IndraLab

Statements

USP34 binds RNF168. 7 / 7
| 4 3
reach
"As USP34 interacted with RNF168, but not RNF8 (XREF_FIG C and D), we focused our attention to dissect the functional interaction of USP34 and RNF168, although we are fully aware of the possibility that RNF8 may also transiently associate with USP34 and may represent a bona fide target of USP34."
23863847
reach
"USP34 [123] and USP7 [124] directly associate with RNF168 to prevent its poly-ubiquitylation and subsequent degradation via the proteasome (Figure 2A)."
38572758
sparser
"As USP34 interacted with RNF168, but not RNF8 ( xref C and D), we focused our attention to dissect the functional interaction of USP34 and RNF168, although we are fully aware of the possibility that RNF8 may also transiently associate with USP34 and may represent a bona fide target of USP34."
23863847
reach
"USP34 also associates and stabilizes RNF168 especially after IR, thereby enhancing H2A and gammaH2AX ubiquitylation."
28764946
sparser
"In line with our observation, a previous study showed that USP34 binds and stabilizes RNF168, an E3 required for DNA DSB-associated ubiquitylation [ 25 ]."
30585151
reach
"In line with our observation, a previous study showed that USP34 binds and stabilizes RNF168, an E3 required for DNA DSB-associated ubiquitylation [ 25 ]."
30585151
sparser
"The exact substrate subjected to USP34-RNF168 regulation remains to be identified."
30585151