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Statements

PAN2 is phosphorylated. 15 / 15
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"We hypothesized that ATM-mediated phosphorylation of USP52 activates its DUB activity."
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"Because the interaction between CtIP and USP52 was not changed before or after IR treatment, it is possible that the phosphorylation of USP52 increases its catalytic capability but not the affinity toward CtIP."
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"Then we considered the possibility that Ccr4, Pan2, and Pan3 are phosphorylated in response to the change of carbon source."
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"To further analyze the role of USP52 phosphorylation in regulating DNA end resection and HR, we re-expressed WT USP52 and USP52 S1003A mutant in USP52-deficient cells to compare their biological functions."
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"In this experiment, the phosphorylation of Ccr4, Pan2, and Pan3 were assessed in vivo using the HA-tagged version of proteins and Phos-tag SDS-PAGE."
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"We further evaluated whether USP52 phosphorylation by ATM affects CHK1 and RPA2 phosphorylation and render cells resistant to cancer therapy."
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"As shown in Fig.  xref , CtIP ubiquitination level was significantly decreased in cells expressing WT USP52 but not the S1003A mutant after IR treatment, suggesting that USP52 phosphorylation is critical for deubiquitinating CtIP following IR exposure."
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"These results suggest that USP52 phosphorylation by ATM is important for its role in regulating DNA end resection and HR through regulating CtIP deubiquitination."
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"Indeed, we found that USP52 was phosphorylated at SQ/TQ motifs in response to IR, and this phosphorylation could be abolished by pretreating cells with an ATM inhibitor or treating cell lysates with phosphatase (Fig.  xref ), indicating that USP52 could be phosphorylated in an ATM-dependent manner following IR treatment."
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"As shown in Supplementary Fig.  xref , xref , reconstitution of USP52-deficient cells with WT USP52 but not USP52 S1003A rescued USP52 depletion-induced defects, including CHK1 and RPA2 phosphorylation and IR and PARPi response, suggesting that USP52 phosphorylation by ATM is important for proper DDR."
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"These results indicated that Ccr4, Pan2, and Pan3 are phosphorylated in GlyLac medium, and suggested the possibility that the activities of Ccr4, Pan2, and Pan3 are regulated by phosphorylation in res[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Since Ccr4, Pan2, and Pan3 seem to be more phosphorylated in GlyLac medium, these phosphorylated Ccr4, Pan2, and Pan3 proteins might be required to maintain a proper homeostasis in low energy media."
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"As shown in Fig.  xref , incubating WT, but not the S1003A mutant of USP52, with ATM further decreased the ubiquitination level of CtIP, suggesting that ATM-mediated USP52 phosphorylation is important for USP52 activation to deubiquitinate CtIP following DNA damage."
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"We next examined which SQ/TQ site of USP52 was phosphorylated and found that the S1003A but not S469A mutation mostly abolished the phosphorylation of USP52 after DNA damage (Fig.  xref and Supplementary Fig.  xref ), suggesting that USP52 is phosphorylated on Ser-1003 in an ATM-dependent manner following IR treatment."
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"To further investigate the biological significance of USP52 phosphorylation, we compared the activities of WT USP52 and the S1003A mutant after DNA damage by in vitro deubiquitination assays."
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