Evidence map›Paper›PMID 26031751›Full record

ArticleJournal of molecular cell biology2016

Post-translational O-GlcNAcylation is essential for nuclear pore integrity and maintenance of the pore selectivity filter.

Yanping Zhu, Ta-Wei Liu, Zarina Madden, Scott A Yuzwa, Kelsey Murray, Samy Cecioni, Natasha Zachara, David J Vocadlo

Open access · bronzeAbstract read
In one paragraph

Article in Journal of molecular cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

50 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Molecular Crowing in Nuclear Pore.Sub-cellular biochemistry · 2025
    Review
  9. Review
  10. Review
  11. Article
  12. Tissue-specificeLife · 2024
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
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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

8 authors at 2 institutions in 2 countries.

Yanping ZhuDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Ta-Wei LiuDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Zarina MaddenDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Scott A YuzwaDepartment of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Kelsey MurrayDepartment of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Samy CecioniDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Natasha ZacharaDepartment of Biological Chemistry, Johns Hopkins University Medical School, Baltimore, MD 21205, USA.
David J VocadloDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada dvocadlo@sfu.ca.
Simon Fraser University · CAJohns Hopkins University · US

Funding

Shared Resource CoresP01HL107153 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2011 to 2017
$16.8M
Canadian Institutes of Health Research MOP-123341NHLBI NIH HHS P01HL107153
6 · The paper itself

Abstract

O-glycosylation of the nuclear pore complex (NPC) by O-linked N-acetylglucosamine (O-GlcNAc) is conserved within metazoans. Many nucleoporins (Nups) comprising the NPC are constitutively O-GlcNAcylated, but the functional role of this modification remains enigmatic. We show that loss of O-GlcNAc, induced by either inhibition of O-GlcNAc transferase (OGT) or deletion of the gene encoding OGT, leads to decreased cellular levels of a number of natively O-GlcNAcylated Nups. Loss of O-GlcNAc enables increased ubiquitination of these Nups and their increased proteasomal degradation. The decreased half-life of these deglycosylated Nups manifests in their gradual loss from the NPC and a downstream malfunction of the nuclear pore selective permeability barrier in both dividing and post-mitotic cells. These findings define a critical role of O-GlcNAc modification of the NPC in maintaining its composition and the function of the selectivity filter. The results implicate NPC glycosylation as a regulator of NPC function and reveal the role of conserved glycosylation of the NPC among metazoans.

Indexed as

AnimalsCell LineGlycosylationMiceNuclear PoreNuclear Pore Complex ProteinsProtein Processing, Post-TranslationalProtein StabilityUbiquitinationNuclear Pore Complex Proteinsglycosylationnuclear pore complexnucleoporinO-GlcNAcylationpost-translational modificationprotein stabilityubiquitination

Identifiers

PMID26031751
PMCPMC4710208
OpenAlexW2257136749

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.