James Maylie

TL;DR: The mechanism of calcium gating is studied and it is found that small-conductance calcium-activated potassium channels are not gated by calcium binding directly to the channel α-subunits, instead, the functional SK channels are heteromeric complexes with calmodulin, which is constitutively associated with the α- subunits in a calcium-independent manner.

TL;DR: Biophysical and pharmacological properties of hIK1, cloned from human pancreas, are consistent with native intermediate conductance calcium-activated potassium channels, including the erythrocyte Gardos channel.

TL;DR: Blocking SK channels facilitates the induction of long-term potentiation by enhancing NMDAR-dependent Ca2+ signals within dendritic spines, mediated by a feedback loop within the spine head.

TL;DR: Well-known for their roles in regulating somatic excitability in central neurons, SK channels are also expressed in the postsynaptic membrane of glutamatergic synapses, where their activation and regulated trafficking modulate synaptic transmission and the induction and expression of synaptic plasticity, thereby affecting learning and memory.

TL;DR: The structural basis for differences in the pharmacology of SK channels is investigated and it is found that two amino acid residues on either side of the deep pore are the primary determinants of sensitivity to apamin and differential block by d-tubocurarine.