ArticleChannels (Austin, Tex.)
Acid sensitive background potassium channels K2P3.1 and K2P9.1 undergo rapid dynamin-dependent endocytosis.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- Dynamic regulation of TASK-1 channels under cellular stress.The journal of physiological sciences : JPS · 2026Article
- Fluvastatin inhibits Rab5-mediated IKs internalization caused by chronic CaJournal of molecular and cellular cardiology · 2019Article
- Endocytosis as a mode to regulate functional expression of two-pore domain potassium (K₂p) channels.Pflugers Archiv : European journal of physiology · 2015Review
- Cooperative endocytosis of the endosomal SNARE protein syntaxin-8 and the potassium channel TASK-1.Molecular biology of the cell · 2014Article
- Ion channels under the sun.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
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Authors and funding
3 authors at 2 institutions in 3 countries.
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Abstract
Acid-sensitive, two-pore domain potassium channels, K(2P)3.1 and K(2P)9.1, are implicated in cardiac and nervous tissue responses to hormones, neurotransmitters and drugs. K(2P)3.1 and K(2P)9.1 leak potassium from the cell at rest and directly impact membrane potential. Hence altering channel number on the cell surface drives changes in cellular electrical properties. The rate of K(2P)3.1 and K(2P)9.1 delivery to and recovery from the plasma membrane determines both channel number at the cell surface and potassium leak from cells. This study examines the endocytosis of K(2P)3.1 and K(2P)9.1. Plasma membrane biotinylation was used to follow the fate of internalized GFP-tagged rat K(2P)3.1 and K(2P)9.1 transiently expressed in HeLa cells. Confocal fluorescence images were analyzed using Imaris software, which revealed that both channels are endocytosed by a dynamin-dependent mechanism and over the course of 60 min, move progressively toward the nucleus. Endogenous endocytosis of human K(2P)3.1 and K(2P)9.1 was examined in the lung carcinoma cell line, A549. Endogenous channels are endocytosed over a similar time-scale to the channels expressed transiently in HeLa cells. These findings both validate the use of recombinant systems and identify an endogenous model system in which K(2P)3.1 and K(2P)9.1 trafficking can be further studied.
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