Evidence map›Paper›PMID 36541703›Full record

ArticleAutophagy2023

PEX13 prevents pexophagy by regulating ubiquitinated PEX5 and peroxisomal ROS.

Nicholas D Demers, Victoria Riccio, Doo Sin Jo, Sushil Bhandari, Kelsey B Law, Weifang Liao, Choy Kim, G Angus McQuibban, Seong-Kyu Choe, Dong-Hyung Cho and 1 more

Open access · greenAbstract read
In one paragraph

Article in Autophagy, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
8.9field-weighted citation impact, top 1% 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

42 citing papers in PubMed, 61 citations in OpenAlex.

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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

11 authors at 3 institutions in 2 countries.

Nicholas D DemersCell Biology Program, Hospital for Sick Children, Peter Gilgan Centre for Research and Learning, Toronto, ON, Canada.
Victoria RiccioCell Biology Program, Hospital for Sick Children, Peter Gilgan Centre for Research and Learning, Toronto, ON, Canada.
Doo Sin JoSchool of Life Sciences, BK21 Four Knu Creative BioResearch Group Kyungpook National University, Republic of Korea.
Sushil BhandariDepartment of Microbiology, Wonkwang University School of Medicine, Iksan, Republic of Korea.
Kelsey B LawCell Biology Program, Hospital for Sick Children, Peter Gilgan Centre for Research and Learning, Toronto, ON, Canada.
Weifang LiaoDepartment of Microbiology, Wonkwang University School of Medicine, Iksan, Republic of Korea.
Choy KimDepartment of Microbiology, Wonkwang University School of Medicine, Iksan, Republic of Korea.
G Angus McQuibbanDepartment of Biochemistry, University of Toronto, Toronto, ON, Canada.
Seong-Kyu ChoeDepartment of Microbiology, Wonkwang University School of Medicine, Iksan, Republic of Korea.ORCID 0000-0002-2102-973X
Dong-Hyung ChoSchool of Life Sciences, BK21 Four Knu Creative BioResearch Group Kyungpook National University, Republic of Korea.
Peter K KimCell Biology Program, Hospital for Sick Children, Peter Gilgan Centre for Research and Learning, Toronto, ON, Canada.ORCID 0000-0001-6626-0575
University of Toronto · CAWonkwang University · KRKyungpook National University · KR

Funding

CIHR PJT#156196
6 · The paper itself

Abstract

Peroxisomes are rapidly degraded during amino acid and oxygen deprivation by a type of selective autophagy called pexophagy. However, how damaged peroxisomes are detected and removed from the cell is poorly understood. Recent studies suggest that the peroxisomal matrix protein import machinery may serve double duty as a quality control machinery, where they are directly involved in activating pexophagy. Here, we explored whether any matrix import factors are required to prevent pexophagy, such that their loss designates peroxisomes for degradation. Using gene editing and quantitative fluorescence microscopy on culture cells and a zebrafish model system, we found that PEX13, a component of the peroxisomal matrix import system, is required to prevent the degradation of otherwise healthy peroxisomes. The loss of PEX13 caused an accumulation of ubiquitinated PEX5 on peroxisomes and an increase in peroxisome-dependent reactive oxygen species that coalesce to induce pexophagy. We also found that PEX13 protein level is downregulated to aid in the induction of pexophagy during amino acid starvation. Together, our study points to PEX13 as a novel pexophagy regulator that is modulated to maintain peroxisome homeostasis.

Indexed as

AutophagyMacroautophagyActinsAmino AcidsAnimalsFibroblastsHumansLeucineLysineMembrane ProteinsMiceOxygenPeroxisomesReactive Oxygen SpeciesSirolimusUbiquitinActinsAmino AcidsLeucineLysineMembrane ProteinsOxygenPEX13 protein, humanReactive Oxygen SpeciesSirolimusUbiquitinPeroxisomesPEX13PEX5pexophagyreactive oxygen speciesselective autophagyubiquitinzebrafish

Identifiers

PMID36541703
PMCPMC10262789
OpenAlexW4313423959

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.