TASK Assays
Background of TASK
TASK channel and its three subunits belong to the K2p channel superfamily, they are sensitive to the changes in intracellular acidity and participate in the process of cell membrane potential polarization/depolarization. Disruption and disfunction of the Task channel often lead to severe respiratory, neurological diseases, or other clinical conditions.
Fig.1. Structure Prediction of the Human TASK-2. (Uniprot ID O95279; obtained from Alphafold)
Distributions and Functions of TASK
TASK channel is widely distributed in nerve cells and various excitable cells and is also abundantly expressed in the central nervous system, especially in the brainstem region. TASK channel contributes to the maintenance and regulation of membrane potential of adrenocortical and medullary cells, which in turn manipulates corticotropin-dependent stimulation of aldosterone and cortisol synthesis. At the same time, the TASK channel is also an important part of the brainstem respiratory control system, especially the pH sensing module.
Submembers and Mechanisms of TASK
TASK has three subunits, which are designated as TASK 1, TASK 2, and TASK 3.
| Channel | Gene | Mechanism | Activator | Blocker |
| TASK.1 | KCNK3 |
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| TASK.2 | KCNK5 | |||
| TASK.3 | KCNK9 |
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Assay List of TASK Channel
Creative Biolabs can provide a range of assays of TASK channels. You can choose the assay in the list or contact us for more information:
Published Data
| Paper Title | A direct interaction between cyclodextrins and TASK channels decreases the leak current in cerebellar granule neurons |
| Journal | Biology |
| Published | 2022 |
| Abstract | K2P channels are abundantly expressed in the nervous system and control the generation of neural excitability. K2P channels are regulated by multiple stimuli in vivo, including G protein, pH, mechanical force, activating enzymes, phospholipids, and protein interactions. Tight and precise regulation of K2P is key to fine-tuning the electrical properties of cells. In previous studies, the regulatory mechanism of TWIK-1, TASK-1, and TASK-3 heterodimers in cerebellar granule neurons (CGN) has been explored in depth, there is also evidence that the lipid environment may affect K2P ion channel activity by affecting plasma membrane biophysical properties, structural and/or functional regulation, or direct protein-lipid interactions. In this study, the researchers used immunocytochemistry, heterologous expression of K2P channels, and cholesterol-removal action to provide a link between K2P channel expression and its association in cultured rat cerebellar granule neurons (CGN) using specific lipid raft markers. In addition, the experiment also verified the coexistence of K2P channels and lipid RAFT protein markers. |
| Result |
In the experiment, TWIK-1, TRESK, and TASK channels were heterologously expressed in HEK293 cells, the expression of TWIK-1, TRESK, and TASK channels in primary cultured CGN and their relationship with lipid rafts were detected by immunocytochemistry, and observed changes in cell excitability under the stimulation of methyl β-cyclodextrin (MβCD). Data shows that MβCD directly blocks TASK-1 and TASK-3 channels as well as TASK-1/TASK-3 covalent cascade heterodimer currents. In contrast, MβCD did not affect K+ currents mediated by TWIK-1 and TRESK. This illustrates the effects of MβCD through direct interactions with TASK-1 and TASK-3 channels. Cholesterol depletion experiments ruled out a direct effect of cholesterol-lowering treatment on K2P channel function. Collectively, neuronal K2P channels interact with lipid rafts and likely share the same lipid raft association structure core, but their functional activity is independent of the membrane composition and organization of cholesterol domains.
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Fig.2. Staining of K2P channel and flotillin-2. (Zuniga, 2022)
Reference
- Zuniga, R.; et al. A direct interaction between cyclodextrins and TASK channels decreases the leak current in cerebellar granule neurons. Biology. 2022, 11: 1097.
