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The deubiquitinating enzyme UBPY is required for Lysosomal Biogenesis and productive autophagy in drosophila

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Jacomin, Anne-Claire, Bescond, Amandine, Soleilhac, Emmanuelle, Gallet, Benoît, Schoehn, Guy, Fauvarque, Marie-Odile and Taillebourg, Emmanuel (2015) The deubiquitinating enzyme UBPY is required for Lysosomal Biogenesis and productive autophagy in drosophila. PLoS One, 10 (11). e0143078. doi:10.1371/journal.pone.0143078

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Official URL: http://dx.doi.org/10.1371/journal.pone.0143078

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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.

Item Type: Journal Article
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QL Zoology
Divisions: Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Lysosomes, Life -- Origin, Drosophila
Journal or Publication Title: PLoS One
Publisher: Public Library of Science
ISSN: 1932-6203
Official Date: 16 November 2015
Dates:
DateEvent
16 November 2015Published
30 October 2015Accepted
Volume: 10
Number: 11
Article Number: e0143078
DOI: 10.1371/journal.pone.0143078
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
Funder: France. Grenoble Partnership for Structural Biology (PSB)
Grant number: ISBG; UMS 3518 CNRS-CEA-UJF-EMBL, ANR-10-INSB-05-02, ANR-10-LABX-49-01

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