Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase
| Authors | |
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| Year of publication | 2008 |
| Type | Article in Proceedings |
| Conference | XIX. Biologické dny. Biologický výzkum pro lidské zdraví |
| MU Faculty or unit | |
| 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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