Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage. / Gibbs-Seymour, Ian; Markiewicz, Ewa; Bekker-Jensen, Simon; Mailand, Niels; Hutchison, Christopher J.

In: Aging Cell, Vol. 14, No. 2, 04.2015, p. 162-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Gibbs-Seymour, I, Markiewicz, E, Bekker-Jensen, S, Mailand, N & Hutchison, CJ 2015, 'Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage', Aging Cell, vol. 14, no. 2, pp. 162-9. https://doi.org/10.1111/acel.12258

APA

Gibbs-Seymour, I., Markiewicz, E., Bekker-Jensen, S., Mailand, N., & Hutchison, C. J. (2015). Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage. Aging Cell, 14(2), 162-9. https://doi.org/10.1111/acel.12258

Vancouver

Gibbs-Seymour I, Markiewicz E, Bekker-Jensen S, Mailand N, Hutchison CJ. Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage. Aging Cell. 2015 Apr;14(2):162-9. https://doi.org/10.1111/acel.12258

Author

Gibbs-Seymour, Ian ; Markiewicz, Ewa ; Bekker-Jensen, Simon ; Mailand, Niels ; Hutchison, Christopher J. / Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage. In: Aging Cell. 2015 ; Vol. 14, No. 2. pp. 162-9.

Bibtex

@article{c0101919a4844ff9811428ab4a706bce,
title = "Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage",
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.",
author = "Ian Gibbs-Seymour and Ewa Markiewicz and Simon Bekker-Jensen and Niels Mailand and Hutchison, {Christopher J}",
note = "{\textcopyright} 2014 The Authors. Aging Cell published by the Anatomical Society and John Wiley & Sons Ltd.",
year = "2015",
month = apr,
doi = "10.1111/acel.12258",
language = "English",
volume = "14",
pages = "162--9",
journal = "Aging Cell",
issn = "1474-9718",
publisher = "Wiley-Blackwell",
number = "2",

}

RIS

TY - JOUR

T1 - Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage

AU - Gibbs-Seymour, Ian

AU - Markiewicz, Ewa

AU - Bekker-Jensen, Simon

AU - Mailand, Niels

AU - Hutchison, Christopher J

N1 - © 2014 The Authors. Aging Cell published by the Anatomical Society and John Wiley & Sons Ltd.

PY - 2015/4

Y1 - 2015/4

N2 - 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.

AB - 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.

U2 - 10.1111/acel.12258

DO - 10.1111/acel.12258

M3 - Journal article

C2 - 25645366

VL - 14

SP - 162

EP - 169

JO - Aging Cell

JF - Aging Cell

SN - 1474-9718

IS - 2

ER -

ID: 139975416