The deubiquitinating enzyme USP36 controls selective autophagy activation by ubiquitinated proteins

Taillebourg, Emmanuel; Grégoire, Isabel Pombo; Viargues, Perrine; Jacomin, Anne-Claire; Thevenon, Dominique; Faure, Mathias; Fauvarque, Marie-Odile

doi:10.4161/auto.19381

Cited by 64 publications

(52 citation statements)

References 48 publications

(66 reference statements)

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“…Immunofluorescence microscopy of S2 cells and dissected fat body were performed as described by Bergeret et al [15] and Taillebourg et al [31], respectively. …”

Section: Methodsmentioning

confidence: 99%

The Nonaspanins TM9SF2 and TM9SF4 Regulate the Plasma Membrane Localization and Signalling Activity of the Peptidoglycan Recognition Protein PGRP-LC in Drosophila

Perrin¹,

Mortier²,

Jacomin³

et al. 2014

J Innate Immun

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Transmembrane 9 (TM9) proteins, or nonaspanins, are a family of proteins conserved throughout evolution and characterized by 9 transmembrane domains. In Drosophila, TM9 superfamily protein member 4 (TM9SF4) and its closest paralogue, TM9SF2, contribute to phagocytosis of various types of particles, while TM9SF4 displays non-redundant requirement in Gram-negative bacteria engulfment. In addition, the two TM9 proteins control the actin cytoskeleton in larval haemocytes and in Drosophila S2 cells. Here, we show that TM9SF4 and TM9SF2 co-immunoprecipitate with the peptidoglycan recognition protein (PGRP)-LC, which triggers the Drosophila immune response to bacterial infection. Furthermore, both TM9 proteins co-localize with this receptor in intracellular vesicles and at the plasma membrane in Drosophila S2 cells in culture and in the fly fat body. Silencing TM9SF4 prevents plasma membrane localization of PGRP-LC, whereas silencing TM9SF2 does not, which may account for the non-redundant role of TM9SF4 in phagocytosis of Gram-negative bacteria. Finally, we provide a set of data suggesting that TM9 proteins can prevent inappropriate signalling from the unstimulated receptor.

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“…Immunofluorescence microscopy of S2 cells and dissected fat body were performed as described by Bergeret et al [15] and Taillebourg et al [31], respectively. …”

Section: Methodsmentioning

confidence: 99%

The Nonaspanins TM9SF2 and TM9SF4 Regulate the Plasma Membrane Localization and Signalling Activity of the Peptidoglycan Recognition Protein PGRP-LC in Drosophila

Perrin¹,

Mortier²,

Jacomin³

et al. 2014

J Innate Immun

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“…Interestingly, this enzyme was previously shown by Richardson et al to positively control cell growth by stabilizing rRNA production and ribosome biogenesis (38). Moreover, knockdown of both yeast and fly USP36 homologs was shown to result in an inhibition of cell growth (38,39). Although further biological validation is required, in light of our model system, USP36 can potentially provide a novel link between deubiquitination and growth arrest in OIS.…”

Section: Resultsmentioning

confidence: 62%

Phosphoproteome Dynamics in Onset and Maintenance of Oncogene-induced Senescence

Graaf

Kaplon

Zhou

et al. 2014

Molecular & Cellular Proteomics

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Expression of the BRAFV600E oncoprotein is known to cause benign lesions, such as melanocytic nevi (moles). Despite the oncogenic function of mutant BRAF, these lesions are arrested by a cell-autonomous mechanism called oncogene-induced senescence. Infrequently, nevi can progress to malignant melanoma, through mechanisms that are incompletely understood. To gain more insight into this vital tumor-suppression mechanism, we performed a mass-spectrometry-based screening of the proteome and phosphoproteome in cycling and senescent cells and in cells with abrogated senescence. Proteome analysis of senescent cells revealed the up-regulation of established senescence biomarkers, including specific cytokines, but also several proteins not previously associated with senescence, including extracellular matrix-interacting. Using both general and targeted phosphopeptide enrichment by Ti 4؉ -IMAC and phosphotyrosine antibody enrichment, we identified over 15,000 phosphorylation sites. Among the regulated phosphorylation sites we encountered components of the interleukin, BRAF/MAPK, and CDK-retinoblastoma pathways and several other factors. The extensive proteome and phosphoproteome dataset of BRAF V600E

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“…dUsp36 hemocyte-specific knockdown was achieved by expressing a double-stranded RNA (dsRNA) targeting dUsp36 in hemocytes using the driver line hml-Gal4 [28]. The efficiency and specificity of the dsRNA construct used in this study have already been thoroughly characterized [26]. We observed that, with the three different doses of L. monocytogenes used for infection (10, 100 or 1,000 CFUs), flies with dUsp36 -depleted hemocytes ( hml>dUsp36-IR ) died significantly faster than control flies ( hml/+ ; fig.…”

Section: Resultsmentioning

confidence: 99%

“…Scrawny or Emperor's thumb ) deubiquitinating enzyme acts as a negative regulator of the imd pathway by deubiquitinating the IMD protein [25]. We have also shown that dUsp36 controls cell growth and selective autophagy activation by ubiquitinated proteins [26]. Interestingly, a genome-wide RNAi-based screen conducted to identify host processes that contribute to L. monocytogenes pathogenesis identified dUsp36 (referred to as CG5505 ) as part of a group of genes whose knockdown led to enhanced L. monocytogenes intracellular growth [27].…”

Section: Introductionmentioning

confidence: 99%

The Drosophila Deubiquitinating Enzyme dUSP36 Acts in the Hemocytes for Tolerance to Listeria monocytogenes Infections

Taillebourg

Fauvarque

2014

J Innate Immun

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Listeria monocytogenes is a facultative intracellular pathogen which can infect Drosophila melanogaster. Upon infection, Drosophila mounts an immune response including antimicrobial peptide production and autophagy activation. A set of previously published results prompted us to study the role of the deubiquitinating enzyme dUSP36 in response to L. monocytogenes infections. We show in this report that flies with dUsp36-specific inactivation in hemocytes are susceptible to L. monocytogenes infections (as are flies with autophagy-deficient hemocytes) but are still able to control bacterial growth. Interestingly, flies with dUsp36-depleted hemocytes are not sensitized to infection by other pathogens. We conclude that dUsp36 plays a major role in hemocytes for tolerance to L. monocytogenes.

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The deubiquitinating enzyme USP36 controls selective autophagy activation by ubiquitinated proteins

Cited by 64 publications

References 48 publications

The Nonaspanins TM9SF2 and TM9SF4 Regulate the Plasma Membrane Localization and Signalling Activity of the Peptidoglycan Recognition Protein PGRP-LC in <b><i>Drosophila</i></b>

The Nonaspanins TM9SF2 and TM9SF4 Regulate the Plasma Membrane Localization and Signalling Activity of the Peptidoglycan Recognition Protein PGRP-LC in <b><i>Drosophila</i></b>

Phosphoproteome Dynamics in Onset and Maintenance of Oncogene-induced Senescence

The <b><i>Drosophila</i></b> Deubiquitinating Enzyme dUSP36 Acts in the Hemocytes for Tolerance to <b><i>Listeria monocytogenes</i></b> Infections

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