Evidence map›Paper›PMID 27255711›Full record

ArticleThe Journal of biological chemistry2016

Structural Basis of the Recruitment of Ubiquitin-specific Protease USP15 by Spliceosome Recycling Factor SART3.

Qi Zhang, Rachel Harding, Feng Hou, Aiping Dong, John R Walker, Joseph Bteich, Yufeng Tong

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. The Multifaceted Roles of USP15 in Signal Transduction.International journal of molecular sciences · 2021
    Review
  7. Spotlight on USP4: Structure, Function, and Regulation.Frontiers in cell and developmental biology · 2021
    Review
  8. Article
  9. Article
  10. The RNA-binding protein SART3 promotes miR-34a biogenesis and GThe Journal of biological chemistry · 2019
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Qi ZhangFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Rachel HardingFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Feng HouFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Aiping DongFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
John R WalkerFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Joseph Bteichthe Drug Discovery Program, Ontario Institute for Cancer Research, Toronto, Ontario M5G 0A3, and.
Yufeng TongFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, the Department of Pharmacology and Toxicology, University of Toronto, Toronto, Ontario M5G 1L7, Canada yufeng.tong@utoronto.ca.ORCID 0000-0001-7740-1812
University of Toronto · CAOntario Institute for Cancer Research · CA

Funding

Wellcome Trust
6 · The paper itself

Abstract

Ubiquitin-specific proteases (USPs) USP15 and USP4 belong to a subset of USPs featuring an N-terminal tandem domain in USP (DUSP) and ubiquitin-like (UBL) domain. Squamous cell carcinoma antigen recognized by T-cell 3 (SART3), a spliceosome recycling factor, binds to the DUSP-UBL domain of USP15 and USP4, recruiting them to the nucleus from the cytosol to control deubiquitination of histone H2B and spliceosomal proteins, respectively. To provide structural insight, we solved crystal structures of SART3 in the apo-form and in complex with the DUSP-UBL domain of USP15 at 2.0 and 3.0 Å, respectively. Structural analysis reveals SART3 contains 12 half-a-tetratricopeptide (HAT) repeats, organized into two subdomains, HAT-N and HAT-C. SART3 dimerizes through the concave surface of HAT-C, whereas the HAT-C convex surface binds USP15 in a novel bipartite mode. Isothermal titration calorimetry measurements and mutagenesis analysis confirmed key residues of USP15 involved in the interaction and indicated USP15 binds 20-fold stronger than USP4.

Indexed as

Antigens, NeoplasmCrystallography, X-RayHumansProtein BindingProtein Structure, QuaternaryRepetitive Sequences, Amino AcidRNA-Binding ProteinsStructure-Activity RelationshipUbiquitin-Specific ProteasesUbiquitin ThiolesteraseAntigens, NeoplasmRNA-Binding ProteinsSART3 protein, humanUbiquitin-Specific ProteasesUbiquitin ThiolesteraseUSP15 protein, humanUSP4 protein, humancrystal structuredeubiquitinasedimerizationhalf-a-tetratricopeptide repeatsprotein-protein interactionsite-directed mutagenesisubiquitin-dependent protease

Identifiers

PMID27255711
PMCPMC5016127
OpenAlexW2418121389

What OpenQuestion holds

Textmetadata
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.