Abstract:
:Post-translational modifications contribute to the spliceosome dynamics by facilitating the physical rearrangements of the spliceosome. Here, we report USP15, a deubiquitinating enzyme, as a regulator of protein-protein interactions for the spliceosome dynamics. We show that PRP31, a component of U4 snRNP, is modified with K63-linked ubiquitin chains by the PRP19 complex and deubiquitinated by USP15 and its substrate targeting factor SART3. USP15SART3 makes a complex with USP4 and this ternary complex serves as a platform to deubiquitinate PRP31 and PRP3. The ubiquitination and deubiquitination status of PRP31 regulates its interaction with the U5 snRNP component PRP8, which is required for the efficient splicing of chromosome segregation related genes, probably by stabilizing the U4/U6.U5 tri-snRNP complex. Collectively, our data suggest that USP15 plays a key role in the regulation of dynamic protein-protein interactions of the spliceosome.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Das T,Park JK,Park J,Kim E,Rape M,Kim EE,Song EJdoi
10.1093/nar/gkw1365subject
Has Abstractpub_date
2017-05-05 00:00:00pages
4866-4880issue
8eissn
0305-1048issn
1362-4962pii
gkw1365journal_volume
45pub_type
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