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

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

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.

OriginalsprogEngelsk
TidsskriftAging Cell
Vol/bind14
Udgave nummer2
Sider (fra-til)162-9
Antal sider8
ISSN1474-9718
DOI
StatusUdgivet - apr. 2015

ID: 139975416