Evidence map›Paper›PMID 21764848›Full record

ArticleGenes & development2011

Mechanism for Aar2p function as a U5 snRNP assembly factor.

Gert Weber, Vanessa F Cristão, Flavia de L Alves, Karine F Santos, Nicole Holton, Juri Rappsilber, Jean D Beggs, Markus C Wahl

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Structural basis of human U5 snRNP late biogenesis and recycling.Nature structural & molecular biology · 2024
    Article
  3. Article
  4. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Crystallization and biochemical characterization of the human spliceosomal Aar2-Prp8(RNaseH) complex.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article
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

8 authors at 3 institutions in 2 countries.

Gert WeberFachbereich Biologie/Chemie/Pharmazie, Abteilung Strukturbiochemie, Freie Universität Berlin, D-14195 Berlin, Germany;
Vanessa F Cristão
Flavia de L Alves
Karine F Santos
Nicole Holton
Juri Rappsilber
Jean D Beggs
Markus C Wahl
Freie Universität Berlin · DEUniversity of Edinburgh · GBWellcome Centre for Cell Biology · GB

Funding

Wellcome Trust 084229Wellcome Trust 087551
6 · The paper itself

Abstract

Little is known about how particle-specific proteins are assembled on spliceosomal small nuclear ribonucleoproteins (snRNPs). Brr2p is a U5 snRNP-specific RNA helicase required for spliceosome catalytic activation and disassembly. In yeast, the Aar2 protein is part of a cytoplasmic precursor U5 snRNP that lacks Brr2p and is replaced by Brr2p in the nucleus. Here we show that Aar2p and Brr2p bind to different domains in the C-terminal region of Prp8p; Aar2p interacts with the RNaseH domain, whereas Brr2p interacts with the Jab1/MPN domain. These domains are connected by a long, flexible linker, but the Aar2p-RNaseH complex sequesters the Jab1/MPN domain, thereby preventing binding by Brr2p. Aar2p is phosphorylated in vivo, and a phospho-mimetic S253E mutation in Aar2p leads to disruption of the Aar2p-Prp8p complex in favor of the Brr2p-Prp8p complex. We propose a model in which Aar2p acts as a phosphorylation-controlled U5 snRNP assembly factor that regulates the incorporation of the particle-specific Brr2p. The purpose of this regulation may be to safeguard against nonspecific RNA binding to Prp8p and/or premature activation of Brr2p activity.

Indexed as

Adaptor Proteins, Vesicular TransportModels, MolecularMutationNuclear ProteinsPhosphorylationProtein BindingProtein Structure, TertiaryRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA HelicasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAar2p protein, S cerevisiaeAdaptor Proteins, Vesicular TransportBRR2 protein, S cerevisiaeNuclear ProteinsPRP8 protein, S cerevisiaeRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA HelicasesSaccharomyces cerevisiae Proteins

Identifiers

PMID21764848
PMCPMC3182018
OpenAlexW2154451619

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.