Cyclic AMP-Dependent Regulation of Kv7 Voltage-Gated Potassium Channels.

Jennifer Van Der Horst,Thomas A Jepps,Iain A Greenwood

doi:10.3389/fphys.2020.00727

Jennifer Van Der Horst, Thomas A Jepps + Show 1 more

Open Access

https://doi.org/10.3389/fphys.2020.00727

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Abstract

Voltage-gated Kv7 potassium channels, encoded by KCNQ genes, have major physiological impacts cardiac myocytes, neurons, epithelial cells, and smooth muscle cells. Cyclic adenosine monophosphate (cAMP), a well-known intracellular secondary messenger, can activate numerous downstream effector proteins, generating downstream signaling pathways that regulate many functions in cells. A role for cAMP in ion channel regulation has been established, and recent findings show that cAMP signaling plays a role in Kv7 channel regulation. Although cAMP signaling is recognized to regulate Kv7 channels, the precise molecular mechanism behind the cAMP-dependent regulation of Kv7 channels is complex. This review will summarize recent research findings that support the mechanisms of cAMP-dependent regulation of Kv7 channels.

Highlights

Kv7.5 can be phosphorylated and stimulated by protein kinase A (PKA) on serine 53 on the N-terminus (Brueggemann et al, 2018); it is still unclear whether the heterotetrameric Kv7.3/Kv7.5 channel found in neurones are regulated in the same way by Cyclic adenosine monophosphate (cAMP)
This study identified serine 53 on the Kv7.5 N-terminus to be responsible for the increased Kv7.5 currents in response to cAMP elevation, which could be a common mechanism for β adrenoceptor/cAMP activation of Kv7.5 channels in vascular smooth muscle cells
Depending on the isoforms expressed in a cell type, extracellular signals through G proteincoupled receptor (GPCR) activation can be integrated differently

Summary

Introduction

Cyclic adenosine monophosphate (cAMP), a well-known intracellular secondary messenger, can activate numerous downstream effector proteins, generating downstream signaling pathways that regulate many functions in cells. These studies conclude that AKAP protein yotiao has a crucial and complex regulatory role on the cAMP-dependent activity of IKs channels (see Figure 1A). Kv7.5 can be phosphorylated and stimulated by PKA on serine 53 on the N-terminus (Brueggemann et al, 2018); it is still unclear whether the heterotetrameric Kv7.3/Kv7.5 channel found in neurones are regulated in the same way by cAMP.

Results

Conclusion