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Article ; Online: The Ykt6-Snap29-Syx13 SNARE complex promotes crinophagy via secretory granule fusion with Lamp1 carrier vesicles.

Szenci, Győző / Glatz, Gábor / Takáts, Szabolcs / Juhász, Gábor

2024 Volume 14, Issue 1, Page(s) 3200

Abstract: In the Drosophila larval salivary gland, developmentally programmed fusions between lysosomes and secretory granules (SGs) and their subsequent acidification promote the maturation of SGs that are secreted shortly before puparium formation. Subsequently, ...

Abstract	In the Drosophila larval salivary gland, developmentally programmed fusions between lysosomes and secretory granules (SGs) and their subsequent acidification promote the maturation of SGs that are secreted shortly before puparium formation. Subsequently, ongoing fusions between non-secreted SGs and lysosomes give rise to degradative crinosomes, where the superfluous secretory material is degraded. Lysosomal fusions control both the quality and quantity of SGs, however, its molecular mechanism is incompletely characterized. Here we identify the R-SNARE Ykt6 as a novel regulator of crinosome formation, but not the acidification of maturing SGs. We show that Ykt6 localizes to Lamp1+ carrier vesicles, and forms a SNARE complex with Syntaxin 13 and Snap29 to mediate fusion with SGs. These Lamp1 carriers represent a distinct vesicle population that are functionally different from canonical Arl8+, Cathepsin L+ lysosomes, which also fuse with maturing SGs but are controlled by another SNARE complex composed of Syntaxin 13, Snap29 and Vamp7. Ykt6- and Vamp7-mediated vesicle fusions also determine the fate of SGs, as loss of either of these SNAREs prevents crinosomes from acquiring endosomal PI3P. Our results highlight that fusion events between SGs and different lysosome-related vesicle populations are critical for fine regulation of the maturation and crinophagic degradation of SGs.
MeSH term(s)	SNARE Proteins/genetics ; SNARE Proteins/metabolism ; R-SNARE Proteins/genetics ; R-SNARE Proteins/metabolism ; Qa-SNARE Proteins/metabolism ; Secretory Vesicles/metabolism ; Membrane Fusion/physiology ; Lysosomes/metabolism
Chemical Substances	SNARE Proteins ; R-SNARE Proteins ; Qa-SNARE Proteins
Language	English
Publishing date	2024-02-08
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-53607-x
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Article ; Online: Investigating Non-selective Autophagy in Drosophila.

Takáts, Szabolcs / Tóth, Sarolta / Szenci, Győző / Juhász, Gábor

Methods in molecular biology (Clifton, N.J.)

2019 Volume 1880, Page(s) 589–600

Abstract: Drosophila melanogaster is a popular model organism in molecular genetics and cell biology. Various Drosophila tissues have been successfully used for studying autophagy, and our knowledge about the genetic regulation of this process is constantly ... ...

Abstract	Drosophila melanogaster is a popular model organism in molecular genetics and cell biology. Various Drosophila tissues have been successfully used for studying autophagy, and our knowledge about the genetic regulation of this process is constantly growing. It is important to use assays that distinguish between non-selective autophagy and the selective forms. Here we introduce a selection of proven methods, which, taking into account their limitations, are suitable to measure non-selective autophagy in Drosophila fat and other tissues.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Autophagosomes/metabolism ; Autophagosomes/ultrastructure ; Autophagy/physiology ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Biological Assay/instrumentation ; Biological Assay/methods ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/physiology ; Fat Body/metabolism ; Fluorescent Dyes/chemistry ; Genes, Reporter/genetics ; Larva/physiology ; Lysosomes/metabolism ; Lysosomes/ultrastructure ; Microscopy, Electron, Transmission/methods ; Models, Animal
Chemical Substances	Autophagy-Related Proteins ; Drosophila Proteins ; Fluorescent Dyes
Language	English
Publishing date	2019-01-04
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-8873-0_38
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Article ; Online: Removal of hypersignaling endosomes by simaphagy.

Migliano, Simona M / Schultz, Sebastian W / Wenzel, Eva M / Takáts, Szabolcs / Liu, Dan / Mørk, Silje / Tan, Kia Wee / Rusten, Tor Erik / Raiborg, Camilla / Stenmark, Harald

Autophagy

2023 Volume 20, Issue 4, Page(s) 769–791

Abstract: Activated transmembrane receptors continue to signal following endocytosis and are only silenced upon ESCRT-mediated internalization of the receptors into intralumenal vesicles (ILVs) of the endosomes. Accordingly, endosomes with dysfunctional receptor ... ...

Abstract	Activated transmembrane receptors continue to signal following endocytosis and are only silenced upon ESCRT-mediated internalization of the receptors into intralumenal vesicles (ILVs) of the endosomes. Accordingly, endosomes with dysfunctional receptor internalization into ILVs can cause sustained receptor signaling which has been implicated in cancer progression. Here, we describe a surveillance mechanism that allows cells to detect and clear physically intact endosomes with aberrant receptor accumulation and elevated signaling. Proximity biotinylation and proteomics analyses of ESCRT-0 defective endosomes revealed a strong enrichment of the ubiquitin-binding macroautophagy/autophagy receptors SQSTM1 and NBR1, a phenotype that was confirmed in cell culture and fly tissue. Live cell microscopy demonstrated that loss of the ESCRT-0 subunit HGS/HRS or the ESCRT-I subunit VPS37 led to high levels of ubiquitinated and phosphorylated receptors on endosomes. This was accompanied by dynamic recruitment of NBR1 and SQSTM1 as well as proteins involved in autophagy initiation and autophagosome biogenesis. Light microscopy and electron tomography revealed that endosomes with intact limiting membrane, but aberrant receptor downregulation were engulfed by phagophores. Inhibition of autophagy caused increased intra- and intercellular signaling and directed cell migration. We conclude that dysfunctional endosomes are surveyed and cleared by an autophagic process, simaphagy, which serves as a failsafe mechanism in signal termination.
MeSH term(s)	Endosomes/metabolism ; Humans ; Endosomal Sorting Complexes Required for Transport/metabolism ; Autophagy/physiology ; Signal Transduction ; Animals ; Intracellular Signaling Peptides and Proteins/metabolism ; Sequestosome-1 Protein/metabolism ; Autophagosomes/metabolism ; Endocytosis/physiology ; HeLa Cells ; Cell Movement
Chemical Substances	Endosomal Sorting Complexes Required for Transport ; NBR1 protein, human ; Intracellular Signaling Peptides and Proteins ; Sequestosome-1 Protein ; SQSTM1 protein, human
Language	English
Publishing date	2023-10-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2023.2267958
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Article ; Online: A genetic model with specifically impaired autophagosome-lysosome fusion.

Takáts, Szabolcs / Juhász, Gábor

Autophagy

2013 Volume 9, Issue 8, Page(s) 1251–1252

Abstract: Yeast studies identified the evolutionarily conserved core ATG genes responsible for autophagosome formation. However, the SNARE-dependent machinery involved in autophagosome fusion with the vacuole in yeast is not conserved. We recently reported that ... ...

Abstract	Yeast studies identified the evolutionarily conserved core ATG genes responsible for autophagosome formation. However, the SNARE-dependent machinery involved in autophagosome fusion with the vacuole in yeast is not conserved. We recently reported that the SNARE complex consisting of Syx17 (Syntaxin 17), ubisnap (SNAP-29) and Vamp7 is required for the fusion of autophagosomes with late endosomes and lysosomes in Drosophila. Syx17 mutant flies are viable but exhibit neuronal dysfunction, locomotion defects and premature death. These data point to the critical role of autophagosome clearance in organismal homeodynamics.
MeSH term(s)	Animals ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology ; Lysosomes/metabolism ; Neurons/metabolism ; Phagosomes/physiology ; Qa-SNARE Proteins/metabolism ; R-SNARE Proteins/metabolism ; SNARE Proteins/metabolism
Chemical Substances	Drosophila Proteins ; Qa-SNARE Proteins ; R-SNARE Proteins ; SNARE Proteins
Language	English
Publishing date	2013-06-25
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.4161/auto.25470
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Article ; Online: iFly: The eye of the fruit fly as a model to study autophagy and related trafficking pathways.

Lőrincz, Péter / Takáts, Szabolcs / Kárpáti, Manuéla / Juhász, Gábor

Experimental eye research

2016 Volume 144, Page(s) 90–98

Abstract: Autophagy is a process by which eukaryotic cells degrade and recycle their intracellular components within lysosomes. Autophagy is induced by starvation to ensure survival of individual cells, and it has evolved to fulfill numerous additional roles in ... ...

Abstract	Autophagy is a process by which eukaryotic cells degrade and recycle their intracellular components within lysosomes. Autophagy is induced by starvation to ensure survival of individual cells, and it has evolved to fulfill numerous additional roles in animals. Autophagy not only provides nutrient supply through breakdown products during starvation, but it is also required for the elimination of damaged or surplus organelles, toxic proteins, aggregates, and pathogens, and is essential for normal organelle turnover. Because of these roles, defects in autophagy have pathological consequences. Here we summarize the current knowledge of autophagy and related trafficking pathways in a convenient model: the compound eye of the fruit fly Drosophila melanogaster. In our review, we present a general introduction of the development and structure of the compound eye. This is followed by a discussion of various neurodegeneration models including retinopathies, with special emphasis on the protective role of autophagy against these diseases.
MeSH term(s)	Animals ; Autophagy ; Cell Movement ; Compound Eye, Arthropod/physiology ; Disease Models, Animal ; Drosophila melanogaster ; Nerve Degeneration/physiopathology ; Nerve Degeneration/prevention & control ; Protein Transport/physiology ; Retinal Diseases/physiopathology ; Retinal Diseases/prevention & control
Language	English
Publishing date	2016-03
Publishing country	England
Document type	Journal Article
ZDB-ID	80122-7
ISSN	1096-0007 ; 0014-4835
ISSN (online)	1096-0007
ISSN	0014-4835
DOI	10.1016/j.exer.2015.06.013
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Article ; Online: Small GTPases controlling autophagy-related membrane traffic in yeast and metazoans.

Takáts, Szabolcs / Boda, Attila / Csizmadia, Tamás / Juhász, Gábor

Small GTPases

2016 Volume 9, Issue 6, Page(s) 465–471

Abstract: During macroautophagy, the phagophore-mediated formation of autophagosomes and their subsequent fusion with lysosomes requires extensive transformation of the endomembrane system. Membrane dynamics in eukaryotic cells is regulated by small GTPase ... ...

Abstract	During macroautophagy, the phagophore-mediated formation of autophagosomes and their subsequent fusion with lysosomes requires extensive transformation of the endomembrane system. Membrane dynamics in eukaryotic cells is regulated by small GTPase proteins including Arfs and Rabs. The small GTPase proteins that regulate autophagic membrane traffic are mostly conserved in yeast and metazoans, but there are also several differences. In this mini-review, we compare the small GTPase network of yeast and metazoan cells that regulates autophagy, and point out the similarities and differences in these organisms.
MeSH term(s)	Animals ; Autophagy ; Biological Transport ; Cell Membrane/metabolism ; GTP Phosphohydrolases/metabolism ; Intracellular Space/metabolism ; Yeasts/cytology ; Yeasts/enzymology ; Yeasts/metabolism
Chemical Substances	GTP Phosphohydrolases (EC 3.6.1.-)
Language	English
Publishing date	2016-12-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2682247-7
ISSN	2154-1256 ; 2154-1248
ISSN (online)	2154-1256
ISSN	2154-1248
DOI	10.1080/21541248.2016.1258444
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Article ; Online: Loss of Drosophila Vps16A enhances autophagosome formation through reduced Tor activity.

Takáts, Szabolcs / Varga, Ágnes / Pircs, Karolina / Juhász, Gábor

Autophagy

2015 Volume 11, Issue 8, Page(s) 1209–1215

Abstract: The HOPS tethering complex facilitates autophagosome-lysosome fusion by binding to Syx17 (Syntaxin 17), the autophagosomal SNARE. Here we show that loss of the core HOPS complex subunit Vps16A enhances autophagosome formation and slows down Drosophila ... ...

Abstract	The HOPS tethering complex facilitates autophagosome-lysosome fusion by binding to Syx17 (Syntaxin 17), the autophagosomal SNARE. Here we show that loss of the core HOPS complex subunit Vps16A enhances autophagosome formation and slows down Drosophila development. Mechanistically, Tor kinase is less active in Vps16A mutants likely due to impaired endocytic and biosynthetic transport to the lysosome, a site of its activation. Tor reactivation by overexpression of Rheb suppresses autophagosome formation and restores growth and developmental timing in these animals. Thus, Vps16A reduces autophagosome numbers both by indirectly restricting their formation rate and by directly promoting their clearance. In contrast, the loss of Syx17 blocks autophagic flux without affecting the induction step in Drosophila.
MeSH term(s)	Animals ; Autophagy/physiology ; Cloning, Molecular ; Densitometry ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Endocytosis ; Gene Expression Regulation, Developmental ; Lipids/chemistry ; Lysosomes/metabolism ; Models, Genetic ; Mutation ; Phagosomes/metabolism ; Phosphorylation ; Polymerase Chain Reaction ; Qa-SNARE Proteins/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Up-Regulation ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism
Chemical Substances	Drosophila Proteins ; Lipids ; Qa-SNARE Proteins ; TORC1 protein complex, Drosophila ; Transcription Factors ; VPS16A protein, Drosophila ; Vesicular Transport Proteins
Language	English
Publishing date	2015-06-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2015.1059559
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Article ; Online: Analysis of Drosophila Atg8 proteins reveals multiple lipidation-independent roles.

Jipa, András / Vedelek, Viktor / Merényi, Zsolt / Ürmösi, Adél / Takáts, Szabolcs / Kovács, Attila L / Horváth, Gábor V / Sinka, Rita / Juhász, Gábor

Autophagy

2020 Volume 17, Issue 9, Page(s) 2565–2575

Abstract: Yeast Atg8 and its homologs are involved in autophagosome biogenesis in all eukaryotes. These are the most widely used markers for autophagy thanks to the association of their lipidated forms with autophagic membranes. The Atg8 protein family expanded in ...

Abstract	Yeast Atg8 and its homologs are involved in autophagosome biogenesis in all eukaryotes. These are the most widely used markers for autophagy thanks to the association of their lipidated forms with autophagic membranes. The Atg8 protein family expanded in animals and plants, with most
MeSH term(s)	Animals ; Autophagy/genetics ; Autophagy-Related Protein 8 Family/genetics ; Autophagy-Related Protein 8 Family/metabolism ; Drosophila Proteins/genetics ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Microtubule-Associated Proteins/metabolism
Chemical Substances	Atg8a protein, Drosophila ; Autophagy-Related Protein 8 Family ; Drosophila Proteins ; Microtubule-Associated Proteins
Language	English
Publishing date	2020-12-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2020.1856494
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Article ; Online: Drosophila Arl8 is a general positive regulator of lysosomal fusion events.

Boda, Attila / Lőrincz, Péter / Takáts, Szabolcs / Csizmadia, Tamás / Tóth, Sarolta / Kovács, Attila L / Juhász, Gábor

Biochimica et biophysica acta. Molecular cell research

2018 Volume 1866, Issue 4, Page(s) 533–544

Abstract: The small GTPase Arl8 is known to be involved in the periphery-directed motility of lysosomes. However, the overall importance of moving these vesicles is still poorly understood. Here we show that Drosophila Arl8 is required not only for the proper ... ...

Abstract	The small GTPase Arl8 is known to be involved in the periphery-directed motility of lysosomes. However, the overall importance of moving these vesicles is still poorly understood. Here we show that Drosophila Arl8 is required not only for the proper distribution of lysosomes, but also for autophagosome-lysosome fusion in starved fat cells, endosome-lysosome fusion in garland nephrocytes, and developmentally programmed secretory granule degradation (crinophagy) in salivary gland cells. Moreover, proper Arl8 localization to lysosomes depends on the shared subunits of the BLOC-1 and BORC complexes, which also promote autophagy and crinophagy. In conclusion, we demonstrate that Arl8 is responsible not only for positioning lysosomes but also acts as a general lysosomal fusion factor.
MeSH term(s)	ADP-Ribosylation Factors/genetics ; ADP-Ribosylation Factors/metabolism ; ADP-Ribosylation Factors/physiology ; Animals ; Autophagosomes/physiology ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila Proteins/physiology ; Drosophila melanogaster/physiology ; Drosophila melanogaster/ultrastructure ; Lysosomes/metabolism ; Lysosomes/physiology ; Lysosomes/ultrastructure ; Membrane Fusion ; Protein Subunits/physiology ; rab GTP-Binding Proteins/physiology
Chemical Substances	Arl8 protein, Drosophila ; Drosophila Proteins ; Protein Subunits ; ADP-Ribosylation Factors (EC 3.6.5.2) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2018-12-24
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2018.12.011
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Article ; Online: Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion.

Takáts, Szabolcs / Glatz, Gábor / Szenci, Győző / Boda, Attila / Horváth, Gábor V / Hegedűs, Krisztina / Kovács, Attila L / Juhász, Gábor

PLoS genetics

2018 Volume 14, Issue 4, Page(s) e1007359

Abstract: The autophagosomal SNARE Syntaxin17 (Syx17) forms a complex with Snap29 and Vamp7/8 to promote autophagosome-lysosome fusion via multiple interactions with the tethering complex HOPS. Here we demonstrate that, unexpectedly, one more SNARE (Ykt6) is also ... ...

Abstract	The autophagosomal SNARE Syntaxin17 (Syx17) forms a complex with Snap29 and Vamp7/8 to promote autophagosome-lysosome fusion via multiple interactions with the tethering complex HOPS. Here we demonstrate that, unexpectedly, one more SNARE (Ykt6) is also required for autophagosome clearance in Drosophila. We find that loss of Ykt6 leads to large-scale accumulation of autophagosomes that are unable to fuse with lysosomes to form autolysosomes. Of note, loss of Syx5, the partner of Ykt6 in ER-Golgi trafficking does not prevent autolysosome formation, pointing to a more direct role of Ykt6 in fusion. Indeed, Ykt6 localizes to lysosomes and autolysosomes, and forms a SNARE complex with Syx17 and Snap29. Interestingly, Ykt6 can be outcompeted from this SNARE complex by Vamp7, and we demonstrate that overexpression of Vamp7 rescues the fusion defect of ykt6 loss of function cells. Finally, a point mutant form with an RQ amino acid change in the zero ionic layer of Ykt6 protein that is thought to be important for fusion-competent SNARE complex assembly retains normal autophagic activity and restores full viability in mutant animals, unlike palmitoylation or farnesylation site mutant Ykt6 forms. As Ykt6 and Vamp7 are both required for autophagosome-lysosome fusion and are mutually exclusive subunits in a Syx17-Snap29 complex, these data suggest that Vamp7 is directly involved in membrane fusion and Ykt6 acts as a non-conventional, regulatory SNARE in this process.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Autophagosomes/physiology ; Binding Sites ; Drosophila Proteins/genetics ; Drosophila Proteins/physiology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/physiology ; Lysosomes/physiology ; Membrane Fusion/genetics ; Membrane Fusion/physiology ; Models, Biological ; Multiprotein Complexes/genetics ; Multiprotein Complexes/physiology ; Qa-SNARE Proteins/genetics ; Qa-SNARE Proteins/physiology ; R-SNARE Proteins/genetics ; R-SNARE Proteins/physiology ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; SNARE Proteins/genetics ; SNARE Proteins/physiology
Chemical Substances	Drosophila Proteins ; Multiprotein Complexes ; Qa-SNARE Proteins ; R-SNARE Proteins ; Recombinant Proteins ; SNARE Proteins ; Snap29 protein, Drosophila ; VAMP7 protein, Drosophila
Language	English
Publishing date	2018-04-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1007359
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