TY - JOUR
T1 - A New Mutational aktivation in the PI3K Pathway
AU - Brugge, Joan
AU - Hung, Mien Chie
AU - Mills, Gordon B.
PY - 2007/8/14
Y1 - 2007/8/14
N2 - 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.
AB - 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.
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U2 - 10.1016/j.ccr.2007.07.014
DO - 10.1016/j.ccr.2007.07.014
M3 - Short survey
C2 - 17692802
AN - SCOPUS:34547574720
SN - 1535-6108
VL - 12
SP - 104
EP - 107
JO - Cancer Cell
JF - Cancer Cell
IS - 2
ER -