A New Mutational aktivation in the PI3K Pathway

Joan Brugge, Mien Chie Hung, Gordon Mills

Research output: Contribution to journalShort survey

184 Citations (Scopus)

Abstract

Although multiple members of the phosphatidylinositol-3-kinase pathway (PI3K) are targeted by germline or somatic mutations, functional mutations in the three akt isoforms have proven elusive. This is somewhat surprising, as AKT represents a key node in the PI3K pathway, exhibiting transforming activity when incorporated into the AKT8 retrovirus. A recent report in Nature identifies a transforming E17K PH domain mutation in akt1 in breast (8%), colorectal (6%), and ovarian (2%) cancers. E17K-akt1 transforming activity appears due to PtdIns(3,4)P2- and PtdIns(3,4,5)P3-independent recruitment of AKT1 to the membrane. This novel observation raises important theoretical and clinical questions.

Original languageEnglish (US)
Pages (from-to)104-107
Number of pages4
JournalCancer Cell
Volume12
Issue number2
DOIs
StatePublished - Aug 14 2007
Externally publishedYes

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Phosphatidylinositol 3-Kinase
Mutation
Retroviridae
Ovarian Neoplasms
Protein Isoforms
Breast
Observation
Membranes

ASJC Scopus subject areas

  • Cancer Research
  • Cell Biology
  • Oncology

Cite this

A New Mutational aktivation in the PI3K Pathway. / Brugge, Joan; Hung, Mien Chie; Mills, Gordon.

In: Cancer Cell, Vol. 12, No. 2, 14.08.2007, p. 104-107.

Research output: Contribution to journalShort survey

Brugge, Joan ; Hung, Mien Chie ; Mills, Gordon. / A New Mutational aktivation in the PI3K Pathway. In: Cancer Cell. 2007 ; Vol. 12, No. 2. pp. 104-107.
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