Evidence map›Paper›PMID 28821844›Full record

ArticleScientific reports2017

N-glycosylation Triggers a Dual Selection Pressure in Eukaryotic Secretory Proteins.

Máximo Lopez Medus, Gabriela E Gomez, Lucía F Zacchi, Paula M Couto, Carlos A Labriola, María S Labanda, Rodrigo Corti Bielsa, Eugenia M Clérico, Benjamin L Schulz, Julio J Caramelo

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
1.0field-weighted citation impact, top 24% 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, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Uncovering a Latent Bioactive Interleukin-6 Glycoform.Angewandte Chemie (International ed. in English) · 2024
    Article
  5. Article
  6. Article
  7. Acceptors stability modulates the efficiency of post-translational protein N-glycosylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  8. Review
  9. Article
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  11. Article
  12. Article
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  15. Review
  16. Review
  17. Article
  18. Why Glycosylation Matters in Building a Better Flu Vaccine.Molecular & cellular proteomics : MCP · 2019
    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

10 authors at 5 institutions in 3 countries.

Máximo Lopez MedusFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), 1405, Buenos Aires, Argentina.
Gabriela E GomezUniversidad de Buenos Aires. CONICET. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica. Instituto de Química y Fisicoquímica Biológicas (IQUIFIB), 1113, Buenos Aires, Argentina.
Lucía F ZacchiSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia.
Paula M CoutoFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), 1405, Buenos Aires, Argentina.
Carlos A LabriolaFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), 1405, Buenos Aires, Argentina.
María S LabandaFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), 1405, Buenos Aires, Argentina.
Rodrigo Corti BielsaFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), 1405, Buenos Aires, Argentina.
Eugenia M CléricoDepartment of Biochemistry and Molecular Biology, Life Sciences Laboratories, University of Massachusetts, Amherst, MA, 01003, USA.
Benjamin L SchulzSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia.
Julio J CarameloFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), 1405, Buenos Aires, Argentina. jcaramelo@leloir.org.ar.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARFundación Instituto Leloir · ARUniversity of Queensland · AUFundación Ciencias Exactas y Naturales · ARUniversity of Massachusetts Amherst · US

Funding

Protein folding in the cell: Challenges and coping mechanisms Administrative Supplement for Equipment PurchaseR35GM118161 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M · 2016 to 2025
$5.5M
PEPTIDE CONFORMATIONS &INTERACTIONS WITH MEMBRANESR01GM027616 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI GIERASCH, LILA M · 1985 to 2015
$5.3M
Modeling a cellular protein homeostasis networkR01GM101644 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M, POWERS, EVAN THOMAS · 2013 to 2016
$1.6M
NIGMS NIH HHS R01 GM027616NIGMS NIH HHS R01 GM101644NIGMS NIH HHS R35 GM118161
6 · The paper itself

Abstract

Nearly one third of the eukaryotic proteome traverses the secretory pathway and most of these proteins are N-glycosylated in the lumen of the endoplasmic reticulum. N-glycans fulfill multiple structural and biological functions, and are crucial for productive folding of many glycoproteins. N-glycosylation involves the attachment of an oligosaccharide to selected asparagine residues in the sequence N-X-S/T (X ≠ P), a motif known as an N-glycosylation'sequon'. Mutations that create novel sequons can cause disease due to the destabilizing effect of a bulky N-glycan. Thus, an analogous process must have occurred during evolution, whenever ancestrally cytosolic proteins were recruited to the secretory pathway. Here, we show that during evolution N-glycosylation triggered a dual selection pressure on secretory pathway proteins: while sequons were positively selected in solvent exposed regions, they were almost completely eliminated from buried sites. This process is one of the sharpest evolutionary signatures of secretory pathway proteins, and was therefore critical for the evolution of an efficient secretory pathway.

Indexed as

Selection, GeneticAnimalsChlorocebus aethiopsComputational BiologyCOS CellsEndoplasmic ReticulumEukaryotic CellsGenetic Diseases, InbornGlycoproteinsGlycosylationHumansMembrane ProteinsModels, MolecularProtein BindingProtein ConformationGlycoproteinsMembrane Proteins

Identifiers

PMID28821844
PMCPMC5562741
OpenAlexW2747519953

What OpenQuestion holds

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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.