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

Title
USP15 regulates dynamic protein-protein interactions of the spliceosome through deubiquitination of PRP31
Authors
김은경송은주박진영김은지타누자다스박준규Michael Rape
Keywords
USP15; SART3; spliceosome
Issue Date
2017-05
Publisher
Nucleic acids research
Citation
VOL 45, NO 8-4880
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.
URI
https://pubs.kist.re.kr/handle/201004/65454
ISSN
0305-1048
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KIST Publication > Article
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