Evidence map›Paper›PMID 28088760›Full record

ArticleNucleic acids research2017

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

Tanuza Das, Joon Kyu Park, Jinyoung Park, Eunji Kim, Michael Rape, Eunice EunKyeong Kim, Eun Joo Song

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 37 citations in OpenAlex.

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  14. Article
  15. Spotlight on USP4: Structure, Function, and Regulation.Frontiers in cell and developmental biology · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Prp8 regulates oncogene-induced hyperplastic growth inDevelopment (Cambridge, England) · 2018
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Tanuza DasMolecular Recognition Research Center, Korea Institute of Science and Technology, Hwarangno 14-gil 5, Seongbuk-gu, Seoul 02792, Korea.
Joon Kyu ParkBiomedical Research Institute, Korea Institute of Science and Technology, Hwarangno 14-gil 5, Seongbuk-gu 02792, Seoul, Korea.
Jinyoung ParkMolecular Recognition Research Center, Korea Institute of Science and Technology, Hwarangno 14-gil 5, Seongbuk-gu, Seoul 02792, Korea.
Eunji KimBiomedical Research Institute, Korea Institute of Science and Technology, Hwarangno 14-gil 5, Seongbuk-gu 02792, Seoul, Korea.
Michael RapeDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Eunice EunKyeong KimBiomedical Research Institute, Korea Institute of Science and Technology, Hwarangno 14-gil 5, Seongbuk-gu 02792, Seoul, Korea.
Eun Joo SongMolecular Recognition Research Center, Korea Institute of Science and Technology, Hwarangno 14-gil 5, Seongbuk-gu, Seoul 02792, Korea.
Korea Institute of Science and Technology · KRUniversity of California, Berkeley · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Antigens, NeoplasmDNA Repair EnzymesHeLa CellsHumansMultiprotein ComplexesNuclear ProteinsProtein Interaction MapsProtein Processing, Post-TranslationalRibonucleoprotein, U4-U6 Small NuclearRNA-Binding ProteinsRNA Splicing FactorsSpliceosomesUbiquitinationUbiquitin-Specific ProteasesAntigens, NeoplasmDNA Repair EnzymesMultiprotein ComplexesNuclear ProteinsPRPF19 protein, humanPRPF3 protein, humanPRPF8 protein, humanRibonucleoprotein, U4-U6 Small NuclearRNA-Binding ProteinsRNA Splicing FactorsSART3 protein, humanUbiquitin-Specific ProteasesUSP15 protein, human

Identifiers

PMID28088760
PMCPMC5416801
OpenAlexW2571588017

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.