Work

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

Year: 2015

Type: article

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.

Source: Aging Cell

DOI: 10.1111/acel.12258

Authors: Ian Gibbs-Seymour, Ewa Markiewicz, Simon Bekker-Jensen, Niels Mailand, Christopher J. Hutchison

Institutions: University of Copenhagen, Durham University, Novo Nordisk Foundation

Language: English

Topic: Nuclear Structure and Function

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: gold

Estimated APC paid: $2,482