@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:3346802, title = {Sex-specific regulation of aging in Caenorhabditis elegans}, url = {https://m2.mtmt.hu/api/publication/3346802}, author = {Hotzi, Bernadette and Kosztelnik, Mónika and Hargitai, Balázs and Vellainé Takács, Krisztina and Barna, János and Bördén, Ka and Málnási Csizmadia, András and Lippai, Mónika and Ortutay, Csaba Péter and Bacquet, C and Pasparaki, A and Arányi, Tamás and Tavernarakis, N and Vellai, Tibor}, doi = {10.1111/acel.12724}, journal-iso = {AGING CELL}, journal = {AGING CELL}, volume = {17}, unique-id = {3346802}, issn = {1474-9718}, abstract = {A fascinating aspect of sexual dimorphism in various animal species is that the two sexes differ substantially in lifespan. In humans, for example, women's life expectancy exceeds that of men by 3-7 years. Whether this trait can be attributed to dissimilar lifestyles or genetic (regulatory) factors remains to be elucidated. Herein, we demonstrate that in the nematode Caenorhabditis elegans, the significantly longer lifespan of hermaphrodites-which are essentially females capable of sperm production-over males is established by TRA-1, the terminal effector of the sex-determination pathway. This transcription factor directly controls the expression of daf-16/FOXO, which functions as a major target of insulin/IGF-1 signaling (IIS) and key modulator of aging across diverse animal phyla. TRA-1 extends hermaphrodite lifespan through promoting daf-16 activity. Furthermore, TRA-1 also influences reproductive growth in a DAF-16-dependent manner. Thus, the sex-determination machinery is an important regulator of IIS in this organism. These findings provide a mechanistic insight into how longevity and development are specified unequally in the two genders. As TRA-1 is orthologous to mammalian GLI (glioma-associated) proteins, a similar sex-specific mechanism may also operate in humans to determine lifespan. © 2018 The Anatomical Society and John Wiley & Sons Ltd.}, keywords = {LIFE-SPAN; GENE; DIFFERENTIATION; PROTEINS; TRANSCRIPTION; C-ELEGANS; DEATH; LONGEVITY; INSULIN; Aging; Caenorhabditis elegans; sex determination; foxo; DAF-16; Dauer development; TRA-1/GLI; TRA-1; IGF-1 signaling}, year = {2018}, eissn = {1474-9726}, orcid-numbers = {Hotzi, Bernadette/0000-0003-1433-6843; Kosztelnik, Mónika/0000-0001-6735-3597; Vellainé Takács, Krisztina/0000-0002-4472-0363; Barna, János/0000-0002-9242-0939; Málnási Csizmadia, András/0000-0002-2430-8398; Lippai, Mónika/0000-0002-7307-4233; Ortutay, Csaba Péter/0000-0001-6306-6101; Vellai, Tibor/0000-0002-3520-2572} } @article{MTMT:3278744, title = {Drosophila Atg16 promotes enteroendocrine cell differentiation via regulation of intestinal Slit/Robo signaling.}, url = {https://m2.mtmt.hu/api/publication/3278744}, author = {Nagy, Péter and Szatmári, Zsuzsanna and Sándor, Gyöngyvér Orsolya and Lippai, Mónika and Hegedűs, Krisztina and Juhász, Gábor}, doi = {10.1242/dev.147033}, journal-iso = {DEVELOPMENT}, journal = {DEVELOPMENT}, volume = {144}, unique-id = {3278744}, issn = {0950-1991}, abstract = {Genetic variations of Atg16L1, Slit and Rab19 predispose to the development of inflammatory bowel disease (IBD), but the relationship of these mutations is unclear. Here we show that in Drosophila guts lacking the WD40 domain of Atg16, pre-enteroendocrine cells (pre-EEs) accumulate that fail to differentiate into properly functioning secretory EEs. Mechanistically, loss of Atg16 or its binding partner Rab19 impairs Slit production, which normally inhibits EE generation by activating Robo signaling in stem cells. Importantly, loss of Atg16 or decreased Slit/Robo signaling trigger an intestinal inflammatory response. Surprisingly, analysis of Rab19 and domain-specific Atg16 mutants indicates that their stem cell niche regulatory function is independent of autophagy. Our study reveals how mutations in these different genes may contribute to IBD.}, year = {2017}, eissn = {1477-9129}, pages = {3990-4001}, orcid-numbers = {Nagy, Péter/0000-0002-5053-0646; Sándor, Gyöngyvér Orsolya/0000-0002-0838-2838; Lippai, Mónika/0000-0002-7307-4233; Juhász, Gábor/0000-0001-8548-8874} } @article{MTMT:3158690, title = {Autophagy—from molecular mechanisms to clinical relevance}, url = {https://m2.mtmt.hu/api/publication/3158690}, author = {Lippai, Mónika and Szatmári, Zsuzsanna}, doi = {10.1007/s10565-016-9374-5}, journal-iso = {CELL BIOL TOXICOL}, journal = {CELL BIOLOGY AND TOXICOLOGY}, volume = {33}, unique-id = {3158690}, issn = {0742-2091}, abstract = {Autophagy is a lysosomal degradation pathway of eukaryotic cells that is highly conserved from yeast to mammals. During this process, cooperating protein complexes are recruited in a hierarchic order to the phagophore assembly site (PAS) to mediate the elongation and closure of double-membrane vesicles called autophagosomes, which sequester cytosolic components and deliver their content to the endolysosomal system for degradation. As a major cytoprotective mechanism, autophagy plays a key role in the stress response against nutrient starvation, hypoxia, and infections. Although numerous studies reported that impaired function of core autophagy proteins also contributes to the development and progression of various human diseases such as neurodegenerative disorders, cardiovascular and muscle diseases, infections, and different types of cancer, the function of this process in human diseases remains unclear. Evidence often suggests a controversial role for autophagy in the pathomechanisms of these severe disorders. Here, we provide an overview of the molecular mechanisms of autophagy and summarize the recent advances on its function in human health and disease. © 2016 Springer Science+Business Media Dordrecht}, keywords = {CANCER; INFECTION; cardiovascular disease; Autophagy; NEURODEGENERATIVE DISEASE}, year = {2017}, eissn = {1573-6822}, pages = {145-168}, orcid-numbers = {Lippai, Mónika/0000-0002-7307-4233} } @article{MTMT:30901168, title = {MiniCORVET is a Vps8-containing early endosomal tether in Drosophila}, url = {https://m2.mtmt.hu/api/publication/30901168}, author = {Lőrincz, Péter and Lakatos, Zsolt and Varga, Ágnes and Maruzs, Tamás and Simon-Vecsei, Zsófia Judit and Darula, Zsuzsanna and Benkő, Péter and Csordás, Gábor and Lippai, Mónika and Andó, István and Hegedűs, Krisztina and Medzihradszky F., Katalin and Takáts, Szabolcs and Juhász, Gábor}, doi = {10.7554/eLife.14226}, journal-iso = {ELIFE}, journal = {ELIFE}, volume = {5}, unique-id = {30901168}, issn = {2050-084X}, abstract = {Yeast studies identified two heterohexameric tethering complexes, which consist of 4 shared (Vps11, Vps16, Vps18 and Vps33) and 2 specific subunits: Vps3 and Vps8 (CORVET) versus Vps39 and Vps41 (HOPS). CORVET is an early and HOPS is a late endosomal tether. The function of HOPS is well known in animal cells, while CORVET is poorly characterized. Here we show that Drosophila Vps8 is highly expressed in hemocytes and nephrocytes, and localizes to early endosomes despite the lack of a clear Vps3 homolog. We find that Vps8 forms a complex and acts together with Vps16A, Dor/Vps18 and Car/Vps33A, and loss of any of these proteins leads to fragmentation of endosomes. Surprisingly, Vps11 deletion causes enlargement of endosomes, similar to loss of the HOPS-specific subunits Vps39 and Lt/Nps41. We thus identify a 4 subunit-containing miniCORVET complex as an unconventional early endosomal tether in Drosophila.}, year = {2016}, eissn = {2050-084X}, orcid-numbers = {Lőrincz, Péter/0000-0001-7374-667X; Lakatos, Zsolt/0000-0003-1900-3167; Maruzs, Tamás/0000-0001-8142-3221; Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Benkő, Péter/0000-0002-2050-7509; Csordás, Gábor/0000-0001-6871-6839; Lippai, Mónika/0000-0002-7307-4233; Andó, István/0000-0002-4648-9396; Takáts, Szabolcs/0000-0003-2139-7740; Juhász, Gábor/0000-0001-8548-8874} } @book{MTMT:3165682, title = {Állatszervezettani Gyakorlatok}, url = {https://m2.mtmt.hu/api/publication/3165682}, author = {Csikós, György and Csizmadia, Tamás and Csörgő, Tibor and Kárpáti, Manuéla and Kis, Viktor and Dr. Kovács, Attila and Molnár, Kinga and Pálfia, Zsolt}, editor = {Lippai, Mónika}, publisher = {ELTE TTK}, unique-id = {3165682}, year = {2015}, orcid-numbers = {Csikós, György/0000-0002-5881-5363; Csizmadia, Tamás/0000-0002-2098-9165; Csörgő, Tibor/0000-0002-7060-9853; Molnár, Kinga/0000-0002-7196-5331; Pálfia, Zsolt/0000-0002-4277-8131; Lippai, Mónika/0000-0002-7307-4233} } @article{MTMT:2941631, title = {Specialized Cortex Glial Cells Accumulate Lipid Droplets in Drosophila melanogaster}, url = {https://m2.mtmt.hu/api/publication/2941631}, author = {Kis, Viktor and Barti, Benjámin and Lippai, Mónika and Sass, Miklós}, doi = {10.1371/journal.pone.0131250}, journal-iso = {PLOS ONE}, journal = {PLOS ONE}, volume = {10}, unique-id = {2941631}, issn = {1932-6203}, abstract = {Lipid droplets (LDs) are common organelles of the majority of eukaryotic cell types. Their biological significance has been extensively studied in mammalian liver cells and white adipose tissue. Although the central nervous system contains the highest relative amount and the largest number of different lipid species, neither the spatial nor the temporal distribution of LDs has been described. In this study, we used the brain of the fruitfly, Drosophila melanogaster, to investigate the neuroanatomy of LDs. We demonstrated that LDs are exclusively localised in glial cells but not in neurons in the larval nervous system. We showed that the brain's LD pool, rather than being constant, changes dynamically during development and reaches its highest value at the beginning of metamorphosis. LDs are particularly enriched in cortex glial cells located close to the brain surface. These specialized superficial cortex glial cells contain the highest amount of LDs among glial cell types and encapsulate neuroblasts and their daughter cells. Superficial cortex glial cells, combined with subperineurial glial cells, express the Drosophila fatty acid binding protein (Dfabp), as we have demonstrated through light-and electron microscopic immunocytochemistry. To the best of our best knowledge this is the first study that describes LD neuroanatomy in the Drosophila larval brain.}, year = {2015}, eissn = {1932-6203}, orcid-numbers = {Lippai, Mónika/0000-0002-7307-4233} } @article{MTMT:2708962, title = {The Role of the Selective Adaptor p62 and Ubiquitin-Like Proteins in Autophagy.}, url = {https://m2.mtmt.hu/api/publication/2708962}, author = {Lippai, Mónika and Lőw, Péter}, doi = {10.1155/2014/832704}, journal-iso = {BIOMED RES INT}, journal = {BIOMED RESEARCH INTERNATIONAL}, volume = {2014}, unique-id = {2708962}, issn = {2314-6133}, abstract = {The ubiquitin-proteasome system and autophagy were long viewed as independent, parallel degradation systems with no point of intersection. By now we know that these degradation pathways share certain substrates and regulatory molecules and show coordinated and compensatory function. Two ubiquitin-like protein conjugation pathways were discovered that are required for autophagosome biogenesis: the Atg12-Atg5-Atg16 and Atg8 systems. Autophagy has been considered to be essentially a nonselective process, but it turned out to be at least partially selective. Selective substrates of autophagy include damaged mitochondria, intracellular pathogens, and even a subset of cytosolic proteins with the help of ubiquitin-binding autophagic adaptors, such as p62/SQSTM1, NBR1, NDP52, and Optineurin. These proteins selectively recognize autophagic cargo and mediate its engulfment into autophagosomes by binding to the small ubiquitin-like modifiers that belong to the Atg8/LC3 family.}, year = {2014}, eissn = {2314-6141}, orcid-numbers = {Lippai, Mónika/0000-0002-7307-4233; Lőw, Péter/0000-0003-2450-7087} } @article{MTMT:2483302, title = {Rab11 facilitates crosstalk between autophagy and endosomal pathway through regulation of Hook localization.}, url = {https://m2.mtmt.hu/api/publication/2483302}, author = {Szatmári, Zsuzsanna and Kis, Viktor and Lippai, Mónika and Hegedűs, Krisztina and Faragó, Tamás and Lőrincz, Péter and Tanaka, T and Juhász, Gábor and Sass, Miklós}, doi = {10.1091/mbc.E13-10-0574}, journal-iso = {MOL BIOL CELL}, journal = {MOLECULAR BIOLOGY OF THE CELL}, volume = {25}, unique-id = {2483302}, issn = {1059-1524}, abstract = {During autophagy, double-membrane autophagosomes deliver sequestered cytoplasmic content to late endosomes and lysosomes for degradation. The molecular mechanism of autophagosome maturation is still poorly characterized. The small GTPase Rab11 regulates endosomal traffic, and is thought to function at the level of recycling endosomes. Here we show that loss of Rab11 leads to accumulation of autophagosomes and late endosomes in Drosophila melanogaster. Rab11 translocates from recycling endosomes to autophagosomes in response to autophagy induction, and physically interacts with Hook, a negative regulator of endosome maturation. Hook anchors endosomes to microtubules, and we show that Rab11 facilitates the fusion of endosomes and autophagosomes by removing Hook from mature late endosomes and inhibiting its homodimerization. Thus, induction of autophagy appears to promote autophagic flux by increased convergence with the endosomal pathway.}, year = {2014}, eissn = {1939-4586}, pages = {522-531}, orcid-numbers = {Lippai, Mónika/0000-0002-7307-4233; Faragó, Tamás/0000-0001-5987-2629; Lőrincz, Péter/0000-0001-7374-667X; Juhász, Gábor/0000-0001-8548-8874} } @book{MTMT:3061796, title = {Molekuláris sejtbiológia}, url = {https://m2.mtmt.hu/api/publication/3061796}, author = {Sass, Miklós and Lippai, Mónika and László, Lajos and Pálfa, Zsolt and Kovács, János and Laskay, Gábor and Szigeti, Csaba}, editor = {Sass, Miklós and Laskay, Gábor}, publisher = {ELTE TTK}, unique-id = {3061796}, year = {2013}, orcid-numbers = {Lippai, Mónika/0000-0002-7307-4233} }