<i>Drosophila</i> Mtm and class II PI3K coregulate a PI(3)P pool with cortical and endolysosomal functions

Velichkova, Michaella; Juan, Joseph; Kadandale, Pavan; Jean, Sae Rin; Ribeiro, Inês; Raman, Venu; Stefan, Coassin; Aa, Kiger

doi:10.1083/jcb.20091102008192010c

Cited by 13 publications

(27 citation statements)

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“…As godzilla CG10277 mutant larva cannot survive on agar‐based fly food, mutant larvae were maintained with yeast paste on apple juice plate. UAS::mCherry::FYVE Hrs (Velichkova et al , 2010) and UAS‐GFP caax (Finley et al , 1998) were used in subcellular localization studies. For mutant clone analysis, Δ godzilla 2 was recombined with P{neoFRT}82B ry[506] (BL2035).…”

Section: Methodsmentioning

confidence: 99%

Goliath family E3 ligases regulate the recycling endosome pathway via VAMP3 ubiquitylation

Yamazaki

Schönherr

Varshney

et al. 2013

EMBO J

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Diverse cellular processes depend on endocytosis, intracellular vesicle trafficking, sorting and exocytosis, processes regulated post‐transcriptionally by modifications such as phosphorylation and ubiquitylation. In addition to sorting to the lysosome, cargo is recycled to the plasma membrane via recycling endosomes. Here, we describe a role of the goliath gene family of protease‐associated (PA) domain E3 ligases in regulating recycling endosome trafficking. The two Drosophila members of this family—Goliath and GodzillaCG10277—are located on endosomes, and both ectopic expression and loss‐of‐function lead to the accumulation of Rab5‐positive giant endosomes. Furthermore, the human homologue RNF167 exhibits similar behaviour. We show that the soluble N‐ethylmaleimide‐sensitive fusion attachment protein receptor (SNARE) protein VAMP3 is a target of these ubiquitin ligases, and that recycling endosome trafficking is abrogated in response to their activity. Furthermore, mutation of the Godzilla ubiquitylation target lysines on VAMP3 abrogates the formation of enlarged endosomes induced by either Godzilla or RNF167. Thus, Goliath ubiquitin ligases play a novel role in regulating recycling endosome trafficking via ubiquitylation of the VAMP3 SNARE protein.

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Section: Methodsmentioning

confidence: 99%

Goliath family E3 ligases regulate the recycling endosome pathway via VAMP3 ubiquitylation

Yamazaki

Schönherr

Varshney

et al. 2013

EMBO J

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“…Thus, depletion of PI3K‐C2α leads to a defect in endosomal‐recycling to the plasma membrane which was shown to affect Rho and Rac GTPases , Rab11‐mediated polarized trafficking of vesicles to the primary cilium , growth factor receptor signalling and general endosomal sorting signalling . Interestingly, class II PI3K‐dependent PI3P synthesis has similar functions in Drosophila , where it is involved in protrusion formation in hemocytes . In addition, PI3K‐C2α is required, via the production of PI3,4P 2 , for clathrin‐mediated endocytic trafficking and insulin receptor signalling .…”

Section: Pi3kc3‐independent Autophagymentioning

confidence: 99%

Phosphatidylinositol‐3‐phosphate in the regulation of autophagy membrane dynamics

2017

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Phosphatidylinositol-3-phosphate (PI3P) is a key player in membrane dynamics and trafficking regulation. Most PI3P is associated with endosomal membranes and with the autophagosome preassembly machinery, presumably at the endoplasmic reticulum. The enzyme responsible for most PI3P synthesis, VPS34 and proteins such as Beclin1 and ATG14L that regulate PI3P levels are positive modulators of autophagy initiation. It had been assumed that a local PI3P pool was present at autophagosomes and preautophagosomal structures, such as the omegasome and the phagophore. This was recently confirmed by the demonstration that PI3P-binding proteins participate in the complex sequence of signalling that results in autophagosome assembly and activity. Here we summarize the historical discoveries of PI3P lipid kinase involvement in autophagy, and we discuss the proposed role of PI3P during autophagy, notably during the autophagosome biogenesis sequence. PI3P in membrane identity and traffickingPhosphatidylinositol-3-phosphate (PI3P) is a phosphoinositide [1]. Many lipids, including some phosphoinositides such as PI4,5P 2 , have been shown to play crucial roles in cellular organization, motility and intracellular membrane trafficking [2] including membrane protrusion, invagination and remodelling. Interestingly, the subcellular location of phosphoinositides inside the cell is tightly regulated, and the presence, or absence, of specific phosphoinositides, together with specialized membrane trafficking proteins such as Rab small GTPases, at a given membrane compartment is often directly correlated with compartment function [3]. Phosphoinositides such as PI4,5P 2 , PI3,4,5P 3 and PI4P have been detected at the plasma membrane and at the Golgi apparatus (Fig. 1). Instead, PI3P is detected at surface of early endosomes and on intraluminal vesicles of multivesicular endosomes and on autophagosomes, the main organelle of the autophagy degradation pathway [4,5]. PI3,5P 2 , a subproduct of PI3P, is also detected on autophagosomes and the limiting membranes of late endosomes. Finally, PI3P is observed at sites of LC3-associated phagocytosis and Abbreviations 3-MA, 3-methyl-adenine; ALFY, autophagy-FYVE-linked protein; ALR, autophagosome-lysosome reformation; AMBRA1, autophagy/beclin-1 regulator 1; ATG, autophagy-related; CMA, chaperone-mediated autophagy; ER, endoplasmic reticulum; FYCO1, FYVE and coiled-coil domain containing 1; INPP5E, inositol polyphosphate-5-phosphatase E; LIR, LC3 interaction region; MTMRs, myotubularins; NRBF2, nuclear receptor-binding factor 2; PAS, preautophagosomal structure; PI3KC2, class II phosphoinositide-3-kinase; PI3KC3, class III phosphoinositide-3-kinase; PI3P, phosphatidylinositol-3-phosphate; PROPPIN, β-propellers that bind phosphoinositides; RUFY4, RUN and FYVE domain containing 4; TECPR1, Tectonin domain-containing protein 1; VMP1, vacuole membrane protein 1.

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“…Although still controversial, the location of animal MTM1 is considered to be mainly on the early endosomes where the substrate PtdIns3 P is located (Laporte et al, 2002;Cao et al, 2007), while MTMR2 may localize to both late (Cao et al, 2008) and early endosomes (Franklin et al, 2011). Consequently, animal MTM1 and MTM2 as well as the MTM homologs in Drosophila and C. elegans are implicated in endosomal trafficking (Velichkova et al, 2010;Neukomm et al, 2011). As Arabidopsis MTMs localize to the ER-GA interface, they might be relevant to the unique plant-specific nature of the ER-GA transport (Robinson et al, 2015).…”

Section: Discussionmentioning

confidence: 98%

Subcellular localizations of Arabidopsis myotubularins MTM1 and MTM2 suggest possible functions in vesicular trafficking between ER and cis-Golgi

Nagpal

Ndamukong

Hassan

et al. 2016

Journal of Plant Physiology

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Drosophila Mtm and class II PI3K coregulate a PI(3)P pool with cortical and endolysosomal functions

Abstract: Due to a production error, a source of funding was omitted from the authors' acknowledgments. The grant information has been restored in the html and pdf versions of the paper, and the error remains only in print. The corrected acknowledgment paragraph appears below.

Cited by 13 publications

References 0 publications

Goliath family E3 ligases regulate the recycling endosome pathway via VAMP3 ubiquitylation

Goliath family E3 ligases regulate the recycling endosome pathway via VAMP3 ubiquitylation

Phosphatidylinositol‐3‐phosphate in the regulation of autophagy membrane dynamics

Subcellular localizations of Arabidopsis myotubularins MTM1 and MTM2 suggest possible functions in vesicular trafficking between ER and cis-Golgi

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