Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. STKE, 22 February 2005
Vol. 2005, Issue 272, p. tw74
[DOI: 10.1126/stke.2722005tw74]

EDITORS' CHOICE

CANCER Getting In on the Akt

Akt [also known as protein kinase B (PKB)] is deregulated in many human cancers. Sarbassov et al. have identified an enzyme in Drosophila and human cells that initiates its activation. Upon association with the cytoplasmic protein rictor, the cytoplasmic kinase mammalian target of rapamycin (mTOR) phosphorylates a critical hydrophobic motif in Akt/PKB. This modification is required for full activation of Akt and its subsequent regulation of cell survival. In contrast, association of mTOR with another cytoplasmic protein, raptor, does not target Akt and is sensitive to the drug rapamycin. Reduced expression of mTOR or rictor blocked Akt activity, which suggests that the complex may serve as an effective target in cancer cells for drug development.

D. D. Sarbassov, D. A. Guertin, S. M. Ali, D. M. Sabatini, Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307, 1098-1101 (2005). [Abstract] [Full Text]

Citation: Getting In on the Akt. Sci. STKE 2005, tw74 (2005).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882