Evidence map›Paper›PMID 23263869›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Staufen2 functions in Staufen1-mediated mRNA decay by binding to itself and its paralog and promoting UPF1 helicase but not ATPase activity.

Eonyoung Park, Michael L Gleghorn, Lynne E Maquat

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

58 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Emerging Roles of RNA-Binding Proteins in Neurodevelopment.Journal of developmental biology · 2022
    Review
  11. Article
  12. Article
  13. International journal of molecular sciences · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Short interspersed nuclear element (SINE)-mediated post-transcriptional effects on human and mouse gene expression: SINE-UP for active duty.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    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

3 authors at 1 institution in 1 country.

Eonyoung ParkDepartment of Biochemistry and Biophysics, School of Medicine and Dentistry, University of Rochester, Rochester, NY 14642, USA.
Michael L Gleghorn
Lynne E Maquat
University of Rochester · US

Funding

Regulation of Normal and Defective Human GenesR01GM074593 · NIGMS · UNIVERSITY OF ROCHESTER · PI MAQUAT, LYNNE E · 2006 to 2013
$3.1M
CANCER RESEARCH TRAINING-EXPERIMENTAL THERAPY MODELST32CA009363 · NCI · UNIVERSITY OF ROCHESTER · PI LAND, HARTMUT · 1985 to 2013
$2.9M
Structural characterization of RNA recognition during Staufen-mediated decayF32GM090479 · NIGMS · UNIVERSITY OF ROCHESTER · PI GLEGHORN, MICHAEL LEONARD · 2010 to 2011
$99k
NCI NIH HHS T32 CA009363NCI NIH HHS T32 CA09363NIGMS NIH HHS F32 GM090479NIGMS NIH HHS R01 GM074593
6 · The paper itself

Abstract

Staufen (STAU)1-mediated mRNA decay (SMD) is a posttranscriptional regulatory mechanism in mammals that degrades mRNAs harboring a STAU1-binding site (SBS) in their 3'-untranslated regions (3' UTRs). We show that SMD involves not only STAU1 but also its paralog STAU2. STAU2, like STAU1, is a double-stranded RNA-binding protein that interacts directly with the ATP-dependent RNA helicase up-frameshift 1 (UPF1) to reduce the half-life of SMD targets that form an SBS by either intramolecular or intermolecular base-pairing. Compared with STAU1, STAU2 binds ~10-fold more UPF1 and ~two- to fivefold more of those SBS-containing mRNAs that were tested, and it comparably promotes UPF1 helicase activity, which is critical for SMD. STAU1- or STAU2-mediated augmentation of UPF1 helicase activity is not accompanied by enhanced ATP hydrolysis but does depend on ATP binding and a basal level of UPF1 ATPase activity. Studies of STAU2 demonstrate it changes the conformation of RNA-bound UPF1. These findings, and evidence for STAU1-STAU1, STAU2-STAU2, and STAU1-STAU2 formation in vitro and in cells, are consistent with results from tethering assays: the decrease in mRNA abundance brought about by tethering siRNA-resistant STAU2 or STAU1 to an mRNA 3' UTR is inhibited by downregulating the abundance of cellular STAU2, STAU1, or UPF1. It follows that the efficiency of SMD in different cell types reflects the cumulative abundance of STAU1 and STAU2. We propose that STAU paralogs contribute to SMD by "greasing the wheels" of RNA-bound UPF1 so as to enhance its unwinding capacity per molecule of ATP hydrolyzed.

Indexed as

3' Untranslated RegionsAdenosine TriphosphatasesBlotting, WesternCytoskeletal ProteinsDNA PrimersElectrophoretic Mobility Shift AssayHEK293 CellsHeLa CellsHumansImmunoprecipitationNerve Tissue ProteinsPlasmidsProtein BindingReal-Time Polymerase Chain ReactionReverse Transcriptase Polymerase Chain ReactionRNA-Binding Proteins3' Untranslated RegionsAdenosine TriphosphatasesCytoskeletal ProteinsDNA PrimersNerve Tissue ProteinsRNA-Binding ProteinsRNA HelicasesSTAU1 protein, humanSTAU2 protein, humanTrans-ActivatorsUPF1 protein, human

Identifiers

PMID23263869
PMCPMC3545820
OpenAlexW2115833472

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.