Evidence map›Paper›PMID 27559127›Full record

ArticleMolecular biology of the cell2016

The Ccz1-Mon1-Rab7 module and Rab5 control distinct steps of autophagy.

Krisztina Hegedűs, Szabolcs Takáts, Attila Boda, András Jipa, Péter Nagy, Kata Varga, Attila L Kovács, Gábor Juhász

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed, 1 pooled it
14.5field-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

124 citing papers in PubMed, 1 synthesis or guideline pooled it, 222 citations in OpenAlex.

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64 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

Krisztina HegedűsDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary.
Szabolcs TakátsDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary sz.takats@ttk.elte.hu szmrt@elte.hu.
Attila BodaDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary.
András JipaInstitute of Genetics, Biological Research Centre, Szeged H-6726, Hungary.
Péter NagyDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary.
Kata VargaInstitute of Genetics, Biological Research Centre, Szeged H-6726, Hungary.
Attila L KovácsDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary.
Gábor JuhászDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary Institute of Genetics, Biological Research Centre, Szeged H-6726, Hungary sz.takats@ttk.elte.hu szmrt@elte.hu.
Eötvös Loránd University · HUHUN-REN Szegedi Biológiai Kutatóközpont · HU

Funding

Wellcome Trust 087518
6 · The paper itself

Abstract

The small GTPase Rab5 promotes recruitment of the Ccz1-Mon1 guanosine exchange complex to endosomes to activate Rab7, which facilitates endosome maturation and fusion with lysosomes. How these factors function during autophagy is incompletely understood. Here we show that autophagosomes accumulate due to impaired fusion with lysosomes upon loss of the Ccz1-Mon1-Rab7 module in starved Drosophila fat cells. In contrast, autophagosomes generated in Rab5-null mutant cells normally fuse with lysosomes during the starvation response. Consistent with that, Rab5 is dispensable for the Ccz1-Mon1-dependent recruitment of Rab7 to PI3P-positive autophagosomes, which are generated by the action of the Atg14-containing Vps34 PI3 kinase complex. Finally, we find that Rab5 is required for proper lysosomal function. Thus the Ccz1-Mon1-Rab7 module is required for autophagosome-lysosome fusion, whereas Rab5 loss interferes with a later step of autophagy: the breakdown of autophagic cargo within lysosomes.

Indexed as

AnimalsAutophagyDrosophilaDrosophila ProteinsEndosomesGuanine Nucleotide Exchange FactorsLysosomesPhagosomesProtein Transportrab5 GTP-Binding Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesVesicular Transport ProteinsCcz1 protein, S cerevisiaeDrosophila ProteinsGuanine Nucleotide Exchange FactorsMon1 protein, S cerevisiaerab5 GTP-Binding Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport Proteins

Identifiers

PMID27559127
PMCPMC5063620
OpenAlexW2517263277

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.