◀ Back to AKT3
AKT3 — TNFSF11
Text-mined interactions from Literome
Wong et al., Mol Cell 1999
:
TRANCE , a TNF family member,
activates Akt/PKB through a signaling complex involving TRAF6 and c-Src ... Here, we demonstrate that
TRANCE activates the antiapoptotic serine/threonine kinase
Akt/PKB through a signaling complex involving c-Src and TRAF6
Lee et al., Bone 2002
:
The
RANKL stimulated phosphorylation of
Akt , a downstream target of PI 3-kinase, and that of ERK were observed
Zhang et al., J Immunol 2003
:
In addition, SHP-1 regulated
RANKL stimulated tyrosine phosphorylation of p85 subunit of phosphatidylinositol 3 kinase and the phosphorylation of
Akt
Saito et al., J Biol Chem 2004
(Bacterial Infections...) :
r4-1BB showed no effects on M-CSF- or RANKL induced phosphorylation of I-kappaB, ERK1/2, p38, or JNK, whereas
RANKL induced phosphorylation of
Akt , a downstream target of phosphatidylinositol 3-kinase (PI3K), was completely abolished by r4-1BB, suggesting that 4-1BB/4-1BBL reverse signaling may interfere with PI3K/Akt pathway
Kwak et al., Biochem Pharmacol 2004
(Bone Resorption) :
M-CSF and
RANKL activate the ERK,
Akt , and NF-kappaB signal transduction pathways, and SCOH suppressed this activation
Kim et al., Biochem Pharmacol 2004
(Bone Resorption) :
RANKL activated the ERK,
Akt , and NF-kappaB signal transduction pathways in osteoclast precursor cells, and tanshinone IIA suppressed this activation
Wang et al., J Clin Invest 2004
:
In particular, ritonavir is found to inhibit
RANKL induced
Akt signaling by disrupting the recruitment of TNF receptor associated factor 6/c-Src complex to lipid rafts
Ha et al., Exp Cell Res 2004
:
Pretreatment of osteoclasts with the antioxidants N-acetyl-l-cystein and glutathione reduced
RANKL induced
Akt , NF-kappaB, and ERK activation
Min et al., Blood 2007
(Neovascularization, Pathologic) :
RANKL also
led to the activation of
Akt and eNOS and to NO production in endothelial cells ( ECs )
Kim et al., Mol Pharmacol 2007
(Calcium Signaling) :
On the other hand, DMS strongly inhibited two separate signaling pathways, the
RANKL induced
activation of ERK and
Akt , which eventually converged on the transcription factors c-Fos and NFATc1
Mozar et al., J Cell Physiol 2008
(Bone Resorption) :
Pi was found to specifically inhibit the
RANKL induced JNK and
Akt activation , while RANKL induced p38 and ERK 1/2 phosphorylation were not significantly affected
Hu et al., Eur J Pharmacol 2008
:
RANKL induced
Akt phosphorylation was strongly inhibited by berberine ; however, neither monocyte/macrophage-colony stimulating factor ( M-CSF ) -induced nor insulin induced Akt activation was inhibited by the drug
McGonigle et al., Angiogenesis 2009
:
Signaling studies showed that OPG
induced ERK1/2 and
Akt phosphorylation in HUVECs while
RANKL had no effect
Fumimoto et al., J Pharmacol Sci 2012
:
Kahweol completely abolished
RANKL stimulated phosphorylation of extracellular signal regulated kinase and impaired phosphorylation of
Akt
Hemingway et al., Exp Mol Pathol 2013
:
We found that both
RANKL and LIGHT strongly
induced phosphorylation of
Akt and NF?B but not JNK in mouse osteoclast precursor cells
Li et al., Biochem Biophys Res Commun 2013
:
AG490 had no effects on
RANKL induced activation of
Akt , ERK1/2
Hwang et al., Life Sci 2013
:
We observed suppression of ERK, JNK,
AKT , and p38 mitogen activated protein kinases
induced by
RANKL in Western blotting after BPA treatment in RAW 264.7 cells