Evidence map›Paper›PMID 35780247›Full record

ArticleNature communications2022

Endosomal LC3C-pathway selectively targets plasma membrane cargo for autophagic degradation.

Paula P Coelho, Geoffrey G Hesketh, Annika Pedersen, Elena Kuzmin, Anne-Marie N Fortier, Emily S Bell, Colin D H Ratcliffe, Anne-Claude Gingras, Morag Park

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.4field-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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
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  3. Autophagy · 2026
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  17. ATG5 selectively engages virus-tethered BST2/tetherin in an LC3C-associated pathway.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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 3 institutions in 2 countries.

Paula P CoelhoRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, Canada.ORCID 0000-0002-7006-4523
Geoffrey G Hesketh *Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 992A-600 University Avenue, Toronto, M5G 1X5, Canada.
Annika Pedersen *Rosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, Canada.ORCID 0000-0001-8738-5625
Elena KuzminRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, Canada.
Anne-Marie N FortierRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, Canada.ORCID 0000-0002-0428-3066
Emily S BellDepartment of Biochemistry and Molecular Biology, Pennsylvania State University, State College, PA, 16802, USA.
Colin D H RatcliffeRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, Canada.ORCID 0000-0003-4707-8326
Anne-Claude GingrasLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 992A-600 University Avenue, Toronto, M5G 1X5, Canada.ORCID 0000-0002-6090-4437
Morag ParkRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, Canada. morag.park@mcgill.ca.ORCID 0000-0001-5400-606X
McGill University Health Centre · CAMount Sinai Hospital · CAPennsylvania State University · US

Funding

CIHR 143301CIHR 148423CIHR 242529
6 · The paper itself

Abstract

Autophagy selectively targets cargo for degradation, yet mechanistic understanding remains incomplete. The ATG8-family plays key roles in autophagic cargo recruitment. Here by mapping the proximal interactome of ATG8-paralogs, LC3B and LC3C, we uncover a LC3C-Endocytic-Associated-Pathway (LEAP) that selectively recruits plasma-membrane (PM) cargo to autophagosomes. We show that LC3C localizes to peripheral endosomes and engages proteins that traffic between PM, endosomes and autophagosomes, including the SNARE-VAMP3 and ATG9, a transmembrane protein essential for autophagy. We establish that endocytic LC3C binds cargo internalized from the PM, including the Met receptor tyrosine kinase and transferrin receptor, and is necessary for their recruitment into ATG9 vesicles targeted to sites of autophagosome initiation. Structure-function analysis identified that LC3C-endocytic localization and engagement with PM-cargo requires the extended carboxy-tail unique to LC3C, the TBK1 kinase, and TBK1-phosphosites on LC3C. These findings identify LEAP as an unexpected LC3C-dependent pathway, providing new understanding of selective coupling of PM signalling with autophagic degradation.

Indexed as

EndosomesMicrotubule-Associated ProteinsAutophagyCell MembraneSNARE ProteinsMicrotubule-Associated ProteinsSNARE Proteins

Identifiers

PMID35780247
PMCPMC9250516
OpenAlexW4283782070

What Socratic 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 Socratic graph.