Evidence map›Paper›PMID 26571504›Full record

ArticlePloS one2015

The Deubiquitinating Enzyme UBPY Is Required for Lysosomal Biogenesis and Productive Autophagy in Drosophila.

Anne-Claire Jacomin, Amandine Bescond, Emmanuelle Soleilhac, Benoît Gallet, Guy Schoehn, Marie-Odile Fauvarque, Emmanuel Taillebourg

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

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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

7 authors at 4 institutions in 1 country.

Anne-Claire JacominUniversité Grenoble-Alpes, F-38041, Grenoble, France; CEA-DSV-iRTSV-BGE-Gen&Chem, F-38054, Grenoble, France; INSERM, U1038, F-38054, Grenoble, France.
Amandine BescondUniversité Grenoble-Alpes, F-38041, Grenoble, France; CEA-DSV-iRTSV-BGE-Gen&Chem, F-38054, Grenoble, France; INSERM, U1038, F-38054, Grenoble, France.
Emmanuelle SoleilhacUniversité Grenoble-Alpes, F-38041, Grenoble, France; CEA-DSV-iRTSV-BGE-Gen&Chem, F-38054, Grenoble, France; INSERM, U1038, F-38054, Grenoble, France.
Benoît GalletUniversité Grenoble Alpes, IBS, F-38044, Grenoble, France; CNRS, IBS, F-38044, Grenoble, France; CEA, IBS, F-38044, Grenoble, France.
Guy SchoehnUniversité Grenoble Alpes, IBS, F-38044, Grenoble, France; CNRS, IBS, F-38044, Grenoble, France; CEA, IBS, F-38044, Grenoble, France.
Marie-Odile FauvarqueUniversité Grenoble-Alpes, F-38041, Grenoble, France; CEA-DSV-iRTSV-BGE-Gen&Chem, F-38054, Grenoble, France; INSERM, U1038, F-38054, Grenoble, France.
Emmanuel TaillebourgUniversité Grenoble-Alpes, F-38041, Grenoble, France; CEA-DSV-iRTSV-BGE-Gen&Chem, F-38054, Grenoble, France; INSERM, U1038, F-38054, Grenoble, France.
Université Grenoble Alpes · FRCEA Grenoble · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a catabolic process that delivers cytoplasmic components to the lysosomes. Protein modification by ubiquitination is involved in this pathway: it regulates the stability of autophagy regulators such as BECLIN-1 and it also functions as a tag targeting specific substrates to autophagosomes. In order to identify deubiquitinating enzymes (DUBs) involved in autophagy, we have performed a genetic screen in the Drosophila larval fat body. This screen identified Uch-L3, Usp45, Usp12 and Ubpy. In this paper, we show that Ubpy loss of function results in the accumulation of autophagosomes due to a blockade of the autophagy flux. Furthermore, analysis by electron and confocal microscopy of Ubpy-depleted fat body cells revealed altered lysosomal morphology, indicating that Ubpy inactivation affects lysosomal maintenance and/or biogenesis. Lastly, we have shown that shRNA mediated inactivation of UBPY in HeLa cells affects autophagy in a different way: in UBPY-depleted HeLa cells autophagy is deregulated.

Indexed as

AutophagyOrganelle BiogenesisAnimalsBiocatalysisDrosophila melanogasterDrosophila ProteinsEndopeptidasesEndosomal Sorting Complexes Required for TransportGene SilencingGenetic TestingHeLa CellsHumansLysosomesMutant ProteinsUbiquitin-Specific ProteasesUbiquitin ThiolesteraseDrosophila ProteinsEndopeptidasesEndosomal Sorting Complexes Required for TransportMutant ProteinsUbiquitin-Specific ProteasesUbiquitin ThiolesteraseUSP8 protein, DrosophilaUSP8 protein, human

Identifiers

PMID26571504
PMCPMC4646453
OpenAlexW2180218417

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.