Gene interactions and pathways from curated databases and text-mining

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AKT1 — PIAS2

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
Wanzel et al., Nat Cell Biol 2005 : Akt and 14-3-3eta regulate Miz1 to control cell-cycle arrest after DNA damage
Liu et al., EMBO J 2006 : Akt phosphorylation is also required for interaction between TopBP1 and Miz1 or HPV16 E2, and repression of Miz1 transcriptional activity, suggesting a general role for TopBP1 oligomerization in the control of transcription factors
Ye et al., Am J Physiol Heart Circ Physiol 2007 (Myocardial Reperfusion Injury) : ATV and DIP alone did not affect myocardial Ser473 phosphorylated-Akt and Ser1177 phosphorylated-eNOS levels, whereas ATV + DIP significantly increased them
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