Evidence map›Paper›PMID 30066206›Full record

ArticleJournal of biomolecular NMR2018

Structural investigation of glycan recognition by the ERAD quality control lectin Yos9.

Andreas Kniss, Sina Kazemi, Frank Löhr, Maren Berger, Vladimir V Rogov, Peter Güntert, Thomas Sommer, Ernst Jarosch, Volker Dötsch

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of biomolecular NMR, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. The Dsc complex and its role in Golgi quality control.Biochemical Society transactions · 2024
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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

9 authors at 4 institutions in 3 countries.

Andreas KnissInstitute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Max-von-Laue Str. 9, 60438, Frankfurt am Main, Germany.
Sina KazemiInstitute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Max-von-Laue Str. 9, 60438, Frankfurt am Main, Germany.
Frank LöhrInstitute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Max-von-Laue Str. 9, 60438, Frankfurt am Main, Germany.
Maren BergerMax-Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13125, Berlin-Buch, Germany.
Vladimir V RogovInstitute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Max-von-Laue Str. 9, 60438, Frankfurt am Main, Germany.
Peter GüntertInstitute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Max-von-Laue Str. 9, 60438, Frankfurt am Main, Germany.
Thomas SommerMax-Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13125, Berlin-Buch, Germany.
Ernst JaroschMax-Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13125, Berlin-Buch, Germany.
Volker DötschInstitute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Max-von-Laue Str. 9, 60438, Frankfurt am Main, Germany. vdoetsch@em.uni-frankfurt.de.
Goethe University Frankfurt · DEMax Delbrück Center · DEETH Zurich · CHHumboldt-Universität zu Berlin · DE

Funding

Deutsche Forschungsgemeinschaft SFB 1177Deutsche Forschungsgemeinschaft SFB 740
6 · The paper itself

Abstract

Yos9 is an essential component of the endoplasmic reticulum associated protein degradation (ERAD) system that is responsible for removing terminally misfolded proteins from the ER lumen and mediating proteasomal degradation in the cytosol. Glycoproteins that fail to attain their native conformation in the ER expose a distinct oligosaccharide structure, a terminal α1,6-linked mannose residue, that is specifically recognized by the mannose 6-phoshate receptor homology (MRH) domain of Yos9. We have determined the structure of the MRH domain of Yos9 in its free form and complexed with 3α, 6α-mannopentaose. We show that binding is achieved by loops between β-strands performing an inward movement and that this movement also affects the entire β-barrel leading to a twist. These rearrangements may facilitate the processing of client proteins by downstream acting factors. In contrast, other oligosaccharides such as 2α-mannobiose bind weakly with only locally occurring chemical shift changes underscoring the specificity of this substrate selection process within ERAD.

Indexed as

Protein FoldingCarrier ProteinsEndoplasmic Reticulum-Associated DegradationGlycoproteinsLectinsOligosaccharidesPolysaccharidesProtein BindingProtein ConformationSaccharomyces cerevisiae ProteinsSubstrate SpecificityCarrier ProteinsGlycoproteinsLectinsOligosaccharidesPolysaccharidesSaccharomyces cerevisiae ProteinsYos9 protein, S cerevisiaeConformational changeEndoplasmatic reticulum associated protein degradationGlycan bindingYos9

Identifiers

PMID30066206
OpenAlexW2886668482

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.