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USP10 deubiquitinates PCNA. 6 / 6
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"49 Other studies show that USP10 is also involved in the de-ubiquitination of PCNA after its ISG15 modification (ISGylation)."
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"Recent research has shown that PCNA is also modified by ISG15, and ISGylation of PCNA recruits USP10 to deubiquitinate PCNA, thereby regulating PCNA ubiquitination under UV irradiation induced stress."
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"4 F and S3F , the increased PCNA protein level, resulting from USP10 overexpression declined due to the treatment of Spautin-1, which preliminarily demonstrated that USP10 could mediate PCNA deubiquit[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"An interesting study has recently shown that the deubiquitylation of mammalian PCNA, at least in the context of DNA damage induced by ultraviolet irradiation (UV), is aided by the deubiquitylating activity of USP10."
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"This modification in turn recruits USP10 that de-ubiquitylates PCNA in order to block TLS and resume normal replication."
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"Mechanistically, ISGylation of PCNA on Lys-168, a lysine adjacent to that of the ubiquitination, recruits the ubiquitin-specific peptidase, USP10, which de-ubiquitinates PCNA releasing the TLS polymerase and allowing for the replicative polymerase to re-engage (Fig. 4)."
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