| POSPÍŠILOVÁ, Šárka, Václav BRÁZDA, Kateřina KUCHAŘÍKOVÁ, M.Gloria LUCIANI, Ted R. HUPP, Petr SKLÁDAL, Emil PALEČEK and Bořivoj VOJTĚŠEK. Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. Biochemical Journal. London: Portland Press, 2004, vol. 378, No 11, p. 939-947. ISSN 0264-6021. |
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@article{555474,
author = {Pospíšilová, Šárka and Brázda, Václav and Kuchaříková, Kateřina and Luciani, M.Gloria and Hupp, Ted R. and Skládal, Petr and Paleček, Emil and Vojtěšek, Bořivoj},
article_location = {London},
article_number = {11},
keywords = {Protein p53; Kinase; Phosphorylation; Piezoelectric biosensor},
language = {eng},
issn = {0264-6021},
journal = {Biochemical Journal},
title = {Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2},
volume = {378},
year = {2004}
}
TY - JOUR
ID - 555474
AU - Pospíšilová, Šárka - Brázda, Václav - Kuchaříková, Kateřina - Luciani, M.Gloria - Hupp, Ted R. - Skládal, Petr - Paleček, Emil - Vojtěšek, Bořivoj
PY - 2004
TI - Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2
JF - Biochemical Journal
VL - 378
IS - 11
SP - 939-947
EP - 939-947
PB - Portland Press
SN - 02646021
KW - Protein p53
KW - Kinase
KW - Phosphorylation
KW - Piezoelectric biosensor
N2 - Tumor suppressor protein p53 is one of the most important regulators of cell proliferation, differentiation and programmed cell death, triggering growth arrest and/or apoptosis in response to different cellular stress signals. The sequence-specific DNA binding function of p53 protein can be activated by several different stimuli modulating the C-terminal domain of this protein. The most likely physiological mechanism of p53 sequence-specific DNA binding activity is its post-translational modification, mainly phosphorylation of specific sites. Here we used non-radioactive electrophoretic mobility shift assay (EMSA) to show that C-terminal phosphorylation of p53 protein by cdk2/cyclin A at serine 315 and by PKC at serines 371, 376 and 378 can efficiently stimulate p53 binding to DNA in vitro as well as binding of C-terminal monoclonal antibody Bp53-10 recognizing the residue 371-380.
ER -
POSPÍŠILOVÁ, Šárka, Václav BRÁZDA, Kateřina KUCHAŘÍKOVÁ, M.Gloria LUCIANI, Ted R. HUPP, Petr SKLÁDAL, Emil PALEČEK and Bořivoj VOJTĚŠEK. Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. \textit{Biochemical Journal}. London: Portland Press, 2004, vol.~378, No~11, p.~939-947. ISSN~0264-6021.
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