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Trafficking of neuronal two pore domain potassium channels.

Mathie, Alistair, Rees, Kathryn A., El Hachmane, Mickael F., Veale, Emma L. (2010) Trafficking of neuronal two pore domain potassium channels. Current Neuropharmacology, 8 (3). pp. 276-86. ISSN 1875-6190. (doi:10.2174/157015910792246146) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:38621)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.2174/157015910792246146

Abstract

The activity of two pore domain potassium (K2P) channels regulates neuronal excitability and cell firing. Post-translational regulation of K2P channel trafficking to the membrane controls the number of functional channels at the neuronal membrane affecting the functional properties of neurons. In this review, we describe the general features of K channel trafficking from the endoplasmic reticulum (ER) to the plasma membrane via the Golgi apparatus then focus on established regulatory mechanisms for K2P channel trafficking. We describe the regulation of trafficking of TASK channels from the ER or their retention within the ER and consider the competing hypotheses for the roles of the chaperone proteins 14-3-3, COP1 and p11 in these processes and where these proteins bind to TASK channels. We also describe the localisation of TREK channels to particular regions of the neuronal membrane and the involvement of the TREK channel binding partners AKAP150 and Mtap2 in this localisation. We describe the roles of other K2P channel binding partners including Arf6, EFA6 and SUMO for TWIK1 channels and Vpu for TASK1 channels. Finally, we consider the potential importance of K2P channel trafficking in a number of disease states such as neuropathic pain and cancer and the protection of neurons from ischemic damage. We suggest that a better understanding of the mechanisms and regulations that underpin the trafficking of K2P channels to the plasma membrane and to localised regions therein may considerably enhance the probability of future therapeutic advances in these areas.

Item Type: Article
DOI/Identification number: 10.2174/157015910792246146
Subjects: Q Science > QP Physiology (Living systems)
Divisions: Divisions > Division of Natural Sciences > Medway School of Pharmacy
Depositing User: Alistair Mathie
Date Deposited: 06 Mar 2014 17:06 UTC
Last Modified: 16 Nov 2021 10:14 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/38621 (The current URI for this page, for reference purposes)

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