Evidence map›Paper›PMID 28110670›Full record

ArticleNeoplasia (New York, N.Y.)2017

GALNT6 Stabilizes GRP78 Protein by O-glycosylation and Enhances its Activity to Suppress Apoptosis Under Stress Condition.

Jiaying Lin, Suyoun Chung, Koji Ueda, Koichi Matsuda, Yusuke Nakamura, Jae-Hyun Park

Open access · goldAbstract read
In one paragraph

Article in Neoplasia (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. High-Penetrance Rare Variants Underlying Familial Lung Cancer Risk: Insights From Genetic Epidemiology of Lung Cancer Consortium.Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer · 2026
    Article
  5. GALNT1 emerges as a potential therapeutic target in breast cancer.Journal of cancer research and clinical oncology · 2026
    Article
  6. Article
  7. Article
  8. The Multifaceted Biology of PCSK9.Endocrine reviews · 2022
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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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

6 authors at 3 institutions in 2 countries.

Jiaying LinDepartment of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Suyoun ChungDepartment of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Koji UedaCancer Proteomics Group, Genome Center, Japanese Foundation for Cancer Research, Tokyo, 135-8550, Japan.
Koichi MatsudaLaboratory of Molecular Medicine, Human Genome Center, Institute of Medical Science, The University of Tokyo, Tokyo, 108-8639, Japan.
Yusuke NakamuraDepartment of Medicine, The University of Chicago, Chicago, IL 60637, USA; Department of Surgery, The University of Chicago, Chicago, IL 60637, USA. Electronic address: ynakamura@bsd.uchicago.edu.
Jae-Hyun ParkDepartment of Medicine, The University of Chicago, Chicago, IL 60637, USA.
University of Chicago · USJapanese Foundation For Cancer Research · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously reported that overexpression of an O-type glycosyltransferase, GALNT6 (polypeptide N-acetylgalactosaminyltransferase 6) played critical roles in mammary carcinogenesis. To further investigate the biological function of GALNT6, we screened a substrate protein(s) of GALNT6 using a VVA (Vicia villosa agglutinin) lectin (specific to GalNAc-Ser/Thr) pull-down method followed by mass spectrometry analysis. Here we report GRP78 (glucose-regulated protein 78, also known as HSPA5, heat shock 70 kDa protein 5), which is highly expressed in cancer cells and indicated to play important roles in various cellular processes including ER (endoplasmic reticulum) stress and autophagy, as a novel substrate of GALNT6. We found that GALNT6-induced O-glycosylation is critical for the stability of GRP78, its subcellular localization in ER, and its anti-apoptotic function. Furthermore, we demonstrated that overexpression of GRP78 could be important for Golgi-to-ER relocation of GALNT6. Collectively, our study revealed biological significances of O-glycosylation of GRP78 protein, which might play significant roles in the survival of cancer cells, and thus provided a new insight in cancer cell death and useful information for development of anti-cancer treatment targeting the GALNT6-GRP78 pathway.

Indexed as

ApoptosisStress, PhysiologicalCell Line, TumorCell SurvivalCytoplasmEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPGene ExpressionGene Knockout TechniquesGlycosylationGolgi ApparatusHeat-Shock ProteinsHumansModels, BiologicalN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferaseEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSPA5 protein, humanN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferase

Identifiers

PMID28110670
PMCPMC6197318
OpenAlexW2572366210

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.