Evidence map›Paper›PMID 21697506›Full record

ArticleMolecular biology of the cell2011

Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system.

Shujuan Pan, Shufang Wang, Budi Utama, Lu Huang, Neil Blok, Mary K Estes, Kelley W Moremen, Richard N Sifers

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

41 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. N-Glycosylation.Advances in experimental medicine and biology · 2021
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Plant protein glycosylation.Glycobiology · 2016
    Review
  20. 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

8 authors at 2 institutions in 1 country.

Shujuan PanDepartments of Pathology & Immunology, Baylor College of Medicine, Houston, TX 77030, USA.
Shufang Wang
Budi Utama
Lu Huang
Neil Blok
Mary K Estes
Kelley W Moremen
Richard N Sifers
Baylor College of Medicine · USUniversity of Georgia · US

Funding

Tissue Analysis & Molecular Imaging CoreP30DK056338 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI Geoffrey A Preidis · 2001 to 2026
$28.3M
Regulation of Rotavirus ReplicationR01AI080656 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI Sue Ellen Crawford, Mary Kolb Estes · 2009 to 2026
$7.9M
Mannosidase inhibitors as therapeutics for glycoprotein misfolding diseasesR01DK075322 · NIDDK · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2006 to 2010
$2.6M
Post-translational Surveillance of Genome ExpressionR01DK064232 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI SIFERS, RICHARD NORMAN · 2004 to 2009
$1.0M
NIAID NIH HHS R01 AI080656NIDDK NIH HHS P30 DK056338NIDDK NIH HHS P30 DK56338NIDDK NIH HHS R01 DK064232NIDDK NIH HHS R01 DK075322
6 · The paper itself

Abstract

The Golgi complex has been implicated as a possible component of endoplasmic reticulum (ER) glycoprotein quality control, although the elucidation of its exact role is lacking. ERManI, a putative ER resident mannosidase, plays a rate-limiting role in generating a signal that targets misfolded N-linked glycoproteins for ER-associated degradation (ERAD). Herein we demonstrate that the endogenous human homologue predominantly resides in the Golgi complex, where it is subjected to O-glycosylation. To distinguish the intracellular site where the glycoprotein ERAD signal is generated, a COPI-binding motif was appended to the N terminus of the recombinant protein to facilitate its retrograde translocation back to the ER. Partial redistribution of the modified ERManI was observed along with an accelerated rate at which N-linked glycans of misfolded α1-antitrypsin variant NHK were trimmed. Despite these observations, the rate of NHK degradation was not accelerated, implicating the Golgi complex as the site for glycoprotein ERAD substrate tagging. Taken together, these data provide a potential mechanistic explanation for the spatial separation by which glycoprotein quality control components operate in mammalian cells.

Indexed as

Protein TransportProteolysisAmino Acid SequenceAnimalsAntibodies, Monoclonal, Murine-DerivedBinding SitesCell LineCricetinaeCricetulusEndoplasmic ReticulumGlycoproteinsGlycosylationGolgi ApparatusHumansMannosidasesMiceAntibodies, Monoclonal, Murine-DerivedGlycoproteinsMAN1B1 protein, humanMannosidasesPeptide Fragments

Identifiers

PMID21697506
PMCPMC3154878
OpenAlexW2161047029

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.