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AKT1 — SYT1
Text-mined interactions from Literome
Sizemore et al., Mol Cell Biol 1999
:
Additionally, the expression of a constitutively activated form of either p110 or the PI3K activated protein kinase
Akt also
induces p65/RelA mediated transactivation
Lee et al., J Biol Chem 2003
:
LY294002, dominant negative ( DN ) phosphatidylinositol 3-kinase (PI3K), or
AKT ( DN )
inhibited NFkappaB activation,
p65 transactivation, and cyclooxygenase-2 (COX-2) expression induced by lauric acid or constitutively active ( CA ) TLR4
Yasui et al., Cancer Res 2005
(Multiple Myeloma) :
Finally, it down-regulates interleukin-6 induced phosphorylation of
Akt , signal transducers and activators of transcription 3, and p42/44 mitogen activated protein kinase ; insulin-like growth factor-I triggered Akt phosphorylation ; and tumor necrosis factor alpha
induced IkappaBalpha and nuclear factor-kappaB
p65 phosphorylation
Kawakami et al., J Rheumatol 2007
(Sjogren's Syndrome) :
TLR ligands induced phosphorylation of ERK, JNK, and p38 in HSG cells, but not
Akt phosphorylation or
activation of NF-kappaB
p65
Kang et al., Gastroenterology 2008
(Stomach Neoplasms) :
AKT activation
increased p65/RelA binding to a putative NF-kappaB binding site in the HuR promoter, the stability of HuR target transcripts, and the cytoplasmic import of HuR
Takeshima et al., BMC microbiology 2009
(Helicobacter Infections) :
NF-kappaB activation by Helicobacter pylori requires
Akt mediated phosphorylation of
p65
Ro et al., J Biomed Sci 2010
:
Akt regulates the expression of MafK,
synaptotagmin I , and syntenin-1, which play roles in neuronal function ... These results indicate that dominant negative or pharmacological inhibition of
Akt increases the expression of MafK,
SytI , and Syn-1 genes
Roth et al., Mol Biol Cell 2010
:
Activation of p38 kinase by hypertonicity and downstream activation of
Akt play key roles in TonEBP activity, I?Ba degradation, and
p65 nuclear translocation
Qi et al., Front Biosci (Elite Ed) 2012
(Reperfusion Injury) :
Moreover, the phosphorylation of
AKT and ERK1/2 in the liver was
enhanced , while the phosphorylation of JNK, p38 and
p65 was suppressed