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

EDITORS' CHOICE

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).

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Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)