@article{MTMT:35447765, title = {The Rab7-Epg5 and Rab39-ema modules cooperately position autophagosomes for efficient lysosomal fusions}, url = {https://m2.mtmt.hu/api/publication/35447765}, author = {Boda, Attila and Balázs, Villő and Nagy, Anikó Zsuzsanna and Hargitai, Dávid and Lippai, Mónika and Simon-Vecsei, Zsófia Judit and Molnár, Márton and Fürstenhoffer, Fanni and Juhász, Gábor and Lőrincz, Péter}, doi = {10.7554/eLife.102663.1}, journal-iso = {ELIFE}, journal = {ELIFE}, unique-id = {35447765}, issn = {2050-084X}, year = {2024}, eissn = {2050-084X}, orcid-numbers = {Boda, Attila/0000-0003-1811-8595; Nagy, Anikó Zsuzsanna/0000-0002-0979-1617; Lippai, Mónika/0000-0002-7307-4233; Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Juhász, Gábor/0000-0001-8548-8874; Lőrincz, Péter/0000-0001-7374-667X} } @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}, 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:34720930, title = {A “torn bag mechanism” of small extracellular vesicle release via limiting membrane rupture of en bloc released amphisomes (amphiectosomes)}, url = {https://m2.mtmt.hu/api/publication/34720930}, author = {Visnovitz, Tamás and Lenzinger, Dorina and Koncz, Anna and Vizi, Péter M and Bárkai, Tünde and Visnovitzné Dr Vukman, Krisztina and Galinsoga, Alicia and Németh, Krisztina and Fletcher, Kelsey and Komlósi, Zsolt and Lőrincz, Péter and Valcz, Gábor and Buzás, Edit Irén}, doi = {10.7554/eLife.95828.1}, journal-iso = {ELIFE}, journal = {ELIFE}, volume = {13}, unique-id = {34720930}, issn = {2050-084X}, year = {2024}, eissn = {2050-084X}, orcid-numbers = {Visnovitz, Tamás/0000-0002-7962-5083; Koncz, Anna/0000-0003-2511-2394; Németh, Krisztina/0000-0002-3825-2137; Komlósi, Zsolt/0000-0002-4149-1497; Lőrincz, Péter/0000-0001-7374-667X; Valcz, Gábor/0000-0002-7109-3529; Buzás, Edit Irén/0000-0002-3744-206X} } @CONFERENCE{MTMT:34684460, title = {Convergent evolution in glutamate dehydrogenase activity in Drosophila and human}, url = {https://m2.mtmt.hu/api/publication/34684460}, author = {Vedelek, Viktor and Balázs, Vedelek and Gabor, Juhasz and Lőrincz, Péter and Sinka, Rita}, booktitle = {27th European Drosophila Research Conference}, unique-id = {34684460}, year = {2023}, orcid-numbers = {Lőrincz, Péter/0000-0001-7374-667X; Sinka, Rita/0000-0003-4040-4184} } @misc{MTMT:34486423, title = {Nanoinjection of fluorescent and gold nanoparticles to single live cells by robotic fluidic force microscopy}, url = {https://m2.mtmt.hu/api/publication/34486423}, author = {Kovács, Kinga Dóra and Visnovitz, Tamás and Kanyó, Nicolett and Gerecsei, Tamás and Péter, Beatrix and Lagzi, István and Kurunczi, Sándor and Koncz, Anna and Németh, Krisztina and Lenzinger, Dorina and V. Vukman, Krisztina and Molnár, Kinga and Truszka, Mónika and Nakanishi, Hideyuki and Lőrincz, Péter and Székács, Inna and Buzás, Edit I. and Horváth, Róbert}, unique-id = {34486423}, year = {2023}, orcid-numbers = {Visnovitz, Tamás/0000-0002-7962-5083; Kurunczi, Sándor/0000-0002-6567-5231; Lőrincz, Péter/0000-0001-7374-667X; Horváth, Róbert/0000-0001-8617-2302} } @{MTMT:34486404, title = {Nanoinjection of fluorescent nanoparticles to single live cells by robotic fluidic force microscopy}, url = {https://m2.mtmt.hu/api/publication/34486404}, author = {Kovács, Kinga Dóra and Visnovitz, Tamás and Gerecsei, Tamás and Péter, Beatrix and Kurunczi, Sándor and Koncz, Anna and Németh, Krisztina and Lenzinger, Dorina and V. Vukman, Krisztina and Lőrincz, Péter and Székács, Inna and Buzás, Edit I. and Horváth, Róbert}, booktitle = {Magyar Biofizikai Társaság XXIX. Kongresszusa}, unique-id = {34486404}, year = {2023}, pages = {35-35}, orcid-numbers = {Visnovitz, Tamás/0000-0002-7962-5083; Kurunczi, Sándor/0000-0002-6567-5231; Lőrincz, Péter/0000-0001-7374-667X; Horváth, Róbert/0000-0001-8617-2302} } @article{MTMT:34425078, title = {Nanoinjection of extracellular vesicles to single live cells by robotic fluidic force microscopy}, url = {https://m2.mtmt.hu/api/publication/34425078}, author = {Kovács, Kinga Dóra and Visnovitz, Tamás and Gerecsei, Tamás and Péter, Beatrix and Kurunczi, Sándor and Koncz, Anna and Németh, Krisztina and Lenzinger, Dorina and Visnovitzné Dr Vukman, Krisztina and Balogh, Anna and Rajmon, Imola and Lőrincz, Péter and Székács, Inna and Buzás, Edit Irén and Horváth, Róbert}, doi = {10.1002/jev2.12388}, journal-iso = {J EXTRACELLULAR VESICL}, journal = {JOURNAL OF EXTRACELLULAR VESICLES}, volume = {12}, unique-id = {34425078}, abstract = {In the past decade, extracellular vesicles (EVs) have attracted substantial interest in biomedicine. With progress in the field, we have an increasing understanding of cellular responses to EVs. In this Technical Report, we describe the direct nanoinjection of EVs into the cytoplasm of single cells of different cell lines. By using robotic fluidic force microscopy (robotic FluidFM), nanoinjection of GFP positive EVs and EV‐like particles into single live HeLa, H9c2, MDA‐MB‐231 and LCLC‐103H cells proved to be feasible. This injection platform offered the advantage of high cell selectivity and efficiency. The nanoinjected EVs were initially localized in concentrated spot‐like regions within the cytoplasm. Later, they were transported towards the periphery of the cells. Based on our proof‐of‐principle data, robotic FluidFM is suitable for targeting single living cells by EVs and may lead to information about intracellular EV cargo delivery at a single‐cell level.}, year = {2023}, eissn = {2001-3078}, orcid-numbers = {Visnovitz, Tamás/0000-0002-7962-5083; Kurunczi, Sándor/0000-0002-6567-5231; Koncz, Anna/0000-0003-2511-2394; Németh, Krisztina/0000-0002-3825-2137; Lőrincz, Péter/0000-0001-7374-667X; Buzás, Edit Irén/0000-0002-3744-206X; Horváth, Róbert/0000-0001-8617-2302} } @article{MTMT:34239207, title = {A comparative analysis of fruit fly and human glutamate dehydrogenases in Drosophila melanogaster sperm development}, url = {https://m2.mtmt.hu/api/publication/34239207}, author = {Vedelek, Viktor and Vedelek, Balázs and Lőrincz, Péter and Juhász, Gábor and Sinka, Rita}, doi = {10.3389/fcell.2023.1281487}, journal-iso = {FRONT CELL DEV BIOL}, journal = {FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY}, volume = {11}, unique-id = {34239207}, issn = {2296-634X}, abstract = {Glutamate dehydrogenases are enzymes that take part in both amino acid and energy metabolism. Their role is clear in many biological processes, from neuronal function to cancer development. The putative testis-specific Drosophila glutamate dehydrogenase, Bb8, is required for male fertility and the development of mitochondrial derivatives in spermatids. Testis-specific genes are less conserved and could gain new functions, thus raising a question whether Bb8 has retained its original enzymatic activity. We show that while Bb8 displays glutamate dehydrogenase activity, there are significant functional differences between the housekeeping Gdh and the testis-specific Bb8. Both human GLUD1 and GLUD2 can rescue the bb8 ms mutant phenotype, with superior performance by GLUD2. We also tested the role of three conserved amino acids observed in both Bb8 and GLUD2 in Gdh mutants, which showed their importance in the glutamate dehydrogenase function. The findings of our study indicate that Drosophila Bb8 and human GLUD2 could be novel examples of convergent molecular evolution. Furthermore, we investigated the importance of glutamate levels in mitochondrial homeostasis during spermatogenesis by ectopic expression of the mitochondrial glutamate transporter Aralar1, which caused mitochondrial abnormalities in fly spermatids. The data presented in our study offer evidence supporting the significant involvement of glutamate metabolism in sperm development.}, year = {2023}, eissn = {2296-634X}, orcid-numbers = {Vedelek, Balázs/0000-0001-6981-0026; Lőrincz, Péter/0000-0001-7374-667X; Juhász, Gábor/0000-0001-8548-8874; Sinka, Rita/0000-0003-4040-4184} } @article{MTMT:34021340, title = {Interaction of the sorting nexin 25 homologue Snazarus with Rab11 balances endocytic and secretory transport and maintains the ultrafiltration diaphragm in nephrocytes}, url = {https://m2.mtmt.hu/api/publication/34021340}, author = {Maruzs, Tamás and Feil-Börcsök, Dalma and Lakatos, Enikő and Juhász, Gábor and Blastyák, András and Hargitai, Dávid and Jean, Steve and Lőrincz, Péter and Juhász, Gábor}, doi = {10.1091/mbc.E22-09-0421}, journal-iso = {MOL BIOL CELL}, journal = {MOLECULAR BIOLOGY OF THE CELL}, volume = {34}, unique-id = {34021340}, issn = {1059-1524}, abstract = {Proper balance of exocytosis and endocytosis is important for the maintenance of plasma membrane lipid and protein homeostasis. This is especially critical in human podocytes and the podocyte-like Drosophila nephrocytes that both use a delicate diaphragm system with evolutionarily conserved components for ultrafiltration. Here we show that the sorting nexin 25 homolog Snazarus (Snz) binds to Rab11 and localizes to Rab11-positive recycling endosomes in Drosophila nephrocytes, unlike in fat cells where it is present in plasma membrane/lipid droplet/ER contact sites. Loss of Snz leads to redistribution of Rab11 vesicles from the cell periphery and increases endocytic activity in nephrocytes. These changes are accompanied by defects in diaphragm protein distribution that resemble those seen in Rab11 gain-of-function cells. Of note, co-overexpression of Snz rescues diaphragm defects in Rab11 overexpressing cells, whereas snz knockdown in Rab11 overexpressing nephrocytes or simultaneous knockdown of snz and tbc1d8b encoding a Rab11 GAP lead to massive expansion of the lacunar system that contains mislocalized diaphragm components: Sns and Pyd/ZO-1. We find that loss of Snz enhances while its overexpression impairs secretion, which, together with genetic epistasis analyses, suggest that Snz counteracts Rab11 to maintain the diaphragm via setting the proper balance of exocytosis and endocytosis.}, year = {2023}, eissn = {1939-4586}, orcid-numbers = {Maruzs, Tamás/0000-0001-8142-3221; Feil-Börcsök, Dalma/0000-0003-0823-201X; Lőrincz, Péter/0000-0001-7374-667X; Juhász, Gábor/0000-0001-8548-8874} } @article{MTMT:33750753, title = {Endoplasmin Is a Hypoxia-Inducible Endoplasmic Reticulum-Derived Cargo of Extracellular Vesicles Released by Cardiac Cell Lines}, url = {https://m2.mtmt.hu/api/publication/33750753}, author = {Koncz, Anna and Turiák, Lilla and Németh, Krisztina and Lenzinger, Dorina and Bárkai, Tünde and Lőrincz, Péter and Zelenyánszki, Helga and Visnovitzné Dr Vukman, Krisztina and Buzás, Edit Irén and Visnovitz, Tamás}, doi = {10.3390/membranes13040431}, journal-iso = {MEMBRANES-BASEL}, journal = {MEMBRANES (BASEL)}, volume = {13}, unique-id = {33750753}, abstract = {Cardiomyopathies are leading causes of human mortality. Recent data indicate that the cardiomyocyte-derived extracellular vesicles (EVs) released upon cardiac injury are present in circulation. This paper aimed to analyze EVs released under normal and hypoxic conditions by H9c2 (rat), AC16 (human) and HL1 (mouse) cardiac cell lines. Small (sEVs), medium (mEVs) and large EVs (lEVs) were separated from a conditioned medium by a combination of gravity filtration, differential centrifugation and tangential flow filtration. The EVs were characterized by microBCA, SPV lipid assay, nanoparticle tracking analysis, transmission and immunogold electron microscopy, flow cytometry and Western blotting. Proteomic profiles of the EVs were determined. Surprisingly, an endoplasmic reticulum chaperone, endoplasmin (ENPL, grp94 or gp96), was identified in the EV samples, and its association with EVs was validated. The secretion and uptake of ENPL was followed by confocal microscopy using GFP-ENPL fusion protein expressing HL1 cells. We identified ENPL as an internal cargo of cardiomyocyte-derived mEVs and sEVs. Based on our proteomic analysis, its presence in EVs was linked to hypoxia in HL1 and H9c2 cells, and we hypothesize that EV-associated ENPL may have a cardioprotective role by reducing cardiomyocyte ER stress.}, year = {2023}, eissn = {2077-0375}, orcid-numbers = {Koncz, Anna/0000-0003-2511-2394; Németh, Krisztina/0000-0002-3825-2137; Lőrincz, Péter/0000-0001-7374-667X; Zelenyánszki, Helga/0000-0001-6768-3748; Buzás, Edit Irén/0000-0002-3744-206X; Visnovitz, Tamás/0000-0002-7962-5083} }