IndraLab

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PKC phosphorylates KCNQ1. 5 / 5
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"Our results suggest that the regulation of the KvLQT1 and MinK potassium channel via beta (3)-AR is substantially mediated by PKC phosphorylation of the KvLQT1 protein at its four C-terminal PKC phosphorylation sites."
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"Experiments in which the putative C-terminal PKC phosphorylation sites in the KvLQT1 protein were destroyed by site directed mutagenesis reduced the isoproterenol induced current to 27 +/-3,5% compared to control."
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"Human beta (3)-adrenoreceptors couple to KvLQT1 and MinK potassium channels in Xenopus oocytes via protein kinase C phosphorylation of the KvLQT1 protein."
12879210
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"Our results suggest that the regulation of the KvLQT1/MinK potassium channel via beta(3)-AR is substantially mediated by PKC phosphorylation of the KvLQT1 protein at its four C-terminal PKC phosphorylation sites."
12879210
reach
"In addition, it has been postulated that by directly phosphorylating four putative C-terminals PKC phosphorylation sites of KCNQ1, PKC increases the current amplitude [45]."
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