Publication details
Heavy metals induce phosphorylation of the Bcl
-2 protein by Jun N-terminal kinase
| Basic information | |
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| Original title: | Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase |
| Authors: | Eva Ondroušková, Jana Slováčková, Vendula Pelková, Jiřina Procházková, Karel Souček, Petr Beneš, Jan Šmarda |
| Further information | |
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| Citation: | ONDROUŠKOVÁ, Eva - SLOVÁČKOVÁ, Jana - PELKOVÁ, Vendula - PROCHÁZKOVÁ, Jiřina - SOUČEK, Karel - BENEŠ, Petr - ŠMARDA, Jan. Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase. In XIX. Biologické dny. Biologický výzkum pro lidské zdraví. Brno : Československá biologická společnost a LF Univerzity Karlovy v Hradci Králové, 2008. ISBN 978-80-7399-545-4, pp. 74-75. 2008, Hradec Králové. |
| Original language: | English |
| Field: | Genetics and molecular biology |
| Type: | Article in Proceedings |
| Keywords: | Bcl-2; heavy metals; Jun N-terminal kinase; phosphorylation; posttranslational modification |
The Bcl-2 protein is one of the key components of biochemical pathways controling programmed cell death. Function of this protein can be regulated by posttranslational modifications. Phosphorylation of Bcl-2 has been considered to be significantly associated with cell cycle arrest in the G2/M phase of the cell cycle, and with cell death caused by defects of microtubule dynamics. In this study, we show that heavy metal-induced stress and cell death correlate with induction of the Bcl-2 protein phosphorylation in several cell lines. Zinc-induced phosphorylation of Bcl-2 is mediated by the Jun N-terminal kinase pathway, and it is not linked to cell cycle arrest at G2/M. Cells of breast carcinoma cell line MDA-MB-231 expressing the wild-type Bcl-2 protein are more resistant to zinc-induced cell death than those expressing mutant variant of Bcl-2 that cannot be phosphorylated at amino acid residues Ser70, Ser87, Thr69. These results suggest that phosphorylation of the Bcl-2 protein is an important part of cellular response to the stress and that this posttranslational modification is significantly involved in control of the Bcl-2 protein function.
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