The Ubiquitin Ligase Adaptor NDFIP1 Interacts with TRESK and Negatively Regulates the Background K Current.

The TRESK (K2P18.1, KCNK18) background potassium channel is expressed in primary sensory neurons and has been reported to contribute to the regulation of pain sensations. In the present study, we examined the interaction of TRESK with NDFIP1 (Nedd4 family-interacting protein 1) in the oocyte expression system by two-electrode voltage clamp and biochemical methods.

Critical contribution of the intracellular C-terminal region to TRESK channel activity is revealed by the epithelial Na current ratio method.

TRESK (K18.1) possesses unique structural proportions within the K background potassium channel family. The previously described TRESK regulatory mechanisms are based on the long intracellular loop between the second and the third transmembrane segments (TMS).

Translocation of TMEM175 Lysosomal Potassium Channel to the Plasma Membrane by Dynasore Compounds.

TMEM175 (transmembrane protein 175) coding sequence variants are associated with increased risk of Parkinson's disease. TMEM175 is the ubiquitous lysosomal K channel regulated by growth factor receptor signaling and direct interaction with protein kinase B (PKB/Akt). In the present study, we show that the expression of mouse TMEM175 results in very small K currents through the plasma membrane in oocytes, in good accordance with the previously reported intracellular localization of the channel.

Tubulin binds to the cytoplasmic loop of TRESK background K⁺ channel in vitro.

The cytoplasmic loop between the second and third transmembrane segments is pivotal in the regulation of TRESK (TWIK-related spinal cord K+ channel, K2P18.1, KCNK18). Calcineurin binds to this region and activates the channel by dephosphorylation in response to the calcium signal.