Evidence map›Paper›PMID 11102520›Full record

ArticleMolecular biology of the cell2000

Golgi apparatus immunolocalization of endomannosidase suggests post-endoplasmic reticulum glucose trimming: implications for quality control.

C Zuber, M J Spiro, B Guhl, R G Spiro, J Roth

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2000. 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
3.2field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Structure of human endo-α-1,2-mannosidase (MANEA), an antiviral host-glycosylation target.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Immunoelectron Microscopy of Viral Antigens.Current protocols in microbiology · 2019
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Structural and mechanistic insight into N-glycan processing by endo-α-mannosidase.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Article
  20. Organellar calcium buffers.Cold Spring Harbor perspectives in biology · 2011
    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

5 authors at 2 institutions in 2 countries.

C ZuberDivision of Cell and Molecular Pathology, Department of Pathology, University of Zürich, CH-8091 Zürich, Switzerland.
M J Spiro
B Guhl
R G Spiro
J Roth
University of Zurich · CHJoslin Diabetes Center · US

Funding

STUDIES ON THE BIOSYNTHESIS OF GLYCOPROTEINSR01DK017477 · NIDDK · JOSLIN DIABETES CENTER · PI SPIRO, ROBERT G · 1986 to 1995
–
NIDDK NIH HHS DK17477
6 · The paper itself

Abstract

Trimming of N-linked oligosaccharides by endoplasmic reticulum (ER) glucosidase II is implicated in quality control of protein folding. An alternate glucosidase II-independent deglucosylation pathway exists, in which endo-alpha-mannosidase cleaves internally the glucose-substituted mannose residue of oligosaccharides. By immunogold labeling, we detected most endomannosidase in cis/medial Golgi cisternae (83.8% of immunogold labeling) and less in the intermediate compartment (15.1%), but none in the trans-Golgi apparatus and ER, including its transitional elements. This dual localization became more pronounced under 15 degrees C conditions indicative of two endomannosidase locations. Under experimental conditions when the intermediate compartment marker p58 was retained in peripheral sites, endomannosidase was redistributed to the Golgi apparatus. Double immunogold labeling established a mutually exclusive distribution of endomannosidase and glucosidase II, whereas calreticulin was observed in endomannosidase-reactive sites (17.3% in intermediate compartment, 5.7% in Golgi apparatus) in addition to the ER (77%). Our results demonstrate that glucose trimming of N-linked oligosaccharides is not limited to the ER and that protein deglucosylation by endomannosidase in the Golgi apparatus and intermediate compartment additionally ensures that processing to mature oligosaccharides can continue. Thus, endomannosidase localization suggests that a quality control of N-glycosylation exists in the Golgi apparatus.

Indexed as

Mannose-Binding Lectinsalpha-GlucosidasesAnimalsCalcium-Binding ProteinsCalreticulinCell CompartmentationCell LineEndoplasmic ReticulumGlucoseGlycosylationGolgi ApparatusLiverMannosidasesMembrane ProteinsMicroscopy, FluorescenceMicroscopy, Immunoelectron4-nitrophenyl-alpha-glucosidasealpha-GlucosidasesCalcium-Binding ProteinsCalreticulinendo-alpha-D-mannosidaseGlucoseLman1 protein, ratMannose-Binding LectinsMannosidasesMembrane ProteinsRibonucleoproteins

Identifiers

PMID11102520
PMCPMC15069
OpenAlexW1964702288

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.