TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes

Histone ubiquitylation is a prominent response to DNA double-strand breaks (DSBs), but how these modifications are confined to DNA lesions is not understood. Here, we show that TRIP12 and UBR5, two HECT domain ubiquitin E3 ligases, control accumulation of RNF168, a rate-limiting component of a pathw...

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Bibliographic Details
Published in:	Cell Vol. 150; no. 4; p. 697
Main Authors:	Gudjonsson, Thorkell, Altmeyer, Matthias, Savic, Velibor, Toledo, Luis, Dinant, Christoffel, Grøfte, Merete, Bartkova, Jirina, Poulsen, Maria, Oka, Yasuyoshi, Bekker-Jensen, Simon, Mailand, Niels, Neumann, Beate, Heriche, Jean-Karim, Shearer, Robert, Saunders, Darren, Bartek, Jiri, Lukas, Jiri, Lukas, Claudia
Format:	Journal Article
Language:	English
Published:	United States 17.08.2012
Subjects:	Alphapapillomavirus Carrier Proteins - metabolism Cell Line Cell Line, Tumor Chromatin - metabolism DNA Breaks, Double-Stranded DNA Repair Gene Silencing Humans Intracellular Signaling Peptides and Proteins - metabolism Neoplasms - metabolism Neoplasms - pathology Neoplasms - virology Papillomavirus Infections - metabolism Papillomavirus Infections - pathology Transcription, Genetic Tumor Suppressor p53-Binding Protein 1 Ubiquitin-Protein Ligases - metabolism Ubiquitination
ISSN:	1097-4172, 1097-4172
Online Access:	Get more information
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