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Regulation of the Akt kinase by interacting proteins

Abstract

Ten years ago, it was observed that the Akt kinase is activated by phosphorylation via a phosphoinositide 3-kinase (PI-3K)-dependent process. This discovery generated enormous interest because it provided a link between PI-3K, an enzyme known to play a critical role in cellular physiology, and its downstream targets. Subsequently, it was shown that the activity of the core components of the ‘PI-3K/Akt pathway’ is modulated by a complex network of regulatory proteins and pathways. Some of the Akt-binding partners modulate its activation by external signals by interacting with different domains of the Akt protein. This review focuses on the Akt interacting proteins and the mechanisms by which they regulate Akt activation.

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Acknowledgements

We thank Tung On Chan (Thomas Jefferson University) for helpful discussions. Work on PI-3K and Akt in the PNT laboratory has been supported by PHS grant R01 CA57436. KD is a recipient of Thomas R Lee Career Development Award from the American Diabetes Association.

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Correspondence to Philip N Tsichlis.

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Du, K., Tsichlis, P. Regulation of the Akt kinase by interacting proteins. Oncogene 24, 7401–7409 (2005). https://doi.org/10.1038/sj.onc.1209099

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