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.
Originalsprog | Engelsk |
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Tidsskrift | Aging Cell |
Vol/bind | 14 |
Udgave nummer | 2 |
Sider (fra-til) | 162-9 |
Antal sider | 8 |
ISSN | 1474-9718 |
DOI | |
Status | Udgivet - apr. 2015 |