The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
EphA2 Mediates Ligand-Dependent Inhibition and Ligand-Independent Promotion of Cell Migration and Invasion via a Reciprocal Regulatory Loop with Akt
Open accessAbstract
SUMMARY Both pro- and anti-oncogenic properties have been attributed to EphA2 kinase. We report that a possible cause for this apparent paradox is diametrically opposite roles of EphA2 in regulating cell migration and invasion. While activation of EphA2 with its ligand ephrin-A1 inhibited chemotactic migration of glioma and prostate cancer cells, EphA2 overexpression promoted migration in a ligand-independent manner. Surprisingly, the latter effects required phosphorylation of EphA2 on serine 897 by Akt, and S897A mutation abolished ligand-independent promotion of cell motility. Ephrin-A1 stimulation of EphA2 negated Akt activation by growth factors and caused EphA2 dephosphorylation on S897. In human astrocytoma, S897 phosphorylation was correlated with tumor grades and Akt activation, suggesting that the Akt-EphA2 crosstalk may contribute to brain tumor progression.
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Metadata
- Authors
- Miao, H., Li, D.-Q., Mukherjee, A., Guo, H., Petty, A., Cutter, J., Basilion, J. P., Sedor, J., Wu, J., Danielpour, D., Sloan, A. E., Cohen, M. L., & Wang, B.
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2009-07
- Volume
- 16
- Issue
- 1
- Pages
- 9-20
- ISSN
- 1535-6108 (ISSN-L)
- OpenAlex
- W2139429540
- Cited by
- 533
- References
- 55
- FWCI
- 10.54
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Miao, H., Li, D.-Q., Mukherjee, A., Guo, H., Petty, A., Cutter, J., Basilion, J. P., Sedor, J., Wu, J., Danielpour, D., Sloan, A. E., Cohen, M. L., & Wang, B. (2009). EphA2 Mediates Ligand-Dependent Inhibition and Ligand-Independent Promotion of Cell Migration and Invasion via a Reciprocal Regulatory Loop with Akt. Cancer Cell. https://doi.org/10.1016/j.ccr.2009.04.009
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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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