IndraLab

Statements

USP10 binds PCNA. 22 / 22
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"These results indicate that USP10 preferentially binds to ISGylated PCNA to cleave off mono-ubiquitin for TLS termination.Significantly, USP10 interacted with PCNA when doubly ISGylated PCNA appeared [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Significantly, USP10 interacted with PCNA when doubly ISGylated PCNA appeared (i.e., at 24 hr after UV treatment), but not when PCNA was mono-ISGylated (i.e., at 12 hr) ( Figure 3 J)."
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"Figure 3 H shows that USP10 binds to ISGylated PCNA much more tightly than to its unmodified form."
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"These results indicate that USP10 preferentially binds to ISGylated PCNA to cleave off mono-ubiquitin for TLS termination."
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"Moreover, PCNA binding to USP10 was abrogated by K168R mutation or ISG15 knockdown, both of which block PCNA ISGylation."
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"This important question awaits further studies.Surprisingly, the binding of USP10 to unmodified endogenous PCNA could not be detected, despite the fact that it has a noncanonical PIP box."
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"ISGylated PCNA promotes the interaction between PCNA and USP10 and de-ubiquitination of mono-ubiquitinated PCNA."
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"Ubiquitylated PCNA promotes its ISGylation 12 h after UV irradiation [228] and the ISGylated PCNA binds to USP10, which then removes ubiquitin from PCNA to stop TLS [228]."
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"Likewise, the binding of USP10 to PCNA via its noncanonical PIP box might be very weak, but it could be markedly enhanced by PCNA ISGylation, and this enhancement might provide the ability of USP10 to[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Likewise, the binding of USP10 to PCNA via its noncanonical PIP box might be very weak, but it could be markedly enhanced by PCNA ISGylation, and this enhancement might provide the ability of USP10 to[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Thus, it appears that endogenous USP10 interacts only with doubly ISGylated PCNA, although under overexpression conditions, USP10 can weakly bind to unmodified PCNA via its PIP box ( Figures 3 G and 3[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Overexpression of ISG15 conjugating system significantly enhanced the interaction between PCNA and USP10, and this increase was abrogated by coexpression of UBP43, suggesting that ISGylated PCNA has a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP10 can interact directly with PCNA via its PIP box and its silencing results in increased Ubi-PCNA 24 h after UV irradiation ( xref )."
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"USP10 can interact directly with PCNA via its PIP box and its silencing results in increased Ubi-PCNA 24 h after UV irradiation."
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"On the other hand, PCNA could interact with an inactive USP10 (C424A), of which the active site Cys424 was substituted by Ala ( Figure 3 D), indicating that the activity of USP10 is not required for i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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No evidence text available
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"Moreover, PCNA binding to USP10 was abrogated by K168R mutation or ISG15 knockdown ( Figures 3 I and 3J, respectively), both of which block PCNA ISGylation."
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"Surprisingly, the binding of USP10 to unmodified endogenous PCNA could not be detected ( Figure 3 J), despite the fact that it has a noncanonical PIP box."
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"Overexpression of ISG15-conjugating system significantly enhanced the interaction between PCNA and USP10, and this increase was abrogated by coexpression of UBP43 ( Figure 3 G), suggesting that ISGyla[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"ISGylated PCNA promotes the interaction between PCNA and USP10 and de-ubiquitination of mono-ubiquitinated PCNA."
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"Thus, it appears that endogenous USP10 interacts only with doubly ISGylated PCNA, although under overexpression conditions, USP10 can weakly bind to unmodified PCNA via its PIP box."
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"Ubiquitylated PCNA promotes its ISGylation 12 h after UV irradiation [228] and the ISGylated PCNA binds to USP10, which then removes ubiquitin from PCNA to stop TLS [228] ."
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