Evidence map›Paper›PMID 25484073›Full record

ArticleAutophagy2015

SUMO1 promotes Aβ production via the modulation of autophagy.

Sun-Jung Cho, Sang-Moon Yun, Chulman Jo, Dae-Hoon Lee, Ki Ju Choi, Jae Chun Song, Sang Ick Park, You-Jin Kim, Young Ho Koh

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2015. 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
4.9field-weighted citation impact, top 5% 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, 77 citations in OpenAlex.

  1. Review
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  5. A Vivo-Morpholino-Based Approach to Block Paralog-Specific SUMOylation.Methods in molecular biology (Clifton, N.J.) · 2025
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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

9 authors at 2 institutions in 2 countries.

Sun-Jung Choa Division of Brain Diseases, Center for Biomedical Sciences; Center for Infectious Diseases; Korea National Institute of Health; Osong-eup, Heungdeok-gu , Cheongju-si , Chungcheongbuk-do , Republic of Korea ;
Sang-Moon Yun
Chulman Jo
Dae-Hoon Lee
Ki Ju Choi
Jae Chun Song
Sang Ick Park
You-Jin Kim
Young Ho Koh
National Center for Infectious Diseases · USKorea National Institute of Health · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is one of the main mechanisms in the pathophysiology of neurodegenerative disease. The accumulation of autophagic vacuoles (AVs) in affected neurons is responsible for amyloid-β (Aβ) production. Previously, we reported that SUMO1 (small ubiquitin-like modifier 1) increases Aβ levels. In this study, we explored the mechanisms underlying this. We investigated whether AV formation is necessary for Aβ production by SUMO1. Overexpression of SUMO1 increased autophagic activation, inducing the formation of LC3-II-positive AVs in neuroglioma H4 cells. Consistently, autophagic activation was decreased by the depletion of SUMO1 with small hairpin RNA (shRNA) in H4 cells. The SUMO1-mediated increase in Aβ was reduced by the autophagy inhibitors (3-methyladenine or wortmannin) or genetic inhibitors (siRNA targeting ATG5, ATG7, ATG12, or HIF1A), respectively. Accumulation of SUMO1, ATG12, and LC3 was seen in amyloid precursor protein transgenic mice. Our results suggest that SUMO1 accelerates the accumulation of AVs and promotes Aβ production, which is a key mechanism for understanding the AV-mediated pathophysiology of Alzheimer disease.

Indexed as

AutophagyAmyloid beta-PeptidesAnimalsApoptosis Regulatory ProteinsBeclin-1BrainCell Line, TumorHypoxia-Inducible Factor 1, alpha SubunitMice, TransgenicMicrotubule-Associated ProteinsPlaque, AmyloidRNA, Small InterferingSUMO-1 ProteinTransfectionUp-RegulationAmyloid beta-PeptidesApoptosis Regulatory ProteinsBeclin-1Becn1 protein, mouseHypoxia-Inducible Factor 1, alpha SubunitMap1lc3b protein, mouseMicrotubule-Associated ProteinsRNA, Small InterferingSUMO-1 ProteinAD, Alzheimer diseaseAlzheimer diseaseamyloidATG12ATG, autophagy-relatedautophagyAV, autophagic vacuoleAβ, amyloid-βLC3MAP1LC3/LC3, microtubule-associated protein 1 light chain 3MDC, monodansylcadaverineshRNA, small hairpin RNASUMO1SUMO1, small ubiquitin-like modifier 1TEM, transmission electron microscopy, Tg, transgenic

Identifiers

PMID25484073
PMCPMC4502770
OpenAlexW2092984538

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.