Modulation of TASK-1 (Kcnk3) and TASK-3 (Kcnk9) Potassium Channels

@article{Talley2002ModulationOT,
  title={Modulation of TASK-1 (Kcnk3) and TASK-3 (Kcnk9) Potassium Channels},
  author={Edmund M. Talley and Douglas A. Bayliss},
  journal={The Journal of Biological Chemistry},
  year={2002},
  volume={277},
  pages={17733 - 17742}
}
TASK-1 and TASK-3, members of the two-pore-domain channel family, are widely expressed leak potassium channels responsible for maintenance of cell membrane potential and input resistance. They are sites of action for a variety of modulatory agents, including volatile anesthetics and neurotransmitters/hormones, the latter acting via mechanisms that have remained elusive. To clarify these mechanisms, we generated mutant channels and found that alterations disrupting anesthetic (halothane… Expand
Gαq-Mediated Regulation of TASK3 Two-Pore Domain Potassium Channels: The Role of Protein Kinase C
The TASK subfamily of two pore domain potassium channels (K2P) gives rise to leak potassium currents, which contribute to the resting membrane potential of many neurons and regulate theirExpand
A Small-Molecule Compound Selectively Activates K2P Channel TASK-3 by Acting at Two Distant Clusters of Residues
TLDR
N-(2-((4-nitro-2-(trifluoromethyl)phenyl)amino)ethyl)benzamide (NPBA) showed excellent potency and selectivity as a novel TASK-3 activator and it is shown that NPBA is a more potent activator than terbinafine, the only reported TASk-3 selective activator to date. Expand
Ruthenium red inhibits TASK-3 potassium channel by interconnecting glutamate 70 of the two subunits.
TLDR
The results indicate that RR inhibits TASK-3 by tethering its two subunits and identify amino acid 70 as a possible target for designing selective inhibitors against the different TASk channels. Expand
Covalent Modification of a Volatile Anesthetic Regulatory Site Activates TASK-3 (KCNK9) Tandem-Pore Potassium Channels
TLDR
The data suggest that volatile anesthetics, through perturbations at a single site, increase TASK-3 channel activity and disrupt its regulation by active Gαq protein, a determinant of central nervous system arousal and consciousness. Expand
TASK channels: channelopathies, trafficking, and receptor-mediated inhibition
TLDR
It is likely that a raft membrane domain is a platform where TASK1 is located and the signaling molecules protein kinase C, Pyk2, and Src are recruited in sequence in response to GPCR stimulation. Expand
Two-Pore-Domain (Kcnk) Potassium Channels: Dynamic Roles in Neuronal Function
TLDR
Multiple roles that modulation of leak K+ channels play in CNS function are described and evidence that members of the two-pore-domain family are molecular substrates for these processes are discussed. Expand
Molecular Pharmacology of K2P Potassium Channels.
TLDR
The differential binding sites and mechanisms of channel modulation that are utilized by the different K2P channel blockers and activators are described. Expand
The generation and the characterization of the TASK-3 knockout mice
TLDR
The expression of TasK-1 and TASK-3 genes in the adult mouse brain is analyzed to understand the role of TASk-3 in the K+ leak conductance and in neuronal excitability and to investigate possible compensatory mechanisms. Expand
The response of the tandem pore potassium channel TASK-3 (K2P9.1) to voltage: gating at the cytoplasmic mouth
TLDR
A simple kinetic model is developed to show how gating occurs through two classes of conformation change, with two routes out of the open state, as expected if gating occurring both at the selectivity filter and at its cytoplasmic mouth. Expand
Diacylglycerol mediates regulation of TASK potassium channels by Gq-coupled receptors.
TLDR
DAG is identified as the signal regulating TASK channels downstream of GPCRs and a novel role for DAG is defined that directly links cellular DAG dynamics to excitability. Expand
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