Evidence map›Paper›PMID 26489670›Full record

ArticleScientific reports2015

New Insights into the RNA-Binding and E3 Ubiquitin Ligase Activities of Roquins.

Qi Zhang, Lixin Fan, Feng Hou, Aiping Dong, Yun-Xing Wang, Yufeng Tong

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Deciphering the role of the MALT1-RC3H1 axis in regulating GPX4 protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. MALT1 substrate cleavage: what is it good for?Frontiers in immunology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Modulation of Roquin Function in Myeloid Cells ReducesJournal of immunology (Baltimore, Md. : 1950) · 2017
    Article
  18. Review
  19. Article
  20. 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

6 authors at 4 institutions in 2 countries.

Qi ZhangStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Lixin FanSmall-Angle X-ray Scattering Core Facility, Center for Cancer Research of the National Cancer Institute, Frederick National Laboratory for Cancer Research, Leidos Biomedical Research, Inc., Frederick, MD 21702, USA.
Feng HouStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Aiping DongStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Yun-Xing WangProtein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, National Cancer Institute at Frederick, National Institutes of Health, Frederick, MD 21702, USA.
Yufeng TongStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
University of Toronto · CALeidos (United States) · USNational Institutes of Health · USStructural Genomics Consortium · CA

Funding

Wellcome Trust
6 · The paper itself

Abstract

Roquins are a family of highly conserved RNA-binding proteins that also contain a RING-type E3 ubiquitin ligase domain. They repress constitutive decay elements containing mRNAs and play a critical role in RNA homeostasis and immunological self-tolerance. Here we present the crystal structures of the RNA-binding region of Roquin paralog RC3H2 in both apo- and RNA-bound forms. The RNA-binding region has a bipartite architecture composed of ROQ and HEPN domains, and can bind to stem-loop and double-stranded RNAs simultaneously. The two domains undergo a large orientation change to accommodate RNA duplex binding. We profiled E2 ubiquitin-conjugating enzymes that pair with Roquins and found that RC3H1 and RC3H2 interact with two sets of overlapping but not identical E2 enzymes to drive the assembly of polyubiquitin chains of different linkages. Crystal structures, small-angle X-ray scattering, and E2 profiling revealed that while the two paralogs are highly homologous, RC3H2 and RC3H1 are different in their structures and functions. We also demonstrated that RNA duplex binding to RC3H2 cross-talks with its E3 ubiquitin ligase function using an in vitro auto-ubiquitination assay.

Indexed as

Crystallography, X-RayHumansProtein ConformationRNARNA-Binding ProteinsStructure-Activity RelationshipUbiquitin-Protein LigasesRC3H1 protein, humanRNARNA-Binding ProteinsUbiquitin-Protein Ligases

Identifiers

PMID26489670
PMCPMC4614863
OpenAlexW2336196684

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.