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  Thereby, several signal transduction pathways are initiated, including phosphat

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jy9202
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 Thereby, several signal transduction pathways are initiated, including phosphat Empty
OdoslaťPredmet: Thereby, several signal transduction pathways are initiated, including phosphat    Thereby, several signal transduction pathways are initiated, including phosphat Icon_minitimeŠt august 14, 2014 10:58 am

Further more, we also found that U73122, which blocks both PLC and PLD activities, as well as Ca2 chelating agents, inhib ited the PDGF BB mediated phosphorylation of ARN-509 溶解度 Akt on Ser473, but not on Thr308. It has been reported, and we confirmed, that in Rictor null cells the level of PKC is severely reduced. In addition, we found that PLCγ phosphorylation is dramatically suppressed in Rictor null cells compared to control cells. Interestingly, treatment with PMA overnight to downregulate DAG dependent PKC isoforms resulted in inhibition of phosphorylation of Akt on both Ser473 and Thr308. The effect on Thr308 did not occur by any reduction in p PDK1 levels, indicat ing that a DAG responsive kinase is involved in the phos phorylation of Thr308.<br><br> Another possibility is that while PMA treatment overnight did not affect the phosphoryl ation of PDK1, it may have influenced its intracellular localization. We also found that in PLCγ1 null cells, the phosphorylation of both Ser473 and Thr308 on Akt were reduced. Interestingly, it has recently been demonstrated that PDK1 and AUY922 溶解度 PLCγ interact after EGF stimulation and that PDK1 is involved in the activation of PLCγ in a man ner that only partially depends on PDK1 activity. Thus, it is possible that the interaction between PDK1 and PLCγ regulates the ability of PDK1 to phosphorylate Akt on Thr308, potentially by acting as a scaffold. This hypothesis is consistent with our observation that PDGF BB induced Thr308 phosphorylation is reduced in PLCγ deficient cells but is not affected by PLCγ inhibition or Ca2 chelation.<br><br> Collectively, these results suggest that the pathway leading from the PDGFR to phosphorylation of Akt involves mTORC2 and PLC Ca2 ATP-competitive ALK 阻害剤 signaling, although some aspects of the molecular mechanism remain to be elucidated. Activation of Akt has been associated with increased cell viability. Consistent with a critical role for mTORC2 in Akt activation, we found that in Rictor deficient cells, which are blunted in their ability to activate Akt, PDGF BB was not able to suppress starvation induced caspase 3 cleavage, whereas it did so in control cells. mTORC1 is widely accepted to be responsible for S6 kinase activation leading to phosphorylation of the ribosomal S6 protein, thus facilitating protein transla tion. Several reports have suggested that mTORC1 may be downstream of Akt signaling, although this has been challenged.<br><br> Our results suggest that in PDGF BB stimulated fibroblasts, Akt is not upstream of S6 phosphorylation, for example, in Rictor null cells, where Akt phosphorylation on Ser473 is reduced, S6 phosphor ylation was normal. Moreover, treating cells with the Akt pathway inhibitor triciribine completely abolished Akt phosphorylation, but had no impact on PDGF BB promoted S6 phosphorylation. This is consistent with a study in Drosophila showing that Akt phosphorylation of TSC2 is not required for mTOR activation, but in contrast to studies on insulin signaling, where it was shown that Akt phosphorylation of TSC2 is necessary for mTORC1 activation. We observed inhibition of S6 phosphorylation after treatment with Ca2 chelators.
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