IndraLab
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"Previous studies indicated that EGF activated phosphatidylinositol 3‐kinase (PI3K). xref PI3K is able to phosphorylate AKT1, thus in turn activating cyclin D1 pathway. xref , xref The data presented here show that EGF indeed increased AKT1 phosphorylation without affecting total AKT1 protein levels (Figure xref )."
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"As kinase activation and inhibition has previously been associated with the regulation of the subcellular localisation of huntingtin [XREF_BIBR - XREF_BIBR], we investigated whether the differential responses in AKT1 and MEK1 phosphorylation following EGF stimulation could be reflected in the subcellular localisation of huntingtin."
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"Interestingly, EGF triggers AKT1 phosphorylation via more rapid kinetics than those induced by androgens; this was recently documented by studies on the sensitivity of EGFR family proteins to disruptions in cholesterol synthesis and homeostasis, supporting the functional significance of EGF signal transduction through lipid rafts."
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"As EGF stimulation elicited AKT1 phosphorylation and altered the subcellular localisation of amino-terminal huntingtin in both StHdh Q111 and primary Hdh Q111 cell lines, we sought to investigate whether the phosphorylation of AKT1 may be a mechanism that regulates huntingtin subcellular localisation."