IndraLab

Statements


USP15 deubiquitinates PRPF3. 7 / 7
| 7

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"Moreover, we found that USP15 and USP4 deubiquitinated substrates PRP31 and PRP3 simultaneously."

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"Moreover, it was reported that Sart3, Usp4 and Usp15 form a complex in order to de-ubiquitinate Prp3 and Prp31 simultaneously."
| PMC

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"Deubiquitination of PRP31 and PRP3 by the USP15, SART3, and USP4 complex decreases the affinity towards PRP8 and this regulation is important for the proper splicing of chromosome segregation related genes such as Bub1 and alpha-tubulin."

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"However, USP15 deubiquitinated PRP3 in the presence of E3 ligase."

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"PRP3 was deubiquitinated by USP15 in the presence of PRP19."

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"PRP3 was deubiquitinated by USP4 consistent with a previous report but not by USP15."

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"These findings suggest that USP15 deubiquitinates PRP3 as well as PRP31 when they are ubiquitinated by E3 ligase although USP15 may have more preference for PRP31."