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The KCTD family of proteins: structure, function, disease relevance
The family of potassium channel tetramerizationdomain (KCTD) proteins consists of 26 members with mostly unknown functions. The name of the protein family is due to the sequence similarity between the conserved N-terminal region of KCTD proteins and the tetramerization domain in some voltage-gated p...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3882106/ https://www.ncbi.nlm.nih.gov/pubmed/24268103 http://dx.doi.org/10.1186/2045-3701-3-45 |
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author | Liu, Zhepeng Xiang, Yaqian Sun, Guihong |
author_facet | Liu, Zhepeng Xiang, Yaqian Sun, Guihong |
author_sort | Liu, Zhepeng |
collection | PubMed |
description | The family of potassium channel tetramerizationdomain (KCTD) proteins consists of 26 members with mostly unknown functions. The name of the protein family is due to the sequence similarity between the conserved N-terminal region of KCTD proteins and the tetramerization domain in some voltage-gated potassium channels. Dozens of publications suggest that KCTD proteins have roles in various biological processes and diseases. In this review, we summarize the character of Bric-a-brack,Tram-track, Broad complex(BTB) of KCTD proteins, their roles in the ubiquitination pathway, and the roles of KCTD mutants in diseases. Furthermore, we review potential downstream signaling pathways and discuss future studies that should be performed. |
format | Online Article Text |
id | pubmed-3882106 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-38821062014-01-07 The KCTD family of proteins: structure, function, disease relevance Liu, Zhepeng Xiang, Yaqian Sun, Guihong Cell Biosci Review The family of potassium channel tetramerizationdomain (KCTD) proteins consists of 26 members with mostly unknown functions. The name of the protein family is due to the sequence similarity between the conserved N-terminal region of KCTD proteins and the tetramerization domain in some voltage-gated potassium channels. Dozens of publications suggest that KCTD proteins have roles in various biological processes and diseases. In this review, we summarize the character of Bric-a-brack,Tram-track, Broad complex(BTB) of KCTD proteins, their roles in the ubiquitination pathway, and the roles of KCTD mutants in diseases. Furthermore, we review potential downstream signaling pathways and discuss future studies that should be performed. BioMed Central 2013-11-24 /pmc/articles/PMC3882106/ /pubmed/24268103 http://dx.doi.org/10.1186/2045-3701-3-45 Text en Copyright © 2013 Liu et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Review Liu, Zhepeng Xiang, Yaqian Sun, Guihong The KCTD family of proteins: structure, function, disease relevance |
title | The KCTD family of proteins: structure, function, disease relevance |
title_full | The KCTD family of proteins: structure, function, disease relevance |
title_fullStr | The KCTD family of proteins: structure, function, disease relevance |
title_full_unstemmed | The KCTD family of proteins: structure, function, disease relevance |
title_short | The KCTD family of proteins: structure, function, disease relevance |
title_sort | kctd family of proteins: structure, function, disease relevance |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3882106/ https://www.ncbi.nlm.nih.gov/pubmed/24268103 http://dx.doi.org/10.1186/2045-3701-3-45 |
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