IndraLab

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KCNH2 inhibits Cyclin. 5 / 5
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"In this work, we demonstrate that stimulation of hERG1 promotes an ubiquitin-proteasome-dependent degradation of cyclin E2 in multiple breast cancer cell lines representing Luminal A, HER2+ and Trastuzumab resistant breast cancer cells."
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"Stimulation of hERG1 channel activity promotes a calcium dependent degradation of cyclin E2, but not cyclin E1, in breast cancer cells."
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"Interestingly, MG132 strongly inhibited the effect of NS1643 on cyclin E2, suggesting that that stimulation of hERG1 channel promotes degradation of cyclin E2 via the proteasome."
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"Altogether, our findings strongly suggest that stimulation of the hERG1 potassium channels in breast cancer cells induces a calcium dependent degradation of cyclin E2 via activation of an ubiquitin dependent proteasome pathway."
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"Altogether, our data suggests that stimulation of the hERG1 channel in breast cancer cells activates ubiquitin-proteasome-dependent degradation of cyclin E2 that is independent of GSK3-beta."
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