

N2 - Myf-5, a member of a family of muscle-specific transcription factors, is important for myogenic cell determination and differentiation. Here, we report that Myf-5 protein constitutes a substrate for phosphorylation in vitro by protein kinase CK2. We identified two potential phosphorylation sites at serine49 and serine133, both of which seem to be necessary for Myf-5 activity. Mutants which can no longer be phosphorylated fail to transactivate E-box-dependent reporter genes and act as trans-dominant repressors of wild-type Myf-5. Normal activity can be restored by replacing the serine residues with glutamate suggesting that a negative charge at these sites is obligatory for Myf-5 activity. Although serine133 is part of helix 2 which mediates dimerization, we find no evidence for impaired DNA-binding or heterodimerization of the Ser-Ala133 mutant. Some serine49 mutations exhibit reduced nuclear localization and/or protein stability. Our data suggest that CK2-mediated phosphorylation of Myf-5 is required for Myf-5 activity.

AB - Myf-5, a member of a family of muscle-specific transcription factors, is important for myogenic cell determination and differentiation. Here, we report that Myf-5 protein constitutes a substrate for phosphorylation in vitro by protein kinase CK2. We identified two potential phosphorylation sites at serine49 and serine133, both of which seem to be necessary for Myf-5 activity. Mutants which can no longer be phosphorylated fail to transactivate E-box-dependent reporter genes and act as trans-dominant repressors of wild-type Myf-5. Normal activity can be restored by replacing the serine residues with glutamate suggesting that a negative charge at these sites is obligatory for Myf-5 activity. Although serine133 is part of helix 2 which mediates dimerization, we find no evidence for impaired DNA-binding or heterodimerization of the Ser-Ala133 mutant. Some serine49 mutations exhibit reduced nuclear localization and/or protein stability. Our data suggest that CK2-mediated phosphorylation of Myf-5 is required for Myf-5 activity.

KW - Animals

KW - Binding Sites

KW - Casein Kinase II

KW - Cell Line

KW - Cell Nucleus

KW - DNA

KW - DNA-Binding Proteins

KW - Humans

KW - Muscle Proteins

KW - Mutagenesis, Site-Directed

KW - Myogenic Regulatory Factor 5

KW - Phosphorylation

KW - Protein-Serine-Threonine Kinases

KW - Rats

KW - Recombinant Fusion Proteins

KW - Serine

KW - Trans-Activators

KW - Transcription Factors

U2 - 10.1515/bchm.1997.378.12.1445

DO - 10.1515/bchm.1997.378.12.1445

M3 - Journal article

C2 - 9461343

VL - 378

SP - 1445

EP - 1456

JO - Biological Chemistry

JF - Biological Chemistry

SN - 1431-6730

IS - 12

ER -