Evidence map›Paper›PMID 24100012›Full record

ArticleMolecular and cellular biology2013

Intra- and intermolecular regulatory interactions in Upf1, the RNA helicase central to nonsense-mediated mRNA decay in yeast.

Feng He, Robin Ganesan, Allan Jacobson

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Anti-prion systems in yeast.The Journal of biological chemistry · 2019
    Review
  11. Nonsense-mediated mRNA decay factors cure most [PSI+] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Nonsense suppression by near-cognate tRNAs employs alternative base pairing at codon positions 1 and 3.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Review
  18. 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.

Feng HeDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Robin Ganesan
Allan Jacobson
University of Massachusetts Chan Medical School · US

Funding

Messenger RNA Metabolism in YeastR37GM027757 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JACOBSON, ALLAN S · 2005 to 2014
$6.3M
MESSENGER RNA METABOLISM IN YEASTR01GM027757 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JACOBSON, ALLAN S · 1985 to 2016
$3.8M
NIGMS NIH HHS R01 GM027757NIGMS NIH HHS R37 GM027757NIGMS NIH HHS R37GM27757
6 · The paper itself

Abstract

RNA helicases are involved in almost every aspect of RNA metabolism, yet very little is known about the regulation of this class of enzymes. In Saccharomyces cerevisiae, the stability and translational fidelity of nonsense-containing mRNAs are controlled by the group I RNA helicase Upf1 and the proteins it interacts with, Upf2 and Upf3. Combining the yeast two-hybrid system with genetic analysis, we show here that the cysteine- and histidine-rich (CH) domain and the RNA helicase domain of yeast Upf1 can engage in two new types of molecular interactions: an intramolecular interaction between these two domains and self-association of each of these domains. Multiple observations indicate that these molecular interactions are crucial for Upf1 regulation. First, coexpression of the CH domain and the RNA helicase domain in trans can reconstitute Upf1 function in both promoting nonsense-mediated mRNA decay (NMD) and preventing nonsense suppression. Second, mutations that disrupt Upf1 intramolecular interaction cause loss of Upf1 function. These mutations weaken Upf2 interaction and, surprisingly, promote Upf1 self-association. Third, the genetic defects resulting from deficiency in Upf1 intramolecular interaction or RNA binding are suppressed by expression of Upf2. Collectively, these data reveal a set of sequential molecular interactions and their roles in regulating Upf1 function during activation of NMD and suggest that cis intramolecular interaction and trans self-association may be general mechanisms for regulation of RNA helicase functions.

Indexed as

RNA StabilityAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesAmino Acid SubstitutionMutagenesis, Site-DirectedPeptide Chain Termination, TranslationalProtein Interaction Domains and MotifsRNA, FungalRNA HelicasesRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesNAM7 protein, S cerevisiaeNMD2 protein, S cerevisiaeRNA, FungalRNA HelicasesRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID24100012
PMCPMC3838015
OpenAlexW2032820137

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.