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KCNE Regulation of K(+) Channel Trafficking – a Sisyphean Task?

Voltage-gated potassium (Kv) channels shape the action potentials of excitable cells and regulate membrane potential and ion homeostasis in excitable and non-excitable cells. With 40 known members in the human genome and a variety of homomeric and heteromeric pore-forming α subunit interactions, pos...

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Detalles Bibliográficos
Autores principales: Kanda, Vikram A., Abbott, Geoffrey W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Research Foundation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3385356/
https://www.ncbi.nlm.nih.gov/pubmed/22754540
http://dx.doi.org/10.3389/fphys.2012.00231
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author Kanda, Vikram A.
Abbott, Geoffrey W.
author_facet Kanda, Vikram A.
Abbott, Geoffrey W.
author_sort Kanda, Vikram A.
collection PubMed
description Voltage-gated potassium (Kv) channels shape the action potentials of excitable cells and regulate membrane potential and ion homeostasis in excitable and non-excitable cells. With 40 known members in the human genome and a variety of homomeric and heteromeric pore-forming α subunit interactions, post-translational modifications, cellular locations, and expression patterns, the functional repertoire of the Kv α subunit family is monumental. This versatility is amplified by a host of interacting proteins, including the single membrane-spanning KCNE ancillary subunits. Here, examining both the secretory and the endocytic pathways, we review recent findings illustrating the surprising virtuosity of the KCNE proteins in orchestrating not just the function, but also the composition, diaspora and retrieval of channels formed by their Kv α subunit partners.
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spelling pubmed-33853562012-07-02 KCNE Regulation of K(+) Channel Trafficking – a Sisyphean Task? Kanda, Vikram A. Abbott, Geoffrey W. Front Physiol Physiology Voltage-gated potassium (Kv) channels shape the action potentials of excitable cells and regulate membrane potential and ion homeostasis in excitable and non-excitable cells. With 40 known members in the human genome and a variety of homomeric and heteromeric pore-forming α subunit interactions, post-translational modifications, cellular locations, and expression patterns, the functional repertoire of the Kv α subunit family is monumental. This versatility is amplified by a host of interacting proteins, including the single membrane-spanning KCNE ancillary subunits. Here, examining both the secretory and the endocytic pathways, we review recent findings illustrating the surprising virtuosity of the KCNE proteins in orchestrating not just the function, but also the composition, diaspora and retrieval of channels formed by their Kv α subunit partners. Frontiers Research Foundation 2012-06-28 /pmc/articles/PMC3385356/ /pubmed/22754540 http://dx.doi.org/10.3389/fphys.2012.00231 Text en Copyright © 2012 Kanda and Abbott. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution Non Commercial License, which permits non-commercial use, distribution, and reproduction in other forums, provided the original authors and source are credited.
spellingShingle Physiology
Kanda, Vikram A.
Abbott, Geoffrey W.
KCNE Regulation of K(+) Channel Trafficking – a Sisyphean Task?
title KCNE Regulation of K(+) Channel Trafficking – a Sisyphean Task?
title_full KCNE Regulation of K(+) Channel Trafficking – a Sisyphean Task?
title_fullStr KCNE Regulation of K(+) Channel Trafficking – a Sisyphean Task?
title_full_unstemmed KCNE Regulation of K(+) Channel Trafficking – a Sisyphean Task?
title_short KCNE Regulation of K(+) Channel Trafficking – a Sisyphean Task?
title_sort kcne regulation of k(+) channel trafficking – a sisyphean task?
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3385356/
https://www.ncbi.nlm.nih.gov/pubmed/22754540
http://dx.doi.org/10.3389/fphys.2012.00231
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