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The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration
The integrity of the genome is maintained by a host of surveillance and repair mechanisms that are pivotal for cellular function. The tumour suppressor protein p53 is a major component of the DNA damage response pathway and plays a vital role in the maintenance of cell-cycle checkpoints. Here we sho...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4855670/ https://www.ncbi.nlm.nih.gov/pubmed/27054339 http://dx.doi.org/10.1038/cddis.2016.91 |
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author | Hall, A E Lu, W-T Godfrey, J D Antonov, A V Paicu, C Moxon, S Dalmay, T Wilczynska, A Muller, P A J Bushell, M |
author_facet | Hall, A E Lu, W-T Godfrey, J D Antonov, A V Paicu, C Moxon, S Dalmay, T Wilczynska, A Muller, P A J Bushell, M |
author_sort | Hall, A E |
collection | PubMed |
description | The integrity of the genome is maintained by a host of surveillance and repair mechanisms that are pivotal for cellular function. The tumour suppressor protein p53 is a major component of the DNA damage response pathway and plays a vital role in the maintenance of cell-cycle checkpoints. Here we show that a microRNA, miR-486, and its host gene ankyrin-1 (ANK1) are induced by p53 following DNA damage. Strikingly, the cytoskeleton adaptor protein ankyrin-1 was induced over 80-fold following DNA damage. ANK1 is upregulated in response to a variety of DNA damage agents in a range of cell types. We demonstrate that miR-486-5p is involved in controlling G1/S transition following DNA damage, whereas the induction of the ankyrin-1 protein alters the structure of the actin cytoskeleton and sustains limited cell migration during DNA damage. Importantly, we found that higher ANK1 expression correlates with decreased survival in cancer patients. Thus, these observations highlight ANK1 as an important effector downstream of the p53 pathway. |
format | Online Article Text |
id | pubmed-4855670 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-48556702016-05-10 The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration Hall, A E Lu, W-T Godfrey, J D Antonov, A V Paicu, C Moxon, S Dalmay, T Wilczynska, A Muller, P A J Bushell, M Cell Death Dis Original Article The integrity of the genome is maintained by a host of surveillance and repair mechanisms that are pivotal for cellular function. The tumour suppressor protein p53 is a major component of the DNA damage response pathway and plays a vital role in the maintenance of cell-cycle checkpoints. Here we show that a microRNA, miR-486, and its host gene ankyrin-1 (ANK1) are induced by p53 following DNA damage. Strikingly, the cytoskeleton adaptor protein ankyrin-1 was induced over 80-fold following DNA damage. ANK1 is upregulated in response to a variety of DNA damage agents in a range of cell types. We demonstrate that miR-486-5p is involved in controlling G1/S transition following DNA damage, whereas the induction of the ankyrin-1 protein alters the structure of the actin cytoskeleton and sustains limited cell migration during DNA damage. Importantly, we found that higher ANK1 expression correlates with decreased survival in cancer patients. Thus, these observations highlight ANK1 as an important effector downstream of the p53 pathway. Nature Publishing Group 2016-04 2016-04-07 /pmc/articles/PMC4855670/ /pubmed/27054339 http://dx.doi.org/10.1038/cddis.2016.91 Text en Copyright © 2016 Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ Cell Death and Disease is an open-access journal published by Nature Publishing Group. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Original Article Hall, A E Lu, W-T Godfrey, J D Antonov, A V Paicu, C Moxon, S Dalmay, T Wilczynska, A Muller, P A J Bushell, M The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration |
title | The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration |
title_full | The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration |
title_fullStr | The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration |
title_full_unstemmed | The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration |
title_short | The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration |
title_sort | cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following dna damage and alters cell migration |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4855670/ https://www.ncbi.nlm.nih.gov/pubmed/27054339 http://dx.doi.org/10.1038/cddis.2016.91 |
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