Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage
Copyright policy )Lamin A/C-dependent interaction with 53BP1 promotes cellular responses to DNA damage
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.
- University of Copenhagen Denmark
- Durham University United Kingdom
- University of copenhaguen Denmark
- Novo Nordisk (Denmark) Denmark
- University of Copenhagen Denmark
DNA Repair, Intracellular Signaling Peptides and Proteins, Original Articles, Fibroblasts, Lamin Type A, Protein Structure, Tertiary, HEK293 Cells, Cell Line, Tumor, Humans, Tumor Suppressor p53-Binding Protein 1, DNA Damage, Protein Binding
DNA Repair, Intracellular Signaling Peptides and Proteins, Original Articles, Fibroblasts, Lamin Type A, Protein Structure, Tertiary, HEK293 Cells, Cell Line, Tumor, Humans, Tumor Suppressor p53-Binding Protein 1, DNA Damage, Protein Binding
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