Ubiquitin Phosphorylation at Thr12 Modulates the DNA Damage Response

The ubiquitin system regulates the DNA damage response (DDR) by modifying histone H2A at Lys15 (H2AK15ub) and triggering downstream signaling events. Here, we find that phosphorylation of ubiquitin at Thr12 (pUbT12) controls the DDR by inhibiting the function of 53BP1, a key factor for DNA double-st...

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Veröffentlicht in:	Molecular cell Jg. 80; H. 3; S. 423
Hauptverfasser:	Walser, Franziska, Mulder, Monique P C, Bragantini, Benoît, Burger, Sibylle, Gubser, Tatiana, Gatti, Marco, Botuyan, Maria Victoria, Villa, Alessandra, Altmeyer, Matthias, Neri, Dario, Ovaa, Huib, Mer, Georges, Penengo, Lorenza
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	United States 05.11.2020
Schlagworte:	Animals Cell Line Cell Line, Tumor Chromatin - metabolism DNA - metabolism DNA Breaks, Double-Stranded DNA Damage - genetics DNA Damage - physiology DNA End-Joining Repair - genetics DNA Repair - genetics DNA-Binding Proteins - metabolism Histones - metabolism Homologous Recombination - physiology Humans Intracellular Signaling Peptides and Proteins - metabolism Nuclear Proteins - metabolism Phosphorylation Signal Transduction - genetics Threonine - metabolism Tumor Suppressor p53-Binding Protein 1 - metabolism Tumor Suppressor p53-Binding Protein 1 - physiology Ubiquitin - genetics Ubiquitin - metabolism Ubiquitin-Protein Ligases - metabolism Ubiquitination H2AK15pUbT12 genome stability pUbT12 BRCA1/BARD1 DNA damage response phospho-ubiquitin Thr12 53BP1 RNF8 chromatin ubiquitination DNA repair RNF168 DDR RAD51 RNF169 histone mark H2AK15ub ubiquitin phosphorylation USP51
ISSN:	1097-4164, 1097-4164
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