Evidence map›Paper›PMID 11113196›Full record

ArticleMolecular and cellular biology2001

Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4).

G Serin, A Gersappe, J D Black, R Aronoff, L E Maquat

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In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 papers.

0numbers the graph read from it
0cells of the map it votes in
127citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

127 citing papers in PubMed, 245 citations in OpenAlex.

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  15. Nonsense-mediated mRNA decay and metal ion homeostasis and detoxification in Saccharomyces cerevisiae.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022
    Review
  16. Article
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67 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 2 countries.

G SerinDepartment of Cancer Genetics, Roswell Park Cancer Institute, Buffalo, New York 14263, USA.
A Gersappe
J D Black
R Aronoff
L E Maquat
University of Rochester · USMax Planck Institute for Medical Research · DERoswell Park Comprehensive Cancer Center · US

Funding

Two-Spirit Films in Indigenous Cancer HealthP30CA016056 · NCI · ROSWELL PARK CANCER INSTITUTE CORP · PI MARK G FRATTINI · 1985 to 2026
$116.6M
REGULATION OF SELENOPROTEIN RNA METABOLISMR01GM059614 · NIGMS · UNIVERSITY OF ROCHESTER · PI MAQUAT, LYNNE E · 1999 to 2022
$9.1M
NCI NIH HHS CA 16056NCI NIH HHS P30 CA016056NIDDK NIH HHS DK 33933NIGMS NIH HHS GM 59614NIGMS NIH HHS R01 GM059614
6 · The paper itself

Abstract

Nonsense-mediated mRNA decay (NMD), also called mRNA surveillance, is an important pathway used by all organisms that have been tested to degrade mRNAs that prematurely terminate translation and, as a consequence, eliminate the production of aberrant proteins that could be potentially harmful. In mammalian cells, NMD appears to involve splicing-dependent alterations to mRNA as well as ribosome-associated components of the translational apparatus. To date, human (h) Upf1 protein (p) (hUpf1p), a group 1 RNA helicase named after its Saccharomyces cerevisiae orthologue that functions in both translation termination and NMD, has been the only factor shown to be required for NMD in mammalian cells. Here, we describe human orthologues to S. cerevisiae Upf2p and S. cerevisiae Upf3p (Caenorhabditis elegans SMG-4) based on limited amino acid similarities. The existence of these orthologues provides evidence for a higher degree of evolutionary conservation of NMD than previously appreciated. Interestingly, human orthologues to S. cerevisiae Upf3p (C. elegans SMG-4) derive from two genes, one of which is X-linked and both of which generate multiple isoforms due to alternative pre-mRNA splicing. We demonstrate using immunoprecipitations of epitope-tagged proteins transiently produced in HeLa cells that hUpf2p interacts with hUpf1p, hUpf3p-X, and hUpf3p, and we define the domains required for the interactions. Furthermore, we find by using indirect immunofluorescence that hUpf1p is detected only in the cytoplasm, hUpf2p is detected primarily in the cytoplasm, and hUpf3p-X localizes primarily to nuclei. The finding that hUpf3p-X is a shuttling protein provides additional indication that NMD has both nuclear and cytoplasmic components.

Indexed as

RNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingAlternative SplicingAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCell NucleusCloning, MolecularConserved SequenceCytoplasmFluorescent Antibody TechniqueFungal ProteinsHeLa CellsAdaptor Proteins, Signal TransducingFungal ProteinsNAM7 protein, S cerevisiaeNMD2 protein, S cerevisiaeProtein IsoformsRNA-Binding ProteinsRNA HelicasesRNA, MessengerSaccharomyces cerevisiae ProteinsTrans-ActivatorsUPF1 protein, humanUPF3 protein, S cerevisiae

Identifiers

PMID11113196
PMCPMC88795
OpenAlexW1985847018

What OpenQuestion holds

Textmetadata
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Registered trials

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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.