Evidence map›Paper›PMID 24198248›Full record

ArticleNucleic acids research2014

Identification and functional analysis of novel phosphorylation sites in the RNA surveillance protein Upf1.

Clarivel Lasalde, Andrea V Rivera, Alfredo J León, José A González-Feliciano, Luis A Estrella, Eva N Rodríguez-Cruz, María E Correa, Iván J Cajigas, Dina P Bracho, Irving E Vega and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  4. Review
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  9. Dbp5/DDX19 between Translational Readthrough and Nonsense Mediated Decay.International journal of molecular sciences · 2020
    Review
  10. Article
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  16. Mechanism, factors, and physiological role of nonsense-mediated mRNA decay.Cellular and molecular life sciences : CMLS · 2015
    Review
  17. Review
  18. Review
  19. Review
  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

12 authors at 2 institutions in 2 countries.

Clarivel LasaldeDepartment of Biology, University of Puerto Rico-Río Piedras Campus, San Juan, PR, Department of Reproductive Medicine, University of California, San Diego, CA, Department of Biochemistry, University of Puerto Rico-Medical Sciences Campus, San Juan, PR and Molecular Sciences Research Building, San Juan, PR.
Andrea V Rivera
Alfredo J León
José A González-Feliciano
Luis A Estrella
Eva N Rodríguez-Cruz
María E Correa
Iván J Cajigas
Dina P Bracho
Irving E Vega
Miles F Wilkinson
Carlos I González
University of Puerto Rico, Medical Sciences Campus · PRUniversity of Puerto Rico at Río Piedras · PR

Funding

UPR/MDACC Partnership for Excellence in Cancer Research(Parent Grant U54 CA096297)U54CA096297 · NCI · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI Ilka C Rios · 2002 to 2026
$36.9M
Upgrade Laboratories Facilities at UPR-Rio PiedrasR25GM061151 · NIGMS · UNIVERSITY OF PUERTO RICO RIO PIEDRAS · PI CARBALLEIRA, NESTOR MANUEL · 2001 to 2023
$32.5M
TCR RNA SurveillanceR01GM058595 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI WILKINSON, MILES FROME · 1999 to 2012
$4.1M
POST-TRANSCRIPTIONAL CONTROL OF THE HEART AND LUNGSK01HL004355 · NHLBI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI GONZALEZ, CARLOS I · 2000 to 2004
$603k
Annual Meeting of the NCRR P41 Principal InvestigatorsU13RR016174 · NCRR · UNIVERSITY OF MARYLAND BALTIMORE · PI LAKOWICZ, JOSEPH R. · 2001 to 2005
$378k
NCI NIH HHS U54 CA96297NCRR NIH HHS P20 RR 016174NHLBI NIH HHS KO1 HL-04355-05NIGMS NIH HHS 2R25GM61151NIGMS NIH HHS GM008102-3052NIGMS NIH HHS GM058595
6 · The paper itself

Abstract

One third of inherited genetic diseases are caused by mRNAs harboring premature termination codons as a result of nonsense mutations. These aberrant mRNAs are degraded by the Nonsense-Mediated mRNA Decay (NMD) pathway. A central component of the NMD pathway is Upf1, an RNA-dependent ATPase and helicase. Upf1 is a known phosphorylated protein, but only portions of this large protein have been examined for phosphorylation sites and the functional relevance of its phosphorylation has not been elucidated in Saccharomyces cerevisiae. Using tandem mass spectrometry analyses, we report the identification of 11 putative phosphorylated sites in S. cerevisiae Upf1. Five of these phosphorylated residues are located within the ATPase and helicase domains and are conserved in higher eukaryotes, suggesting a biological significance for their phosphorylation. Indeed, functional analysis demonstrated that a small carboxy-terminal motif harboring at least three phosphorylated amino acids is important for three Upf1 functions: ATPase activity, NMD activity and the ability to promote translation termination efficiency. We provide evidence that two tyrosines within this phospho-motif (Y-738 and Y-742) act redundantly to promote ATP hydrolysis, NMD efficiency and translation termination fidelity.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsAmino Acid SequenceAnimalsHumansMiceMolecular Sequence DataNonsense Mediated mRNA DecayPeptide Chain Termination, TranslationalPhosphorylationRNA HelicasesSaccharomyces cerevisiae ProteinsSequence AlignmentTyrosineAdenosine TriphosphatasesNAM7 protein, S cerevisiaeRNA HelicasesSaccharomyces cerevisiae ProteinsTyrosine

Identifiers

PMID24198248
PMCPMC3919615
OpenAlexW2118264489

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.