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Acid sensitive background potassium channels K2p3.1 and K2p9.1 undergo rapid dynamin-dependent endocytosis

Acid sensitive background potassium channels K2p3.1 and K2p9.1 undergo rapid dynamin-dependent endocytosis
Acid sensitive background potassium channels K2p3.1 and K2p9.1 undergo rapid dynamin-dependent endocytosis
Acid-sensitive, two-pore domain potassium channels, K2p3.1 and K2p9.1, are implicated in cardiac and nervous tissue responses to hormones, neurotransmitters and drugs. K2p3.1 and K2p9.1 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 K2p3.1 and K2p9.1 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 K2p3.1 and K2p9.1. Plasma membrane biotinylation was used to follow the fate of internalized GFP-tagged rat K2p3.1 and K2p9.1 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 K2p3.1 and K2p9.1 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 K2p3.1 and K2p9.1 trafficking can be further studied.
imaris, K2p channel, task, caveolin, clathrin, dynamin, endocytosis, potassium channel, recycling
1933-6950
288-302
Mant, Alexandra
63319e45-deeb-45ad-a30d-e05b42052a0d
Williams, Sarah
f98f47db-b1d6-42c2-b0eb-7c0cb9a981d0
O'Kelly, Ita
e640f28a-42f0-48a6-9ce2-cb5a85d08c66
Mant, Alexandra
63319e45-deeb-45ad-a30d-e05b42052a0d
Williams, Sarah
f98f47db-b1d6-42c2-b0eb-7c0cb9a981d0
O'Kelly, Ita
e640f28a-42f0-48a6-9ce2-cb5a85d08c66

Mant, Alexandra, Williams, Sarah and O'Kelly, Ita (2013) Acid sensitive background potassium channels K2p3.1 and K2p9.1 undergo rapid dynamin-dependent endocytosis. Channels, 7 (4), 288-302. (doi:10.4161/chan.25120). (PMID:23807092)

Record type: Article

Abstract

Acid-sensitive, two-pore domain potassium channels, K2p3.1 and K2p9.1, are implicated in cardiac and nervous tissue responses to hormones, neurotransmitters and drugs. K2p3.1 and K2p9.1 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 K2p3.1 and K2p9.1 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 K2p3.1 and K2p9.1. Plasma membrane biotinylation was used to follow the fate of internalized GFP-tagged rat K2p3.1 and K2p9.1 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 K2p3.1 and K2p9.1 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 K2p3.1 and K2p9.1 trafficking can be further studied.

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e-pub ahead of print date: 10 June 2013
Published date: July 2013
Keywords: imaris, K2p channel, task, caveolin, clathrin, dynamin, endocytosis, potassium channel, recycling
Organisations: Human Development & Health

Identifiers

Local EPrints ID: 352365
URI: http://eprints.soton.ac.uk/id/eprint/352365
ISSN: 1933-6950
PURE UUID: 1ee696af-a8cf-40b0-8cd3-76f801cab348
ORCID for Alexandra Mant: ORCID iD orcid.org/0000-0001-7169-209X

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Date deposited: 13 May 2013 10:36
Last modified: 28 Oct 2023 01:53

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Contributors

Author: Alexandra Mant ORCID iD
Author: Sarah Williams
Author: Ita O'Kelly

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