CHFR is important for the first wave of ubiquitination at DNA damage sites.
Protein ubiquitination plays an important role in activating the DNA damage response and maintaining genomic stability. In response to DNA double-strand breaks (DSBs), a ubiquitination cascade occurs at DNA lesions. Here, we show that checkpoint with Forkhead-associated (FHA) and RING finger domain protein (CHFR), an E3 ubiquitin ligase, is recruited ... to DSBs by poly(ADP-ribose) (PAR). At DSBs, CHFR regulates the first wave of protein ubiquitination. Moreover, CHFR ubiquitinates PAR polymerase 1 (PARP1) and regulates chromatin-associated PARP1 in vivo. Thus, these results demonstrate that CHFR is an important E3 ligase in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation.
Mesh Terms:
Animals, Cell Cycle Proteins, Cell Line, Cells, Cultured, DNA Damage, DNA Repair, Humans, Lasers, Mice, Neoplasm Proteins, Poly Adenosine Diphosphate Ribose, Poly(ADP-ribose) Polymerases, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Ubiquitination
Animals, Cell Cycle Proteins, Cell Line, Cells, Cultured, DNA Damage, DNA Repair, Humans, Lasers, Mice, Neoplasm Proteins, Poly Adenosine Diphosphate Ribose, Poly(ADP-ribose) Polymerases, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Ubiquitination
Nucleic Acids Res.
Date: Feb. 01, 2013
PubMed ID: 23268447
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