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, 18 December 2007
Vol. 2007, Issue 417, p. tw457
[DOI: 10.1126/stke.4172007tw457]


Biochemistry PIKing Oncogenic Mutations

Valda Vinson

Science, AAAS, Washington, DC 20005, USA

Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that can initiate a variety of signaling events. Many human cancers involve mutations that activate PI3K{alpha}, a heterodimer composed of a catalytic subunit, p110{alpha}, and a regulatory subunit, p85{alpha}, both of which contain multiple domains. Huang et al. describe the crystal structure of a complex between the full-length human p110{alpha} catalytic subunit and the binding and activation domains of the p85{alpha} regulatory subunit. The structure provides insight into how oncogenic mutations affect enzyme activity and could assist in the future design of isoform- or mutation-specific inhibitors.

C.-H. Huang, D. Mandelker, O. Schmidt-Kittler, Y. Samuels, V. E. Velculescu, K. W. Kinzler, B. Vogelstein, S. B. Gabelli, L. M. Amzel, The structure of a human p110{alpha}/p85{alpha} complex elucidates the effects of oncogenic PI3K{alpha} mutations. Science 318, 1744-1748 (2007). [Abstract] [Full Text]

Citation: V. Vinson, PIKing Oncogenic Mutations. Sci. STKE 2007, tw457 (2007).

To Advertise     Find Products

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