Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase

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Authors

ONDROUŠKOVÁ Eva SLOVÁČKOVÁ Jana PELKOVÁ Vendula PROCHÁZKOVÁ Jiřina SOUČEK Karel BENEŠ Petr ŠMARDA Jan

Year of publication 2008
Type Article in Proceedings
Conference XIX. Biologické dny. Biologický výzkum pro lidské zdraví
MU Faculty or unit

Faculty of Science

Citation
Field Genetics and molecular biology
Keywords Bcl-2; heavy metals; Jun N-terminal kinase; phosphorylation; posttranslational modification
Description 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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