Evidence map›Paper›PMID 36139350›Full record

ArticleCells2022

Proteome and Glycoproteome Analyses Reveal the Protein N-Linked Glycosylation Specificity of STT3A and STT3B.

Piaopiao Wen, Jingru Chen, Chenyang Zuo, Xiaodong Gao, Morihisa Fujita, Ganglong Yang

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Glycosylation Gene Signatures as Prognostic Biomarkers in Glioblastoma.Annals of clinical and translational neurology · 2025
    Article
  10. Article
  11. Article
  12. Dysregulation of N-glycosylation byInternational journal of biological sciences · 2025
    Article
  13. Article
  14. Article
  15. High-Throughput Mass Spectrometry Analysis ofJournal of proteome research · 2024
    Article
  16. Review
  17. 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

6 authors at 1 institution in 2 countries.

Piaopiao WenKey Laboratory of Carbohydrate Chemistry and Biotechnology, School of Biotechnology, Jiangnan University, Ministry of Education, Wuxi 214122, China.ORCID 0000-0002-7764-3835
Jingru ChenKey Laboratory of Carbohydrate Chemistry and Biotechnology, School of Biotechnology, Jiangnan University, Ministry of Education, Wuxi 214122, China.
Chenyang ZuoKey Laboratory of Carbohydrate Chemistry and Biotechnology, School of Biotechnology, Jiangnan University, Ministry of Education, Wuxi 214122, China.
Xiaodong GaoKey Laboratory of Carbohydrate Chemistry and Biotechnology, School of Biotechnology, Jiangnan University, Ministry of Education, Wuxi 214122, China.
Morihisa FujitaKey Laboratory of Carbohydrate Chemistry and Biotechnology, School of Biotechnology, Jiangnan University, Ministry of Education, Wuxi 214122, China.
Ganglong YangKey Laboratory of Carbohydrate Chemistry and Biotechnology, School of Biotechnology, Jiangnan University, Ministry of Education, Wuxi 214122, China.
Jiangnan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

STT3A and STT3B are the main catalytic subunits of the oligosaccharyltransferase complex (OST-A and OST-B in mammalian cells), which primarily mediate cotranslational and post-translocational N-linked glycosylation, respectively. To determine the specificity of STT3A and STT3B, we performed proteomic and glycoproteomic analyses in the gene knock-out (KO) and wild-type HEK293 cells. In total, 3961 proteins, 4265 unique N-linked intact glycopeptides and 629 glycosites representing 349 glycoproteins were identified from all these cells. Deletion of the STT3A gene had a greater impact on the protein expression than deletion of STT3B, especially on glycoproteins. In addition, total mannosylated N-glycans were reduced and fucosylated N-glycans were increased in STT3A-KO cells, which were caused by the differential expression of glycan-related enzymes. Interestingly, hyperglycosylated proteins were identified in KO cells, and the hyperglycosylation of ENPL was caused by the endoplasmic reticulum (ER) stress due to the STT3A deletion. Furthermore, the increased expression of the ATF6 and PERK indicated that the unfolded protein response also happened in STT3A-KO cells. Overall, the specificity of STT3A and STT3B revealed that defects in the OST subunit not only broadly affect N-linked glycosylation of the protein but also affect protein expression.

Indexed as

HexosyltransferasesMembrane ProteinsGlycopeptidesGlycoproteinsGlycosylationHEK293 CellsHumansPolysaccharidesProteomeProteomicsGlycopeptidesGlycoproteinsHexosyltransferasesMembrane ProteinsPolysaccharidesProteomeSTT3A protein, humanSTT3B protein, humanglycoproteomicsintact glycopeptidesmass spectrometryN-linked glycosylationSTT3ASTT3B

Identifiers

PMID36139350
PMCPMC9496733
OpenAlexW4295063404

What OpenQuestion holds

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LicenceCC BY
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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.