Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase
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Eva Ondroušková
Abstract
The Bcl-2 protein is one of the key components of biochemical pathways controlling programmed cell death. The 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. This study shows that phosphorylation of Bcl-2 can be induced by heavy metals due to activation of the Jun N-terminal kinase pathway that is not linked to the G2/M cell cycle arrest. Furthermore, we demonstrate that hyperphosphorylated Bcl-2 protein is a more potent inhibitor of zinc-induced cell death than its hypophosphorylated mutant form. These data suggest that regulation of Bcl-2 protein function by phosphorylation is an important part of cell responses to stress.
©2009 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Editor's Note
- Editor's Note
- Protein Structure and Function
- Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence
- Biochemical characterization of the catalytic domains of three different clostridial collagenases
- Impact of detergents on the activity of acetylcholinesterase and on the effectiveness of its inhibitors
- The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein
- Membranes, Lipids, Glycobiology
- Glycosphingolipids from bovine milk and milk fat globule membranes: a comparative study. Adhesion to enterotoxigenic Escherichia coli strains
- Mannose 6-phosphate receptor-dependent endocytosis of lysosomal enzymes is increased in sulfatide-storing kidney cells
- Cell Biology and Signaling
- Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase
- Fibroblast growth factor 2 (FGF-2) is a novel substrate for arginine methylation by PRMT5
- Differential functions of the Apoer2 intracellular domain in selenium uptake and cell signaling
- Active immunisation against gastric inhibitory polypeptide (GIP) improves blood glucose control in an animal model of obesity-diabetes
- Novel Techniques
- Applicability of superfolder YFP bimolecular fluorescence complementation in vitro
