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Filamin C: a novel component of the KCNE2 interactome during hypoxia
AIM: KCNE2 encodes for the potassium voltage-gated channel, KCNE2. Mutations in KCNE2 have been associated with long-QT syndrome (LQTS). While KCNE2 has been extensively studied, the functions of its C-terminal domain remain inadequately described. Here, we aimed to elucidate the functions of this d...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Clinics Cardive Publishing
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4816932/ https://www.ncbi.nlm.nih.gov/pubmed/26956495 http://dx.doi.org/10.5830/CVJA-2015-049 |
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author | Neethling, Annika Mouton, Jomien Corfield, Valerie de Villiers, Carin Kinnear, Craig Loos, Ben |
author_facet | Neethling, Annika Mouton, Jomien Corfield, Valerie de Villiers, Carin Kinnear, Craig Loos, Ben |
author_sort | Neethling, Annika |
collection | PubMed |
description | AIM: KCNE2 encodes for the potassium voltage-gated channel, KCNE2. Mutations in KCNE2 have been associated with long-QT syndrome (LQTS). While KCNE2 has been extensively studied, the functions of its C-terminal domain remain inadequately described. Here, we aimed to elucidate the functions of this domain by identifying its protein interactors using yeast two-hybrid analysis. METHODS: The C-terminal domain of KCNE2 was used as bait to screen a human cardiac cDNA library for putative interacting proteins. Co-localisation and co-immunoprecipitation analyses were used for verification. RESULTS: Filamin C (FLNC) was identified as a putative interactor with KCNE2. FLNC and KCNE2 co-localised within the cell, however, a physical interaction was only observed under hypoxic conditions. CONCLUSION: The identification of FLNC as a novel KCNE2 ligand not only enhances current understanding of ion channel function and regulation, but also provides valuable information about possible pathways likely to be involved in LQTS pathogenesis. |
format | Online Article Text |
id | pubmed-4816932 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Clinics Cardive Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-48169322016-04-22 Filamin C: a novel component of the KCNE2 interactome during hypoxia Neethling, Annika Mouton, Jomien Corfield, Valerie de Villiers, Carin Kinnear, Craig Loos, Ben Cardiovasc J Afr Cardiovascular Topics AIM: KCNE2 encodes for the potassium voltage-gated channel, KCNE2. Mutations in KCNE2 have been associated with long-QT syndrome (LQTS). While KCNE2 has been extensively studied, the functions of its C-terminal domain remain inadequately described. Here, we aimed to elucidate the functions of this domain by identifying its protein interactors using yeast two-hybrid analysis. METHODS: The C-terminal domain of KCNE2 was used as bait to screen a human cardiac cDNA library for putative interacting proteins. Co-localisation and co-immunoprecipitation analyses were used for verification. RESULTS: Filamin C (FLNC) was identified as a putative interactor with KCNE2. FLNC and KCNE2 co-localised within the cell, however, a physical interaction was only observed under hypoxic conditions. CONCLUSION: The identification of FLNC as a novel KCNE2 ligand not only enhances current understanding of ion channel function and regulation, but also provides valuable information about possible pathways likely to be involved in LQTS pathogenesis. Clinics Cardive Publishing 2016 /pmc/articles/PMC4816932/ /pubmed/26956495 http://dx.doi.org/10.5830/CVJA-2015-049 Text en Copyright © 2015 Clinics Cardive Publishing http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Cardiovascular Topics Neethling, Annika Mouton, Jomien Corfield, Valerie de Villiers, Carin Kinnear, Craig Loos, Ben Filamin C: a novel component of the KCNE2 interactome during hypoxia |
title | Filamin C: a novel component of the KCNE2 interactome during hypoxia |
title_full | Filamin C: a novel component of the KCNE2 interactome during hypoxia |
title_fullStr | Filamin C: a novel component of the KCNE2 interactome during hypoxia |
title_full_unstemmed | Filamin C: a novel component of the KCNE2 interactome during hypoxia |
title_short | Filamin C: a novel component of the KCNE2 interactome during hypoxia |
title_sort | filamin c: a novel component of the kcne2 interactome during hypoxia |
topic | Cardiovascular Topics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4816932/ https://www.ncbi.nlm.nih.gov/pubmed/26956495 http://dx.doi.org/10.5830/CVJA-2015-049 |
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