IndraLab

Statements

USP2 is phosphorylated. 7 / 7
| 6 1
sparser
"Phosphorylation of two critical residues in USP2 N terminus is required for its recruitment to DSB sites and interaction with RECQL4."
36436562
sparser
"As the N-terminal domain of USP2 showed ATM-dependent recruitment to DSB sites, we further investigated whether phosphorylation of USP2 N terminus is important for its recruitment to DSB sites."
36436562
sparser
"We then examined whether the phosphorylation of USP2 influences its interaction with RECQL4."
36436562
sparser
"Western blotting showed that supernatant from USP2 KD cells repressed insulin-elicited phosphorylation of Akt in 3T3-L1 cells significantly more than media from control HL-60 cells ( xref A)."
28956020
sparser
"Collectively, these data suggest that ATM is a key regulator for USP2 recruitment to DSB sites by phosphorylating USP2 at S2 and T137, which is essential for the interaction between USP2 and RECQL4."
36436562
rlimsp
"However, USP12 was still able to exert an indirect effect on AR Vs by controlling its phosphorylation through AKT activation (Figure 7F), confirming that AR Vs are still phosphorylated at S213 while this phosphorylation is most likely to be of no consequence for AR V activity as phosphorylation at this site reportedly decreases AR-androgen binding and targets AR for ubiquitination by MDM2 [44], both processes that seem irrelevant to AR V biology."
29861848
sparser
"Live-cell imaging of cells expressing EGFP-fused USP2 after laser microirradiation, mapping of domains responsible for recruitment to DSB sites, and analyses of phospho-deficient and phospho-mimetic mutants of USP2 showed that USP2 is recruited to DSB sites in a ATM-dependent manner, and phosphorylation of two critical residues in the N terminus of USP2 is essential for its recruitment to DSBs and interaction with RECQL4."
36436562