Key result
Preventing palmitoylation at C243 of the human Kv1.1 channel by site-directed mutagenesis resulted in a 20-mV leftward shift in the current-voltage relationship.
Population
Sf9 cells expressing human Kv1.1 protein
Comparison
Site-directed mutagenesis preventing… vs Wild-type (WT) human Kv1.1 channels
Design
Preclinical
Authors
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No immediate clinical implications for channelopathies; leaves open whether C243 palmitoylation modulates excitability in vivo.
Effect estimate: 20-mV leftward shift
The study identifies palmitoylation at C243 as a mechanism for human Kv1.1 channel interactions with plasma membrane lipids, modulating voltage sensing, and defines a consensus sequence for protein palmitoylation.
Gubitosi‐Klug et al. (2005) studied this question. Site-directed mutagenesis preventing palmitoylation at C243 vs. Wild-type channels was evaluated on Current-voltage relationship (20-mV leftward shift). Preventing palmitoylation at C243 of the human Kv1.1 channel by site-directed mutagenesis resulted in a 20-mV leftward shift in the current-voltage relationship.
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