International audience
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April 12, 2016 (v1)Journal articleUploaded on: December 4, 2022
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April 12, 2016 (v1)Journal article
Significance Nearly 350 human genes encode ion channels. Posttranscriptional (alternative splicing, editing, and alternative translation initiation) and posttranslational mechanisms (glycosylation, phosphorylation) further increase diversity. For multimeric channels, various heteromeric combinations may raise the number of ion channels to...
Uploaded on: December 3, 2022 -
April 12, 2016 (v1)Journal article
International audience
Uploaded on: February 22, 2023 -
2022 (v1)Journal article
Two-pore domain K+ channels (K2P channels), active as dimers, produce inhibitory currents regulated by a variety of stimuli. Among them, TWIK1-related alkalinization-activated K+ channel 1 (TALK1), TWIK1-related alkalinization-activated K+ channel 2 (TALK2), and TWIK1-related acid-sensitive K+ channel 2 (TASK2) form a subfamily of structurally...
Uploaded on: December 4, 2022 -
September 4, 2018 (v1)Journal article
International audience
Uploaded on: December 4, 2022 -
September 4, 2018 (v1)Journal article
TREK/TRAAK channels are polymodal K+ channels that convert very diverse stimuli,including bioactive lipids, mechanical stretch and temperature, into electrical signals.The nature of the structural changes that regulate their activity remains an openquestion. Here, we show that a cytoplasmic domain (the proximal C-ter domain, pCt)exerts...
Uploaded on: December 4, 2022 -
September 4, 2018 (v1)Journal article
TREK/TRAAK channels are polymodal K+ channels that convert very diverse stimuli,including bioactive lipids, mechanical stretch and temperature, into electrical signals.The nature of the structural changes that regulate their activity remains an openquestion. Here, we show that a cytoplasmic domain (the proximal C-ter domain, pCt)exerts...
Uploaded on: February 22, 2023 -
February 15, 2019 (v1)Journal article
Mutations that modulate the activity of ion channels are essential tools to understand the biophysical determinants that control their gating. Here, we reveal the conserved role played by a single amino acid position (TM2.6) located in the second transmembrane domain of two-pore domain potassium (K2P) channels. Mutations of TM2.6 to aspartate...
Uploaded on: December 4, 2022