Evidence map›Paper›PMID 28835545›Full record

ArticleEMBO reports2017

Rab7b modulates autophagic flux by interacting with Atg4B.

Ingrid Kjos, Marita Borg Distefano, Frank Sætre, Urska Repnik, Petter Holland, Arwyn T Jones, Nikolai Engedal, Anne Simonsen, Oddmund Bakke, Cinzia Progida

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 18% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.

  1. Guideline
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  10. Autophagy in the Neuronal Ceroid Lipofuscinoses (Batten Disease).Frontiers in cell and developmental biology · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.Biochimica et biophysica acta. Molecular cell research · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. 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

10 authors at 2 institutions in 2 countries.

Ingrid KjosDepartment of Biosciences, University of Oslo, Oslo, Norway.
Marita Borg DistefanoDepartment of Biosciences, University of Oslo, Oslo, Norway.
Frank SætreCentre for Molecular Medicine Norway, University of Oslo, Oslo, Norway.
Urska RepnikDepartment of Biosciences, University of Oslo, Oslo, Norway.
Petter HollandInstitute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Arwyn T JonesCardiff School of Pharmacy and Pharmaceutical Sciences, Cardiff University, Wales, UK.
Nikolai EngedalCentre for Molecular Medicine Norway, University of Oslo, Oslo, Norway.
Anne SimonsenInstitute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Oddmund BakkeDepartment of Biosciences, University of Oslo, Oslo, Norway oddmund.bakke@ibv.uio.no c.a.m.progida@ibv.uio.no.ORCID 0000-0003-4843-7626
Cinzia ProgidaDepartment of Biosciences, University of Oslo, Oslo, Norway oddmund.bakke@ibv.uio.no c.a.m.progida@ibv.uio.no.ORCID 0000-0002-9254-0690
University of Oslo · NOCardiff University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy (macroautophagy) is a highly conserved eukaryotic degradation pathway in which cytosolic components and organelles are sequestered by specialized autophagic membranes and degraded through the lysosomal system. The autophagic pathway maintains basal cellular homeostasis and helps cells adapt during stress; thus, defects in autophagy can cause detrimental effects. It is therefore crucial that autophagy is properly regulated. In this study, we show that the cysteine protease Atg4B, a key enzyme in autophagy that cleaves LC3, is an interactor of the small GTPase Rab7b. Indeed, Atg4B interacts and co-localizes with Rab7b on vesicles. Depletion of Rab7b increases autophagic flux as indicated by the increased size of autophagic structures as well as the magnitude of macroautophagic sequestration and degradation. Importantly, we demonstrate that Rab7b regulates LC3 processing by modulating Atg4B activity. Taken together, our findings reveal Rab7b as a novel negative regulator of autophagy through its interaction with Atg4B.

Indexed as

AutophagyAutophagy-Related ProteinsCysteine EndopeptidasesGene Expression RegulationHumansMicrotubule-Associated Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsATG4B protein, humanAutophagy-Related ProteinsCysteine EndopeptidasesMAP1LC3A protein, humanMicrotubule-Associated Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsAtg4BautophagyLC3Rab7bRab GTPases

Identifiers

PMID28835545
PMCPMC5623852
OpenAlexW2750077853

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.