Rnf168 Reference Search Result - Rat Genome Database

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RGD ID	Title	Citation	Abstract	PubMed	Pub Date
11075792	Identification of RNF168 as a PML nuclear body regulator.	Shire K, etal., J Cell Sci. 2016 Feb 1;129(3):580-91. doi: 10.1242/jcs.176446. Epub 2015 Dec 16.	Promyelocytic leukemia (PML) protein forms the basis of PML nuclear bodies (PML NBs), which control many important processes. We have screened an shRNA library targeting ubiquitin pathway proteins for effects on PML NBs, and identified RNF8 and RNF168 DNA-damag ... (more) e response proteins as negative regulators of PML NBs. Additional studies confirmed that depletion of either RNF8 or RNF168 increased the levels of PML NBs and proteins, whereas overexpression induced loss of PML NBs. RNF168 partially localized to PML NBs through its UMI/MIU1 ubiquitin-interacting region and associated with NBs formed by any PML isoform. The association of RNF168 with PML NBs resulted in increased ubiquitylation and SUMO2 modification of PML. In addition, RNF168 was found to associate with proteins modified by SUMO2 and/or SUMO3 in a manner dependent on its ubiquitin-binding sequences, suggesting that hybrid SUMO-ubiquitin chains can be bound. In vitro assays confirmed that RNF168, preferentially, binds hybrid SUMO2-K63 ubiquitin chains compared with K63-ubiquitin chains or individual SUMO2. Our study identified previously unrecognized roles for RNF8 and RNF168 in the regulation of PML, and a so far unknown preference of RNF168 for hybrid SUMO-ubiquitin chains.	26675234	2016-05-01
11053345	USP11 Is a Negative Regulator to gammaH2AX Ubiquitylation by RNF8/RNF168.	Yu M, etal., J Biol Chem. 2016 Jan 8;291(2):959-67. doi: 10.1074/jbc.M114.624478. Epub 2015 Oct 27.	Ubiquitin modification at double strand breaks (DSB) sites is an essential regulator of signaling and repair. gammaH2AX extends from DSB sites and provides a platform for subsequent recruitment and amplification of DNA repair proteins and signaling factors. Here, we found that RNF8/RNF168 ... (more) t-weight:700;'>RNF168 ubiquitylates gammaH2AX. We identified that USP11 is a unique deubiquitylation enzyme for gammaH2AX. USP11 deubiquitylates gammaH2AX both in vivo and in vitro but not the canonical (ub)-K119-H2A and (ub)-K120-H2B in vitro, and USP11 ablation enhances the levels of gammaH2AX ubiquitylation. We also found that USP11 interacts with gammaH2AX both in vivo and in vitro. We found that 53BP1 and ubiquitin-conjugated proteins are misregulated to be retained longer and stronger at DSB sites after knockdown of USP11. We further found that cells are hypersensitive to gamma-irradiation after ablation of USP11. Together, our findings elucidate deeply and extensively the mechanism of RNF8/RNF168 and USP11 to maintain the proper status of ubiquitylation gammaH2AX to repair DSB.	26507658	2016-04-01