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Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum
Open accessAbstract
Proapoptotic BCL-2 family members BAX and BAK are required for the initiation of mitochondrial dysfunction during apoptosis and for maintaining the endoplasmic reticulum (ER) Ca 2+ stores necessary for Ca 2+ -dependent cell death. Conversely, antiapoptotic BCL-2 has been shown to decrease Ca 2+ concentration in the ER. We found that Bax -/- Bak -/- double-knockout (DKO) cells have reduced resting ER Ca 2+ levels because of increased Ca 2+ leak and an increase in the Ca 2+ -permeable, hyperphosphorylated state of the inositol trisphosphate receptor type 1 (IP3R-1). The ER Ca 2+ defect of DKO cells is rescued by RNA interference reduction of IP3R-1, supporting the argument that this channel regulates the increased Ca 2+ leak in these cells. BCL-2 and IP3R-1 physically interact at the ER, and their binding is increased in the absence of BAX and BAK. Moreover, knocking down BCL-2 decreases IP3R-1 phosphorylation and ER Ca 2+ leak rate in the DKO cells. These findings support a model in which BCL-2 family members regulate IP3R-1 phosphorylation to control the rate of ER Ca 2+ leak from intracellular stores.
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Metadata
- Authors
- Oakes, S. A., Scorrano, L., Opferman, J. T., Bassik, M. C., Nishino, M., Pozzan, T., & Korsmeyer, S. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-12-21
- Volume
- 102
- Issue
- 1
- Pages
- 105-110
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2080678485
- Cited by
- 428
- References
- 1
- FWCI
- 8.97
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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