期刊
AGING CELL
卷 14, 期 2, 页码 162-169出版社
WILEY
DOI: 10.1111/acel.12258
关键词
53BP1; DNA damage response; lamins; laminopathy
资金
- Association for International Cancer Research
- Novo Nordisk Foundation
- Danish Medical Research Council
- Danish Cancer Society
- Lundbeck Foundation
- BBSRC [be/ko19760/1]
- Novo Nordisk Foundation Center for Protein Research [PI Niels Mailand] Funding Source: researchfish
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据