Evidence map›Paper›PMID 32782141›Full record

ArticleBiochemical and biophysical research communications2020

Cytosolic N-GlcNAc proteins are formed by the action of endo-β-N-acetylglucosaminidase.

Jason C Maynard, Haruhiko Fujihira, Gabby E Dolgonos, Tadashi Suzuki, Alma L Burlingame

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

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  14. Recent Advances in the Chemical Biology ofMolecules (Basel, Switzerland) · 2021
    Review
  15. Review
  16. AeLife · 2020
    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

5 authors at 3 institutions in 2 countries.

Jason C MaynardDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, USA.
Haruhiko FujihiraDivision of Glycobiologics, Intractable Disease Research Center, Juntendo University Graduate School of Medicine, Tokyo, Japan; Glycometabolic Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, Saitama, Japan.
Gabby E DolgonosDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, USA.
Tadashi SuzukiGlycometabolic Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, Saitama, Japan; Suzuki Project, T-CiRA Discovery, Kanagawa, Japan. Electronic address: tsuzuki_gm@riken.jp.
Alma L BurlingameDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, USA.
University of California, San Francisco · USJuntendo University · JPSuzuki (Japan) · JP

Funding

Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
Purchase of Q-Exactive Mass SpectrometerS10OD016229 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2013 to 2013
$507k
NIGMS NIH HHS P41 GM103481NIH HHS S10 OD016229
6 · The paper itself

Abstract

NGLY1 is a widely conserved eukaryotic cytosolic deglycosylating enzyme involved in the endoplasmic reticulum-associated degradation (ERAD) process, which eliminates misfolded proteins through retrograde translocation and proteasomal degradation. A human genetic disorder called NGLY1-deficiency has been reported, indicating the functional importance of NGLY1 in humans. Evidence suggests that Ngly1-KO is embryonic lethal in mice, while additional deletion of the Engase gene, encoding another cytosolic deglycosylating enzyme (endo-β-N-acetylglucosaminidase; ENGase), partially rescued lethality. Upon compromised Ngly1 activity, ENGase-mediated deglycosylation of misfolded glycoproteins may cause excess formation of N-GlcNAc proteins in the cytosol, leading to detrimental effects in the mice. Whether endogenous N-GlcNAc proteins are really formed in Ngly1-KO cells/animals or not remains unclarified. Here, comprehensive identification of O- and N-GlcNAc proteins was carried out using purified cytosol from wild type, Ngly1-KO, Engase-KO, and Ngly1/Engase double KO mouse embryonic fibroblasts. It was revealed that while there is no dramatic change in the level of O-GlcNAc proteins among cells examined, there was a vast increase of N-GlcNAc proteins in Ngly1-KO cells upon proteasome inhibition. Importantly, few N-GlcNAc proteins were observed in Engase-KO or Ngly1/Engase double-KO cells, clearly indicating that the cytosolic ENGase is responsible for the formation of N-GlcNAc proteins. The excess formation of N-GlcNAc proteins may at least in part account for the pathogenesis of NGLY1-deficiency.

Indexed as

AcetylglucosamineAnimalsCell LineCytosolEndoplasmic Reticulum-Associated DegradationFibroblastsGlycoproteinsGlycosylationMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMiceAcetylglucosamineGlycoproteinsMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseENGaseGlycoproteomicsN-GlcNAcNGLY1NGLY1-DeficiencyO-GlcNAc

Identifiers

PMID32782141
PMCPMC7508226
OpenAlexW3047626135

What OpenQuestion holds

Textmetadata
LicenceTDM
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.