Evidence map›Paper›PMID 35538106›Full record

ArticleScientific reports2022

Exploring selective autophagy events in multiple biologic models using LC3-interacting regions (LIR)-based molecular traps.

Grégoire Quinet, Pierre Génin, Oznur Ozturk, Naima Belgareh-Touzé, Lilas Courtot, Renaud Legouis, Robert Weil, Mickael M Cohen, Manuel S Rodriguez

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. 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

9 authors at 7 institutions in 1 country.

Grégoire QuinetLaboratoire de Chimie de Coordination (LCC)-CNRS, UPS, 31400, Toulouse, France.
Pierre GéninCentre d'immunologie et des Maladies Infectieuses (CIMI-Paris)- Faculté de Médecine, Sorbonne Université, 75013, Paris, France.
Oznur OzturkSorbonne Université, CNRS, UMR8226, Institut de Biologie Physico-Chimique, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, 75005, Paris, France.
Naima Belgareh-TouzéSorbonne Université, CNRS, UMR8226, Institut de Biologie Physico-Chimique, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, 75005, Paris, France.
Lilas CourtotLaboratoire de Chimie de Coordination (LCC)-CNRS, UPS, 31400, Toulouse, France.
Renaud LegouisInstitute for Integrative Biology of the Cell (I2BC), Université Paris-Saclay, CEA, CNRS, 91198, Gif-sur-Yvette, France.
Robert WeilCentre d'immunologie et des Maladies Infectieuses (CIMI-Paris)- Faculté de Médecine, Sorbonne Université, 75013, Paris, France.
Mickael M CohenSorbonne Université, CNRS, UMR8226, Institut de Biologie Physico-Chimique, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, 75005, Paris, France.
Manuel S RodriguezLaboratoire de Chimie de Coordination (LCC)-CNRS, UPS, 31400, Toulouse, France. manuel.rodriguez@lcc-toulouse.fr.
Centre National de la Recherche Scientifique · FRSorbonne Université · FRCentre d'Immunologie et des Maladies Infectieuses · FRInstitut de Biologie Intégrative de la Cellule · FRLaboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes · FRLaboratoire de Chimie de Coordination · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is an essential cellular pathway that ensures degradation of a wide range of substrates including damaged organelles or large protein aggregates. Understanding how this proteolytic pathway is regulated would increase our comprehension on its role in cellular physiology and contribute to identify biomarkers or potential drug targets to develop more specific treatments for disease in which autophagy is dysregulated. Here, we report the development of molecular traps based in the tandem disposition of LC3-interacting regions (LIR). The estimated affinity of LC3-traps for distinct recombinant LC3/GABARAP proteins is in the low nanomolar range and allows the capture of these proteins from distinct mammalian cell lines, S. cerevisiae and C. elegans. LC3-traps show preferences for GABARAP/LGG1 or LC3/LGG2 and pull-down substrates targeted to proteaphagy and mitophagy. Therefore, LC3-traps are versatile tools that can be adapted to multiple applications to monitor selective autophagy events in distinct physiologic and pathologic circumstances.

Indexed as

Caenorhabditis elegansMacroautophagyAnimalsAutophagyMammalsMicrotubule-Associated ProteinsModels, BiologicalProtein BindingSaccharomyces cerevisiaeMicrotubule-Associated Proteins

Identifiers

PMID35538106
PMCPMC9090809
OpenAlexW4229454450

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.