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USP45 binds ERCC1. 28 / 33
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"Consistent with this notion, the DNA damage sensitivity of USP45 knockout cells is only rescued by wild-type USP45 and not by an active USP45 [Asp25Ala, Glu26Ala] mutant that is unable to bind ERCC1 (Fig xref C) or catalytically inactive USP45 [Cys199Ala] (Fig xref A)."
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"This observation, together with the findings that USP45 co-precipitates with XPF-ERCC1 in Slx4 null cells and that ERCC1 interacts with USP45 in a yeast two-hybrid assay, indicate that USP45 interacts directly with ERCC1."
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"Both mass spectrometry and yeast two-hybrid system identify that USP45 interacts with ERCC1, and it was also demonstrated that USP45 deubiquitinates ERCC1 [55]."
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"USP45 interacts with ERCC1."
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"Another study [ xref ] demonstrated a direct interaction between the deubiquitylase USP45 and ERCC1, which may control its ubiquitylation."
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"Importantly, we find that the USP45 mutant [Asp25Ala, Glu26Ala] that is catalytically active but that cannot bind to ERCC1 (Supplementary Fig S5A) failed to deubiquitylate ERCC1 in vitro , indicating that specific interaction between ERCC1 and USP45 is essential to trigger deubiquitylation."
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"Both mass spectrometry and yeast two-hybrid system identify that USP45 interacts with ERCC1, and it was also demonstrated that USP45 deubiquitinates ERCC1 [XREF_BIBR]."
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"Both mass spectrometry and yeast two-hybrid system identify that USP45 interacts with ERCC1, and it was also demonstrated that USP45 deubiquitinates ERCC1 [ xref ]."
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"This revealed that mutation of three acidic adjacent residues (Asp25, Glu26 or Asp27) markedly inhibited interaction with ERCC1 without affecting expression of the USP45 [1–62] fragment (Fig xref C, xref )."
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"This observation, together with the findings that USP45 co-precipitates with XPF–ERCC1 in Slx4 null cells and that ERCC1 interacts with USP45 in a yeast two-hybrid assay, indicate that USP45 interacts directly with ERCC1."
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"Importantly, we find that the USP45 mutant [Asp25Ala, Glu26Ala] that is catalytically active but that can not bind to ERCC1 (Supplementary Fig S5A) failed to deubiquitylate ERCC1 in vitro, indicating that specific interaction between ERCC1 and USP45 is essential to trigger deubiquitylation."
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"Moreover, we observed that in SLX4 knockout MEFs (Castor et al , xref ), co-immunoprecipitation of USP45 and ERCC1 was unaffected (Fig xref E) consistent with USP45 binding to ERCC1 and not to SLX4."
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"This implies that the rescue of the sensitivity phenotype depends on the interaction between ERCC1 and USP45 as well as its catalytic activity."
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"This implies that the rescue of the sensitivity phenotype depends on the interaction between ERCC1 and USP45 as well as its catalytic activity."
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"Our data reveal that the interaction of ERCC1 with USP45 is specific to this particular DUB as the interaction is mediated by the N-terminal 62 amino acids that are highly conserved in USP45 orthologues, but are not found in other DUBs."
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"Both mass spectrometry and yeast two-hybrid system identify that USP45 interacts with ERCC1, and it was also demonstrated that USP45 deubiquitinates ERCC1 [55] ."
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"USP45 interacts with ERCC1."
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"The association of ERCC1 and USP45 was observed to be markedly more robust than interaction with other SLX4 components (Fig xref C, xref ), further suggesting that USP45 associates with ERCC1."
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"Furthermore, USP45 can deubiquitylate ERCC1 in a manner that requires association of USP45 and ERCC1."
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"This revealed that USP45 interacted with ERCC1, but not with SLX4 or XPF (Fig xref C, xref )."
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"USP45 associates with ERCC1, a subunit of the DNA repair endonuclease XPF–ERCC1, via a short acidic motif outside of the USP45 catalytic domain."
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"In addition to the DNA damage complex (ERCC1-XPF), where USP45 can interact with ERCC1 through its N-term domain, already described, and the proteins previously reported by Sowa et al ., (such as RBMX, MYH10 and MYH9) xref , we identified a new potential target of USP45 encoded by the SPDL1 gene called Spindly or CCDC99."
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