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

Research output: Contribution to journalJournal articleResearchpeer-review

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.

Original languageEnglish
JournalAging Cell
Issue number2
Pages (from-to)162-9
Number of pages8
Publication statusPublished - Apr 2015

ID: 139975416