Evidence map›Paper›PMID 32839341›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Structural base for the transfer of GPI-anchored glycoproteins into fungal cell walls.

Marian Samuel Vogt, Gesa Felicitas Schmitz, Daniel Varón Silva, Hans-Ulrich Mösch, Lars-Oliver Essen

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

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  7. International journal of molecular sciences · 2025
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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.

Marian Samuel VogtDepartment of Chemistry, Philipps-Universität, D-35032 Marburg, Germany.ORCID 0000-0002-9867-3603
Gesa Felicitas SchmitzDepartment of Biology, Philipps-Universität, D-35032 Marburg, Germany.
Daniel Varón SilvaDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, D-14476 Potsdam, Germany.ORCID 0000-0003-2804-1923
Hans-Ulrich MöschDepartment of Biology, Philipps-Universität, D-35032 Marburg, Germany; moesch@staff.uni-marburg.de essen@chemie.uni-marburg.de.ORCID 0000-0002-4660-6070
Lars-Oliver EssenDepartment of Chemistry, Philipps-Universität, D-35032 Marburg, Germany; moesch@staff.uni-marburg.de essen@chemie.uni-marburg.de.ORCID 0000-0003-4272-4026

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The correct distribution and trafficking of proteins are essential for all organisms. Eukaryotes evolved a sophisticated trafficking system which allows proteins to reach their destination within highly compartmentalized cells. One eukaryotic hallmark is the attachment of a glycosylphosphatidylinositol (GPI) anchor to C-terminal ω-peptides, which are used as a zip code to guide a subset of membrane-anchored proteins through the secretory pathway to the plasma membrane. In fungi, the final destination of many GPI-anchored proteins is their outermost compartment, the cell wall. Enzymes of the Dfg5 subfamily catalyze the essential transfer of GPI-anchored substrates from the plasma membrane to the cell wall and discriminate between plasma membrane-resident GPI-anchored proteins and those transferred to the cell wall (GPI-CWP). We solved the structure of Dfg5 from a filamentous fungus and used in crystallo glycan fragment screening to reassemble the GPI-core glycan in a U-shaped conformation within its binding pocket. The resulting model of the membrane-bound Dfg5•GPI-CWP complex is validated by molecular dynamics (MD) simulations and in vivo mutants in yeast. The latter show that impaired transfer of GPI-CWPs causes distorted cell-wall integrity as indicated by increased chitin levels. The structure of a Dfg5•β1,3-glycoside complex predicts transfer of GPI-CWP toward the nonreducing ends of acceptor glycans in the cell wall. In addition to our molecular model for Dfg5-mediated transglycosylation, we provide a rationale for how GPI-CWPs are specifically sorted toward the cell wall by using GPI-core glycan modifications.

Indexed as

Cell WallFungal ProteinsFungiGlycoproteinsGlycosylphosphatidylinositolsProtein TransportFungal ProteinsGlycoproteinsGlycosylphosphatidylinositolsfungal cell-wall biogenesisglycoside hydrolaseGPI anchorprotein trafficking

Identifiers

PMID32839341
PMCPMC7486726

What OpenQuestion holds

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Read underepoch 390

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.