Gene interactions and pathways from curated databases and text-mining

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AKT1 — HSP90AA1

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Fujita et al., J Biol Chem 2002 : Screening of drugs that could interfere with the Akt signaling pathway revealed that Hsp90 inhibitors ( e.g. geldanamycin, radicicol, and its analogues ) induced Akt dephosphorylation, which resulted in Akt inactivation and apoptosis of the cells ... Hsp90 inhibitors did not directly affect Akt kinase activity in vitro
Basso et al., J Biol Chem 2002 : Functional Hsp90 is required for the stability of Akt in the complex
Solit et al., Cancer Res 2003 (Breast Neoplasms) : These results suggest that Hsp90 inhibitors can effectively suppress Akt activity in animal models of human cancer at nontoxic doses, thus sensitizing tumor cells to proapoptotic stimuli
Takahashi et al., J Biol Chem 2003 : Akt was not observed in the eNOS complex in the absence of HSP90, but both active and inactive Akt associated with eNOS in the presence of HSP90
Fujita et al., Cancer Chemother Pharmacol 2003 : HSP90 inhibitors and topotecan suppressed AKT activity via indirectly downregulating PDK1 and phosphatidylinositide-3-OH kinase activities
Xu et al., Cancer Res 2003 (Breast Neoplasms) : Decreased AKT phosphorylation is not due to blockade of AKT activation or to preferential HSP90 mediated degradation of phosphorylated AKT
Yun et al., Cell Signal 2005 : In this report, we have examined the role of Hsp90 in regulating the activity of Akt in differentiating C2C12 myoblasts
Koga et al., Proc Natl Acad Sci U S A 2006 : Hsp90 inhibition transiently activates Src kinase and promotes Src dependent Akt and Erk activation
Boehm et al., Arthritis Rheum 2007 : Inhibition of Hsp90 with 100 nM or 500 nM geldanamycin blocked IGF-1 induced cell proliferation, Akt and p42/44 activation, and COL2A1 expression
Zhao et al., Zhonghua Shao Shang Za Zhi 2007 (Disease Models, Animal) : Endogenous HSP90 plays important roles in maintaining the cardiomyocyte activity, and its level might affect the expression of AKT
Hemdan et al., J Neurochem 2008 : The HSP-90 inhibitor caused a decrease in P-Akt level, induced caspase-3 activation, increased nuclear condensation and caused a loss in cell viability
Babchia et al., Invest Ophthalmol Vis Sci 2008 (Melanoma...) : HSP90 inhibition also reduced the expression of Akt , but the inhibition of Akt had no effect on cell proliferation, ruling out a role of Akt in the 17-AAG induced inhibition of cell proliferation
Kabakov et al., Int J Radiat Oncol Biol Phys 2008 : The drug induced radiosensitization of ECs seems to be caused by prevention of Hsp90 dependent phosphorylation ( activation ) of Akt that results in blocking the radioprotective phosphatidylinositol 3-kinase/Akt pathway
Yano et al., Proc Natl Acad Sci U S A 2008 (Bone Neoplasms...) : Hsp90 inhibition transiently activates osteoclast Src kinase and promotes Src dependent Akt activation
Barksdale et al., J Neurochem 2009 (Neuroblastoma) : We have found that HSP90 is responsible for Akt accumulation in the mitochondria in unstimulated cells ... These results indicate that the level of Akt in the mitochondria is dependent on HSP90 chaperoning activity and that Akt import can cause dynamic changes in mitochondrial configuration
Ram et al., Clin Cancer Res 2009 (Neoplasms) : Telomerase was activated by phosphorylation by Akt and by cytoplasmic-nuclear shift
Hackl et al., Surgery 2010 (Acute Disease...) : Inhibition of HSP90 effectively diminished the constitutive phosphorylation of Akt , Erk, and STAT3 in PHHs. Conversely, inhibition of HSP90 significantly increased the expression of both VEGF and HGF mRNA, and induced HSP70 protein in PHH cultures in vitro
Bhat et al., Mol Immunol 2010 : Our results demonstrate that binding of CpG ODN ( 2007 ) to Hsp90 induces activation of ERK2 and AKT phosphorylation leading to the production of high levels of IFN-gamma, IL-6, MIP-3alpha and nitric oxide ( NO )
Liao et al., American journal of translational research 2010 : Reports on ubiquitin dependent Akt degradation, caspase dependent cleavage, and the roles of molecular chaperone heat shock protein 90 (Hsp90) in the regulation of Akt stability are summarized
Redlak et al., Dig Dis Sci 2011 (Stomach Neoplasms) : The binding of HSP90 with pro-survival kinase Akt prevents proteosomal degradation of Akt and contributes to the functional stabilization of PI3K/Akt signaling and cell survival
Bai et al., Apoptosis 2011 (Liver Neoplasms...) : However, Hsp90 inhibitors effectively blocked SMC3 induced NF-?B activation through degradation of RIP1 and IKKß, two key components of the NF-?B activation pathway, and reduced both the constitutive and SMC3 induced Akt activity through degradation of the Akt protein
Tramentozzi et al., J Cell Mol Med 2011 : Results reveal a fundamental role of HSP90 in the PI3K/Akt pathway mediated angiogenic-like effect of Grp94-IgG, also questioning the capacity of CTT to serve as an effective inhibitor of the angiogenic effect
Khan et al., Mol Carcinog 2012 : It inhibited phosphatidylinositol-3-kinase (PI3K)/AKT activity, NF-?B, Hsp-90 , and survivin which may enhance the sensitivity of cells to apoptosis
Sobhan et al., Cancer Lett 2012 : Hsp90 inhibitors induced down regulation of Akt leading to proteasomal degradation of survivin and consequent mitochondrial apoptosis
Yoshida et al., Cell cycle (Georgetown, Tex.) 2011 (Urinary Bladder Neoplasms) : We also showed that CRT induces accumulation of nuclear phospho-Akt , which antagonizes apoptosis, and that Hsp90 inhibitors block the cellular process
Halder et al., FEBS J 2012 : Inhibition of upstream Hsp90 by TF and TR consequently attenuated Akt signaling and reduced the level of CDK2
Flandrin-Gresta et al., Oncotarget 2012 (Cell Transformation, Neoplastic...) : In conclusion, our data suggest the implication of HSP90 and FAK and AKT activation in the pathogenesis of myelodysplastic syndromes with excess of blasts and evolution to leukaemia
Kasukabe et al., Int J Oncol 2013 : We also found that the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin ( 17-AAG ) or arsenic trioxide ( ATO ) in combination with rapamycin markedly inhibited the growth of MCF-7 cells and 17-AAG or ATO suppressed rapamycin induced phosphorylation of Akt
Zhang et al., BMB Rep 2013 : Further study showed that Akt phosphorylation was enhanced by Hsp90ß , which was not due to the activation of upstream PI3K and PDK1 but because of stabilization of pAkt via direct interaction between Hsp90ß and pAkt
Leonard et al., Cell cycle (Georgetown, Tex.) 2013 : Inhibition of Akt activation with MK2206 reduced the whole-cell and centrosome levels of PLK-1 and ?-tubulin and also prevented the recruitment of PTEN to mitotic centrosomes
Su et al., Arch Biochem Biophys 2013 : Hsp90 inhibition causes Akt degradation, but the mechanism remains unclear
Wang et al., Chem Biol Interact 2013 : The Hsp90 inhibitor SNX-2112, induces apoptosis in multidrug resistant K562/ADR cells through suppression of Akt/NF-?B and disruption of mitochondria dependent pathways