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AKT1 — PIAS1
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Castillo et al., Cancer Res 2004
(Carcinoma, Non-Small-Cell Lung...) :
Of 24 compounds tested, five PIAs with modifications at two sites on the inositol ring inhibited Akt with IC ( 50 ) s < 5 micro M. Molecular modeling identified putative interactions of
PIAs with the phosphoinositide binding site in the PH domain of Akt, and growth factor induced translocation of
Akt to the plasma membrane was
inhibited by PIA administration ... Importantly,
PIAs increased apoptosis 20-30-fold in cancer cell lines with high levels of endogenous
Akt activity but only 4-5-fold in cancer cell lines with low levels of Akt activity
Gills et al., Expert Opin Investig Drugs 2004
:
PIAs inhibit
Akt translocation, phosphorylation and kinase activity
Gills et al., J Biol Chem 2007
:
Previously, we identified five active phosphatidylinositol ether lipid analogues (
PIAs ) that target the pleckstrin homology domain of Akt and selectively
induce apoptosis in cancer cells with high levels of
Akt activity
Memmott et al., Cancer Res 2008
(Carcinoma, Non-Small-Cell Lung...) :
PIAs activated AMPK in LKB1-mutant non-small cell lung cancer ( NSCLC ) cell lines with similar concentration dependence as that required to
inhibit Akt
Krech et al., BMC cancer 2010
(Colorectal Neoplasms) :
While the
PIAs clearly
reduce AKT phosphorylation in serum starved cells, we did not observe a significant reduction under serum supplemented conditions, giving us the opportunity to analyze AKT independent effects of these compounds
Gills et al., Cell death & disease 2012
(Lung Neoplasms) :
Pretreatment with sphingomyelinase inhibitors blocked ceramide generation, decreases in
phospho-Akt , nanovesicle release and cell detachment in
response to alkylphospholipids and
PIAs in non-small cell lung cancer cell lines