PKC and AMPK regulation of Kv1.5 potassium channels

Martin Nybo Andersen; Lasse Skibsbye; Chuyi Tang; Frederic Petersen; Nanna MacAulay; Hanne Borger Rasmussen; Thomas Jespersen

doi:10.1080/19336950.2015.1036205

PKC and AMPK regulation of Kv1.5 potassium channels

Martin Nybo Andersen, Lasse Skibsbye, Chuyi Tang, Frederic Petersen, Nanna MacAulay, Hanne Borger Rasmussen, Thomas Jespersen

21 Citations (Scopus)

Abstract

The voltage-gated Kv1.5 potassium channel, conducting the ultra-rapid rectifier K(+) current (IKur), is regulated through several pathways. Here we investigate if Kv1.5 surface expression is controlled by the 2 kinases PKC and AMPK, using Xenopus oocytes, MDCK cells and atrial derived HL-1 cells. By confocal microscopy combined with electrophysiology we demonstrate that PKC activation reduces Kv1.5 current, through a decrease in membrane expressed channels. AMPK activation was found to decrease the membrane expression in MDCK cells, but not in HL-1 cells and was furthermore shown to be dependent on co-expression of Nedd4-2 in Xenopus oocytes. These results indicate that Kv1.5 channels are regulated by both kinases, although through different molecular mechanisms in different cell systems.

Original language	English
Journal	Channels (Austin)
Volume	9
Issue number	3
Pages (from-to)	121-8
Number of pages	8
ISSN	1933-6950
DOIs	https://doi.org/10.1080/19336950.2015.1036205
Publication status	Published - 1 Jan 2015

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title = "PKC and AMPK regulation of Kv1.5 potassium channels",

abstract = "The voltage-gated Kv1.5 potassium channel, conducting the ultra-rapid rectifier K(+) current (IKur), is regulated through several pathways. Here we investigate if Kv1.5 surface expression is controlled by the 2 kinases PKC and AMPK, using Xenopus oocytes, MDCK cells and atrial derived HL-1 cells. By confocal microscopy combined with electrophysiology we demonstrate that PKC activation reduces Kv1.5 current, through a decrease in membrane expressed channels. AMPK activation was found to decrease the membrane expression in MDCK cells, but not in HL-1 cells and was furthermore shown to be dependent on co-expression of Nedd4-2 in Xenopus oocytes. These results indicate that Kv1.5 channels are regulated by both kinases, although through different molecular mechanisms in different cell systems.",

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T1 - PKC and AMPK regulation of Kv1.5 potassium channels

AU - Andersen, Martin Nybo

AU - Skibsbye, Lasse

AU - Tang, Chuyi

AU - Petersen, Frederic

AU - MacAulay, Nanna

AU - Rasmussen, Hanne Borger

AU - Jespersen, Thomas

PY - 2015/1/1

Y1 - 2015/1/1

N2 - The voltage-gated Kv1.5 potassium channel, conducting the ultra-rapid rectifier K(+) current (IKur), is regulated through several pathways. Here we investigate if Kv1.5 surface expression is controlled by the 2 kinases PKC and AMPK, using Xenopus oocytes, MDCK cells and atrial derived HL-1 cells. By confocal microscopy combined with electrophysiology we demonstrate that PKC activation reduces Kv1.5 current, through a decrease in membrane expressed channels. AMPK activation was found to decrease the membrane expression in MDCK cells, but not in HL-1 cells and was furthermore shown to be dependent on co-expression of Nedd4-2 in Xenopus oocytes. These results indicate that Kv1.5 channels are regulated by both kinases, although through different molecular mechanisms in different cell systems.

AB - The voltage-gated Kv1.5 potassium channel, conducting the ultra-rapid rectifier K(+) current (IKur), is regulated through several pathways. Here we investigate if Kv1.5 surface expression is controlled by the 2 kinases PKC and AMPK, using Xenopus oocytes, MDCK cells and atrial derived HL-1 cells. By confocal microscopy combined with electrophysiology we demonstrate that PKC activation reduces Kv1.5 current, through a decrease in membrane expressed channels. AMPK activation was found to decrease the membrane expression in MDCK cells, but not in HL-1 cells and was furthermore shown to be dependent on co-expression of Nedd4-2 in Xenopus oocytes. These results indicate that Kv1.5 channels are regulated by both kinases, although through different molecular mechanisms in different cell systems.

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DO - 10.1080/19336950.2015.1036205

M3 - Letter

C2 - 26043299

SN - 1933-6950

VL - 9

SP - 121

EP - 128

JO - Channels (Austin)

JF - Channels (Austin)

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ER -

PKC and AMPK regulation of Kv1.5 potassium channels

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