IndraLab

Statements

USP3 inhibits RNF168. 9 / 11
| 9
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"Similar to USP26 and USP37, two other DUBs, USP3 and USP44, were shown to reverse RNF168 induced chromatin ubiquitylation, thereby controlling the accumulation of BRCA1 and 53BP1 at sites of DNA damage."
26101254
reach
"By virtue of its ability to oppose histone H2A ubiquitylation and the fact that USP3 over-expression can block accumulation of the ubiquitin E3 ligase RNF168 at DSB sites, USP3 has been linked to the key RNF8-RNF168 pathway of assembling repair and signalling components at DSB sites [XREF_BIBR]."
23712866
reach
"The DUBs USP3, USP16, BRCC36, POH1, and OTUB1 are associated with negative regulation of the RNF8 pathway, with USP3 and USP16 being first linked to this pathway through their ability to oppose H2A ub[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
23416108
reach
"In this context, overexpression of wild-type USP3, but not its catalytically inactive mutant, prevented the IR induced focus formation of RNF168, emphasizing the requirement of UPS3 cysteine protease activity to reverse the DSB ubiquitin response at the level of RNF8 XREF_BIBR."
21056014
reach
"USP3: Antagonizing RNF8/RNF168 at H2A-Type Histones."
32708614
reach
"Overexpression of USP3, a deubiquitylating enzyme that reversed H2A ubiquitylation, as well as mutations in the UIM domains of RNF168, prevented the accumulation of RNF168 at DSBs."
19342239
reach
"By virtue of its ability to oppose histone H2A ubiquitylation and the fact that USP3 over-expression can block accumulation of the ubiquitin E3 ligase RNF168 at DSB sites, USP3 has been linked to the key RNF8–RNF168 pathway of assembling repair and signalling components at DSB sites [84]."
23712866
reach
"In this context, overexpression of wild-type USP3, but not its catalytically inactive mutant, prevented the IR induced focus formation of RNF168, emphasizing the requirement of UPS3 cysteine protease [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
21056014
reach
"But most significantly in this context, overexpression of wild-type USP3, but not its catalytically inactive mutant, prevented the IR induced focus formation of RNF168, indicating that the assembly of[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
19203579