The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
The Activation of p38 and Apoptosis by the Inhibition of Erk Is Antagonized by the Phosphoinositide 3-Kinase/Akt Pathway
Open accessAbstract
Considerable attention has recently been focused on the role played by different kinase cascades in the control of apoptosis. The triggering of stress-activated kinases concomitant with the inhibition of the extracellular signal-regulated kinase (ERK) pathway has been observed in a number of cell systems undergoing programmed cell death. In addition, the activation of the phosphoinositide 3-kinase (PI 3-kinase)-Akt signaling cascade has been shown to protect from apoptosis. Here we have explored the potential role played by the inhibition of ERK in the activation of the stress kinases as well as the possible cross-talk with the PI 3-kinase pathway in HeLa cells. We show that the simple inhibition of ERK basal activity is sufficient to trigger apoptosis and p38 activation with no changes in Jun N-terminal kinase/stress-activated protein kinase. This is a process dependent on the caspases and is completely abrogated by serum. The incubation with wortmannin or the transfection of dominant negative mutants of p85 or Akt block the inhibitory function of serum, suggesting the involvement of the PI 3-kinase-Akt system. Consistent with this, expression of active mutants of PI 3-kinase and Akt inhibits p38 activation and apoptosis. We also show here that the inhibition of ERK triggers the caspase system, which is abolished by serum in a wortmannin-dependent manner. Collectively, these results demonstrate a link between ERK and the p38 apoptotic pathway that is modulated by the survival PI 3-kinase-Akt module, acting upstream the caspase system.
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Cites
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Cited by
Cellular survival: a play in three Akts
Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216
ERK signalling: A master regulator of cell behaviour, life and fate
Lavoie, H., Gagnon, J., & Therrien, M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0255-7 · Cited by 1,185
PI 3-kinase, Akt and cell survival
Downward, J. (2004) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2004.01.002 · Cited by 783
Akt Phosphorylates and Negatively Regulates Apoptosis Signal-Regulating Kinase 1
Kim, A. H., Khursigara, G., Sun, X., Franke, T. F., & Chao, M. V. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.3.893-901.2001 · Cited by 709
PI3K/Akt: getting it right matters
Franke, T. F. (2008) · Oncogene · doi:10.1038/onc.2008.313 · Cited by 695
Metadata
- Authors
- Berra, E., Diaz-Meco, M. T., & Moscat, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-04
- Volume
- 273
- Issue
- 17
- Pages
- 10792-10797
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2047682144
- Cited by
- 254
- References
- 39
- FWCI
- 10.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: The Activation of p38 and Apoptosis by the Inhibition of Erk Is Antagonized by the Phosphoinositide 3-Kinase/Akt Pathway. https://app.cochat.ai/papers/10.1074/jbc.273.17.10792
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- Berra, E., Diaz-Meco, M. T., & Moscat, J. (1998). The Activation of p38 and Apoptosis by the Inhibition of Erk Is Antagonized by the Phosphoinositide 3-Kinase/Akt Pathway. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.17.10792
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
