IndraLab

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USP15 deubiquitinates PRPF31. 6 / 6
1 | 5

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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."

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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."

"USP15 regulates dynamic protein-protein interactions of the spliceosome through deubiquitination of PRP31"

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"We further confirmed that the modified forms of PRP31 represented a covalent modification of PRP31 with ubiquitin using the denaturing NiNTA-pull down assay and found that USP15 WT but not inactive USP15 C269A led to deubiquitination of PRP31 in the cell."