Evidence map›Paper›PMID 27527864›Full record

ArticleOncotarget2016

O-GlcNAcylation of ATG4B positively regulates autophagy by increasing its hydroxylase activity.

Yoon Kyung Jo, Na Yeon Park, So Jung Park, Byung-Gyu Kim, Ji Hyun Shin, Doo Sin Jo, Dong-Jun Bae, Young-Ah Suh, Jeong Ho Chang, Eun Kyung Lee and 3 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Autophagy · 2026
    Review
  3. PerturbingCells · 2026
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  9. Frontiers in immunology · 2025
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  15. Review
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  19. Review
  20. Role ofPhysiological reviews · 2021
    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

13 authors at 5 institutions in 1 country.

Yoon Kyung JoDepartment of Gerontology, Graduate School of East-West Medical Science, Kyung Hee University, Yongin, South Korea.
Na Yeon ParkDepartment of Gerontology, Graduate School of East-West Medical Science, Kyung Hee University, Yongin, South Korea.
So Jung ParkDepartment of Gerontology, Graduate School of East-West Medical Science, Kyung Hee University, Yongin, South Korea.
Byung-Gyu KimLeading-edge Research Center for Drug Discovery and Development for Diabetes and Metabolic Disease, School of Medicine, Kyungpook National University Hospital, Daegu, South Korea.
Ji Hyun ShinDepartment of Gerontology, Graduate School of East-West Medical Science, Kyung Hee University, Yongin, South Korea.
Doo Sin JoDepartment of Gerontology, Graduate School of East-West Medical Science, Kyung Hee University, Yongin, South Korea.
Dong-Jun BaeAsan Institute for Life Sciences, Asan Medical Center, Seoul, South Korea.
Young-Ah SuhAsan Institute for Life Sciences, Asan Medical Center, Seoul, South Korea.
Jeong Ho ChangDepartment of Biology Education, Kyungpook National University, Daegu, South Korea.
Eun Kyung LeeDepartment of Biochemistry, College of Medicine, Catholic University of Korea, Seoul, South Korea.
Sang-Yeob KimAsan Institute for Life Sciences, Asan Medical Center, Seoul, South Korea.
Jin Cheon KimAsan Institute for Life Sciences, Asan Medical Center, Seoul, South Korea.
Dong-Hyung ChoDepartment of Gerontology, Graduate School of East-West Medical Science, Kyung Hee University, Yongin, South Korea.
Kyung Hee University · KRAsan Medical Center · KRCatholic University of Korea · KRKyungpook National University · KRUlsan College · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a catabolic degradation process and maintains cellular homeostasis. And autophagy is activated in response to various stress conditions. Although O-GlcNAcylation functions a sensor for nutrient and stress, the relationship between O-GlcNAcylation and autophagy is largely unknown. Here, we identified that ATG4B is novel target for O-GlcNAcylation under metabolic stress condition. Treatment with PugNAc, an O-GlcNAcase inhibitor increased activation of autophagy in SH-SY5Y cells. Both bimolecular fluorescence complementation and immunoprecipitation assay indicated that OGT directly interacts with ATG4B in SH-SY5Y cells. We also found that the O-GlcNAcylated ATG4B was increased in autophagy activation conditions, and down-regulation of OGT reduces O-GlcNAcylation of ATG4B under low glucose condition. Furthermore, the proteolytic activity of ATG4B for LC3 cleavage was enhanced in PugNAc-treated cells. Taken together, these results imply that O-GlcNAcylation of ATG4B regulates autophagy activation by increasing its proteolytic activity under metabolic stress condition.

Indexed as

AutophagyGene Expression Regulation, EnzymologicAcetylglucosamineAnimalsAutophagy-Related Proteinsbeta-N-AcetylhexosaminidasesCell Line, TumorCysteine EndopeptidasesDown-RegulationFibroblastsFluorescent DyesGlucoseHumansImmunoprecipitationLuciferasesMass SpectrometryAcetylglucosamineATG4B protein, humanAutophagy-Related Proteinsbeta-N-AcetylhexosaminidasesCysteine EndopeptidasesFluorescent DyesGlucosehexosaminidase CLuciferasesMixed Function OxygenasesN-acetylglucosaminono-1,5-lactone O-(phenylcarbamoyl)oximeN-AcetylglucosaminyltransferasesOximesPhenylcarbamatesATG4BautophagyO-GlcNAcylationOGTSH-SY5Y cells

Identifiers

PMID27527864
PMCPMC5302982
OpenAlexW2484652392

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.