Evidence map›Paper›PMID 36729310›Full record

ArticleCellular and molecular life sciences : CMLS2023

Effect of ATG12-ATG5-ATG16L1 autophagy E3-like complex on the ability of LC3/GABARAP proteins to induce vesicle tethering and fusion.

Marina N Iriondo, Asier Etxaniz, Yaiza R Varela, Uxue Ballesteros, Melisa Lázaro, Mikel Valle, Dorotea Fracchiolla, Sascha Martens, L Ruth Montes, Félix M Goñi and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 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
11.4field-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, 53 citations in OpenAlex.

  1. PROTACs in cancer therapy: targeted degradation of GPX4, PARP and epigenetic regulators.Journal of enzyme inhibition and medicinal chemistry · 2026
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  13. Anti-myeloma activity of the CXCR4 antagonist WZ811.Journal of molecular medicine (Berlin, Germany) · 2026
    Article
  14. Review
  15. Autophagy regulation of pyroptosis and ferroptosis: a new strategy for colorectal cancer treatment.Apoptosis : an international journal on programmed cell death · 2026
    Review
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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.

Marina N IriondoInstituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940, Leioa, Spain.ORCID http://orcid.org/0000-0002-3816-0865
Asier EtxanizInstituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940, Leioa, Spain.ORCID http://orcid.org/0000-0003-2916-8256
Yaiza R VarelaInstituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940, Leioa, Spain.ORCID http://orcid.org/0000-0002-7601-4025
Uxue BallesterosInstituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940, Leioa, Spain.ORCID http://orcid.org/0000-0001-8166-6485
Melisa LázaroCIC bioGUNE, Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 800, 48160, Derio, Bizkaia, Spain.ORCID http://orcid.org/0000-0002-9603-9115
Mikel ValleCIC bioGUNE, Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 800, 48160, Derio, Bizkaia, Spain.ORCID http://orcid.org/0000-0001-8268-6912
Dorotea FracchiollaMax Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030, Vienna, Austria.ORCID http://orcid.org/0000-0002-1612-5225
Sascha MartensMax Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030, Vienna, Austria.ORCID http://orcid.org/0000-0003-3786-8199
L Ruth MontesInstituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940, Leioa, Spain.ORCID http://orcid.org/0000-0002-4766-8417
Félix M GoñiInstituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940, Leioa, Spain.ORCID http://orcid.org/0000-0001-6270-9216
Alicia AlonsoInstituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940, Leioa, Spain. alicia.alonso@ehu.eus.ORCID http://orcid.org/0000-0002-2730-7470
University of the Basque Country · ESCIC bioGUNE · ESUniversity of Vienna · AT

Funding

Austrian Science Fund FWF W 1261Fundación Ramón Areces CIVP20A6619Hezkuntza, Hizkuntza Politika Eta Kultura Saila, Eusko Jaurlaritza IT1625-22Ministerio de Ciencia e Innovación PID2021-124461NB-I00
6 · The paper itself

Abstract

In macroautophagy, the autophagosome (AP) engulfs portions of cytoplasm to allow their lysosomal degradation. AP formation in humans requires the concerted action of the ATG12 and LC3/GABARAP conjugation systems. The ATG12-ATG5-ATG16L1 or E3-like complex (E3 for short) acts as a ubiquitin-like E3 enzyme, promoting LC3/GABARAP proteins anchoring to the AP membrane. Their role in the AP expansion process is still unclear, in part because there are no studies comparing six LC3/GABARAP family member roles under the same conditions, and also because the full human E3 was only recently available. In the present study, the lipidation of six members of the LC3/GABARAP family has been reconstituted in the presence and absence of E3, and the mechanisms by which E3 and LC3/GABARAP proteins participate in vesicle tethering and fusion have been investigated. In the absence of E3, GABARAP and GABARAPL1 showed the highest activities. Differences found within LC3/GABARAP proteins suggest the existence of a lipidation threshold, lower for the GABARAP subfamily, as a requisite for tethering and inter-vesicular lipid mixing. E3 increases and speeds up lipidation and LC3/GABARAP-promoted tethering. However, E3 hampers LC3/GABARAP capacity to induce inter-vesicular lipid mixing or subsequent fusion, presumably through the formation of a rigid scaffold on the vesicle surface. Our results suggest a model of AP expansion in which the growing regions would be areas where the LC3/GABARAP proteins involved should be susceptible to lipidation in the absence of E3, or else a regulatory mechanism would allow vesicle incorporation and phagophore growth when E3 is present.

Indexed as

AutophagyMicrotubule-Associated ProteinsApoptosis Regulatory ProteinsAutophagosomesAutophagy-Related Protein 12Autophagy-Related Protein 5Autophagy-Related ProteinsHumansLipidsApoptosis Regulatory ProteinsATG12 protein, humanATG16L1 protein, humanATG5 protein, humanAutophagy-Related Protein 12Autophagy-Related Protein 5Autophagy-Related ProteinsGABARAP protein, humanLipidsMicrotubule-Associated ProteinsATG12 UBL systemAutophagosome expansionAutophagy conjugation systemsHuman ATG8Lipid-protein interactionMembrane fusion

Identifiers

PMID36729310
PMCPMC9894987
OpenAlexW4318933975

What OpenQuestion holds

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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.