Gene interactions and pathways from curated databases and text-mining

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ABL1 — AKT2

Text-mined interactions from Literome

Gross et al., Mol Cell Biol 1999 (Cell Transformation, Neoplastic...) : In addition, we found that DeltaSH3 c-Abl induced less activation of Akt and STAT5 than did Bcr-Abl, suggesting that activation of these pathways plays a critical role in inducing a CML-like disease
Voss et al., Oncogene 2000 (MAP Kinase Signaling System...) : The mitogenic MAPK/Erk kinases as well as Akt/PKB , a kinase implicated to negatively regulate apoptosis, were also constitutively activated by both Bcr-Abl and Tel-Abl
Nieborowska-Skorska et al., Oncogene 2000 (Leukemia, Myeloid) : We show here that the defect in activation of PI-3k/Akt by BCR/ABL DeltaSH2 mutant ( SH2 domain deleted ) and of STAT5 by BCR/ABL DeltaSH3+DeltaSH2 mutant ( SH3 and SH2 domains deleted ) is not permanent and both Akt and STAT5 could be ` re-activated ' by in vitro culture
van der Kuip et al., Blood 2001 : Thus, cooperative activation of PI-3K/AKT by Bcr-Abl and integrins causes synergistic protection of Bcr-Abl+ cells from DNA damage induced apoptosis
Barnes et al., Oncogene 2005 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : Both IL-3 treatment and expression of Bcr-Abl led to enhanced phosphorylation of Akt ( protein kinase B )
Chu et al., Cancer Res 2007 (Cell Transformation, Neoplastic...) : BCR/ABL expression results in enhanced Ras and Akt activity but reduced mitogen activated protein kinase activity in human hematopoietic cells, which is reversed by BCR/ABL-Y177 mutation
Weisberg et al., Blood 2008 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive...) : BAG956 was shown to block AKT phosphorylation induced by BCR-ABL- , and induce apoptosis of BCR-ABL expressing cell lines and patient bone marrow cells at concentrations that also inhibit PI3K signaling
Ghosh-Choudhury et al., J Biol Chem 2013 : Remarkably, inhibition of c-Abl significantly suppressed BMP-2 stimulated PI 3-kinase activity and its downstream Akt phosphorylation