@article{MTMT:34837906,
	title = {CORVET-specific subunit levels determine the balance between HOPS/CORVET endosomal tethering complexes},
	url = {https://m2.mtmt.hu/api/publication/34837906},
	author = {Sőth, Ármin and Molnár, Márton and Lőrincz, Péter and Simon-Vecsei, Zsófia Judit and Juhász, Gábor},
	doi = {10.1038/s41598-024-59775-0},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {14},
	unique-id = {34837906},
	issn = {2045-2322},
	abstract = {The closely related endolysosomal tethering complexes HOPS and CORVET play pivotal roles in the homo- and heterotypic fusion of early and late endosomes, respectively, and HOPS also mediates the fusion of lysosomes with incoming vesicles including late endosomes and autophagosomes. These heterohexameric complexes share their four core subunits that assemble with additional two, complex-specific subunits. These features and the similar structure of the complexes could allow the formation of hybrid complexes, and the complex specific subunits may compete for binding to the core. Indeed, our biochemical analyses revealed the overlap of binding sites for HOPS-specific VPS41 and CORVET-specific VPS8 on the shared core subunit VPS18. We found that the overexpression of CORVET-specific VPS8 or Tgfbrap1 decreased the amount of core proteins VPS11 and VPS18 that are assembled with HOPS-specific subunits VPS41 or VPS39, indicating reduced amount of assembled HOPS. In line with this, we observed the elevation of both lipidated, autophagosome-associated LC3 protein and the autophagic cargo p62 in these cells, suggesting impaired autophagosome-lysosome fusion. In contrast, overexpression of HOPS-specific VPS39 or VPS41 did not affect the level of assembled CORVET or autophagy. VPS8 or Tgfbrap1 overexpression also induced Cathepsin D accumulation, suggesting that HOPS-dependent biosynthetic delivery of lysosomal hydrolases is perturbed, too. These indicate that CORVET-specific subunit levels fine-tune HOPS assembly and activity in vivo.},
	year = {2024},
	eissn = {2045-2322},
	orcid-numbers = {Lőrincz, Péter/0000-0001-7374-667X; Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Juhász, Gábor/0000-0001-8548-8874}
}

@article{MTMT:33569878,
	title = {Correction to: Pathways of integrins in the endo-lysosomal system},
	url = {https://m2.mtmt.hu/api/publication/33569878},
	author = {Molnár, Márton and Sőth, Ármin and Simon-Vecsei, Zsófia Judit},
	doi = {10.1007/s42977-022-00143-2},
	journal-iso = {BIOL FUTURA},
	journal = {BIOLOGIA FUTURA},
	volume = {73},
	unique-id = {33569878},
	issn = {2676-8615},
	year = {2022},
	eissn = {2676-8607},
	pages = {513-513},
	orcid-numbers = {Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895}
}

@article{MTMT:32819271,
	title = {Pathways of integrins in the endo-lysosomal system},
	url = {https://m2.mtmt.hu/api/publication/32819271},
	author = {Molnár, Márton and Sőth, Ármin and Simon-Vecsei, Zsófia Judit},
	doi = {10.1007/s42977-022-00120-9},
	journal-iso = {BIOL FUTURA},
	journal = {BIOLOGIA FUTURA},
	volume = {73},
	unique-id = {32819271},
	issn = {2676-8615},
	year = {2022},
	eissn = {2676-8607},
	pages = {171-185},
	orcid-numbers = {Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895}
}

@article{MTMT:32543729,
	title = {Ion Channels and Pumps in Autophagy: A Reciprocal Relationship},
	url = {https://m2.mtmt.hu/api/publication/32543729},
	author = {Abuammar, Hussein and Bhattacharjee, Arindam and Simon-Vecsei, Zsófia Judit and Blastyák, András and Csordás, Gábor and Páli, Tibor and Juhász, Gábor},
	doi = {10.3390/cells10123537},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {10},
	unique-id = {32543729},
	year = {2021},
	eissn = {2073-4409},
	orcid-numbers = {Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Csordás, Gábor/0000-0001-6871-6839; Páli, Tibor/0000-0003-1649-1097; Juhász, Gábor/0000-0001-8548-8874}
}

@article{MTMT:31952974,
	title = {Identification of new interactions between endolysosomal tethering factors},
	url = {https://m2.mtmt.hu/api/publication/31952974},
	author = {Simon-Vecsei, Zsófia Judit and Sőth, Ármin and Lőrincz, Péter and Rubics, András and Tálas, András and Kulcsár, Péter István and Juhász, Gábor},
	doi = {10.1016/j.jmb.2021.166965},
	journal-iso = {J MOL BIOL},
	journal = {JOURNAL OF MOLECULAR BIOLOGY},
	volume = {443},
	unique-id = {31952974},
	issn = {0022-2836},
	year = {2021},
	eissn = {1089-8638},
	orcid-numbers = {Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Lőrincz, Péter/0000-0001-7374-667X; Kulcsár, Péter István/0000-0002-7783-5108; Juhász, Gábor/0000-0001-8548-8874}
}

@article{MTMT:31279236,
	title = {The Warburg Micro Syndrome-associated Rab3GAP-Rab18 module promotes autolysosome maturation through the Vps34 Complex I},
	url = {https://m2.mtmt.hu/api/publication/31279236},
	author = {Takáts, Szabolcs and Lévay, Luca and Boda, Attila and Tóth, Sarolta and Simon-Vecsei, Zsófia Judit and Rubics, András and Varga, Ágnes and Lippai, Mónika and Lőrincz, Péter and Glatz, Gábor and Juhász, Gábor},
	doi = {10.1111/febs.15313},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	volume = {288},
	unique-id = {31279236},
	issn = {1742-464X},
	year = {2021},
	eissn = {1742-4658},
	pages = {190-211},
	orcid-numbers = {Takáts, Szabolcs/0000-0003-2139-7740; Boda, Attila/0000-0003-1811-8595; Tóth, Sarolta/0000-0002-0341-7675; Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Lippai, Mónika/0000-0002-7307-4233; Lőrincz, Péter/0000-0001-7374-667X; Juhász, Gábor/0000-0001-8548-8874}
}

@article{MTMT:30969186,
	title = {Drosophila Atg9 regulates the actin cytoskeleton via interactions with profilin and Ena},
	url = {https://m2.mtmt.hu/api/publication/30969186},
	author = {Kiss, Viktória and Jipa, András and Varga, Kata and Takáts, Szabolcs and Maruzs, Tamás and Lőrincz, Péter and Simon-Vecsei, Zsófia Judit and Szikora, Szilárd and Földi, István and Bajusz, Csaba and Tóth, Dávid and Vilmos, Péter and Gáspár, Imre and Ronchi, Paolo and Mihály, József and Juhász, Gábor},
	doi = {10.1038/s41418-019-0452-0},
	journal-iso = {CELL DEATH DIFFER},
	journal = {CELL DEATH AND DIFFERENTIATION},
	volume = {27},
	unique-id = {30969186},
	issn = {1350-9047},
	abstract = {Autophagy ensures the turnover of cytoplasm and requires the coordinated action of Atg proteins, some of which also have moonlighting functions in higher eukaryotes. Here we show that the transmembrane protein Atg9 is required for female fertility, and its loss leads to defects in actin cytoskeleton organization in the ovary and enhances filopodia formation in neurons in Drosophila. Atg9 localizes to the plasma membrane anchor points of actin cables and is also important for the integrity of the cortical actin network. Of note, such phenotypes are not seen in other Atg mutants, suggesting that these are independent of autophagy defects. Mechanistically, we identify the known actin regulators profilin and Ena/VASP as novel binding partners of Atg9 based on microscopy, biochemical, and genetic interactions. Accordingly, the localization of both profilin and Ena depends on Atg9. Taken together, our data identify a new and unexpected role for Atg9 in actin cytoskeleton regulation.},
	year = {2020},
	eissn = {1476-5403},
	pages = {1677-1692},
	orcid-numbers = {Jipa, András/0000-0003-4880-7666; Takáts, Szabolcs/0000-0003-2139-7740; Maruzs, Tamás/0000-0001-8142-3221; Lőrincz, Péter/0000-0001-7374-667X; Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Tóth, Dávid/0000-0002-1076-3031; Juhász, Gábor/0000-0001-8548-8874}
}

@{MTMT:30808003,
	title = {Investigation of the interaction of two endosomal tethering factors, Rabenosyn-5 and Vps18},
	url = {https://m2.mtmt.hu/api/publication/30808003},
	author = {Sőth, Ármin and Simon-Vecsei, Zsófia Judit and Kulcsár, Péter István and Tálas, András and Welker, Ervin and Juhász, Gábor},
	booktitle = {Hungarian Molecular Life Sciences 2019: Programme and Books of abstracts},
	unique-id = {30808003},
	year = {2019},
	pages = {234},
	orcid-numbers = {Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Kulcsár, Péter István/0000-0002-7783-5108; Juhász, Gábor/0000-0001-8548-8874}
}

@{MTMT:30807940,
	title = {Loss of Vps18 affect autophagy and cell adhesion of mammalian cells},
	url = {https://m2.mtmt.hu/api/publication/30807940},
	author = {Simon-Vecsei, Zsófia Judit and Sőth, Ármin and Kulcsár, Péter István and Tálas, András and Welker, Ervin and Juhász, Gábor},
	booktitle = {Hungarian Molecular Life Sciences 2019: Programme and Books of abstracts},
	unique-id = {30807940},
	year = {2019},
	pages = {237},
	orcid-numbers = {Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Kulcsár, Péter István/0000-0002-7783-5108; Juhász, Gábor/0000-0001-8548-8874}
}

@article{MTMT:30767841,
	title = {On the Fly: Recent Progress on Autophagy and Aging in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/30767841},
	author = {Maruzs, Tamás and Simon-Vecsei, Zsófia Judit and Kiss, Viktória and Csizmadia, Tamás and Juhász, Gábor},
	doi = {10.3389/fcell.2019.00140},
	journal-iso = {FRONT CELL DEV BIOL},
	journal = {FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY},
	volume = {7},
	unique-id = {30767841},
	issn = {2296-634X},
	abstract = {Autophagy ensures the lysosome-mediated breakdown and recycling of self-material, as it not only degrades obsolete or damaged intracellular constituents but also provides building blocks for biosynthetic and energy producing reactions. Studies in animal models including Drosophila revealed that autophagy defects lead to the rapid decline of neuromuscular function, neurodegeneration, sensitivity to stress (such as starvation or oxidative damage), and stem cell loss. Of note, recently identified human Atg gene mutations cause similar symptoms including ataxia and mental retardation. Physiologically, autophagic degradation (flux) is known to decrease during aging, and this defect likely contributes to the development of such age-associated diseases. Many manipulations that extend lifespan (including dietary restriction, reduced TOR kinase signaling, exercise or treatment with various anti-aging substances) require autophagy for their beneficial effect on longevity, pointing to the key role of this housekeeping process. Importantly, genetic (e.g., Atg8a overexpression in either neurons or muscle) or pharmacological (e.g., feeding rapamycin or spermidine to animals) promotion of autophagy has been successfully used to extend lifespan in Drosophila, suggesting that this intracellular degradation pathway can rejuvenate cells and organisms. In this review, we highlight key discoveries and recent progress in understanding the relationship of autophagy and aging in Drosophila.},
	keywords = {DROSOPHILA; Aging; Autophagy; spermidine; dietary restriction (DR)},
	year = {2019},
	eissn = {2296-634X},
	orcid-numbers = {Maruzs, Tamás/0000-0001-8142-3221; Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Csizmadia, Tamás/0000-0002-2098-9165; Juhász, Gábor/0000-0001-8548-8874}
}