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 ORCID: https://orcid.org/0000-0003-4644-1816, Dalmay, T ORCID: https://orcid.org/0000-0003-1492-5429, Wilczynska, A, Muller, P A J and Bushell, M (2016) The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration. Cell Death & Disease, 7. ISSN 2041-4889

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Abstract

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.

Item Type:	Article
Uncontrolled Keywords:	sdg 3 - good health and well-being ,/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being
Faculty \ School:	Faculty of Science > School of Computing Sciences Faculty of Science Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Plant Sciences
Depositing User:	Pure Connector
Date Deposited:	29 Apr 2016 12:00
Last Modified:	22 Oct 2022 01:04
URI:	https://ueaeprints.uea.ac.uk/id/eprint/58502
DOI:	10.1038/cddis.2016.91

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