- Title
- Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage
- Creator
- Gibbs-Seymour, Ian; Markiewicz, Ewa; Bekker-Jensen, Simon; Mailand, Niels; Hutchison, Chris
- Date
- 2015
- Type
- Text; Journal article
- Identifier
- http://researchonline.federation.edu.au/vital/access/HandleResolver/1959.17/170796
- Identifier
- vital:14209
- Identifier
-
https://doi.org/10.1111/acel.12258
- Identifier
- ISBN:1474-9718
- Abstract
- Lamins A/C have been implicated in DNA damage response pathways. We show that the DNA repair protein 53BP1 is a lamin A/C binding protein. In undamaged human dermal fibroblasts (HDF), 53BP1 is a nucleoskeleton protein. 53BP1 binds to lamins A/C via its Tudor domain, and this is abrogated by DNA damage. Lamins A/C regulate 53BP1 levels and consequently lamin A/C-null HDF display a 53BP1 null-like phenotype. Our data favour a model in which lamins A/C maintain a nucleoplasmic pool of 53BP1 in order to facilitate its rapid recruitment to sites of DNA damage and could explain why an absence of lamin A/C accelerates aging. © 2014 The Authors. Aging Cell published by the Anatomical Society and John Wiley & Sons Ltd.
- Publisher
- Blackwell Publishing Ltd
- Relation
- Aging Cell Vol. 14, no. 2 (2015), p. 162-169
- Rights
- http://creativecommons.org/licenses/by-nc-nd/4.0/
- Rights
- Copyright This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Rights
- Open Access
- Rights
- This metadata is freely available under a CCO license
- Subject
- 53BP1; DNA damage response; Laminopathy; Lamins; 53BP1 protein; Benzyloxycarbonylleucylleucylleucinal; Binding protein; Cathepsin L; Deoxyribonuclease I; Lamin A; Lamin C; Unclassified drug; LMNA protein, human; Protein binding; Signal peptide; TP53BP1 protein, human; Carboxy terminal sequence; Cell cycle arrest; Cell survival; Chromatin; Controlled study; DNA damage; DNA repair; Fluorescence microscopy; Economic instability; Heterochromatin; Human; Human cell; Immunoprecipitation; Ionizing radiation; Nuclear lamina; Null cell; Oligomerization; Phenotype; Priority journal; Protein depletion; Protein expression; Protein phosphorylation; Protein protein interaction; Skin fibroblast; U2OS cell line; Cytology; Fibroblast; Genetics; HEK293 cell line; Metabolism; Physiology; Protein tertiary structure; Tumor cell line; Cell Line, Tumor; Fibroblasts; HEK293 Cells; Humans; Intracellular Signaling Peptides and Proteins; Lamin Type A; Protein Structure, Tertiary
- Full Text
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