@article{MTMT:35619928,
	title = {Dual role for Headcase in hemocyte progenitor fate determination in Drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/35619928},
	author = {Kharrat, Bayan and Gábor, Erika and Virag, Nikolett and Sinka, Rita and Jankovics, Ferenc and Kristó, Ildikó and Vilmos, Péter and Csordás, Gábor and Honti, Viktor},
	doi = {10.1371/journal.pgen.1011448},
	journal-iso = {PLOS GENET},
	journal = {PLOS GENETICS},
	volume = {20},
	unique-id = {35619928},
	issn = {1553-7390},
	abstract = {The hematopoietic organ of the Drosophila larva, the lymph gland, is a simplified representation of mammalian hematopoietic compartments, with the presence of hemocyte progenitors in the medullary zone (MZ), differentiated hemocytes in the cortical zone (CZ), and a hematopoietic niche called the posterior signaling centre (PSC) that orchestrates progenitor differentiation. Our previous work has demonstrated that the imaginal cell factor Headcase (Hdc, Heca) is required in the hematopoietic niche to control the differentiation of hemocyte progenitors. However, the downstream mechanisms of Hdc-mediated hematopoietic control remained unknown. Here we show that Hdc exerts this function by negatively regulating the insulin/mTOR signaling in the niche. When Hdc is depleted in the PSC, the overactivation of this pathway triggers reactive oxygen species (ROS) accumulation and, in turn, the differentiation of effector lamellocytes non-cell-autonomously. Although overactivation of insulin/mTOR signaling normally leads to an increase in the size of the hematopoietic niche, this effect is concealed by cell death caused by hdc loss-of-function. Moreover, we describe here that hdc silencing in progenitors causes cell-autonomous ROS elevation and JNK pathway activation, resulting in decreased MZ size and differentiation of lamellocytes. Similarly to the PSC niche, knocking down hdc in the MZ also leads to caspase activation. Notably, depleting Hdc in the progenitors triggers proliferation, an opposing effect to what is observed in the niche. These findings further our understanding of how progenitor maintenance in the larval lymph gland is controlled autonomously and non-cell-autonomously, and point towards new mechanisms potentially regulating HSC maintenance across vertebrates.},
	keywords = {PROTEIN; CELL; PROLIFERATION; INSULIN; MAINTENANCE; LINEAGES; COMPARTMENTS; Hematopoietic progenitors; Oxidative stress},
	year = {2024},
	eissn = {1553-7404},
	orcid-numbers = {Csordás, Gábor/0000-0001-6871-6839}
}

@article{MTMT:35464318,
	title = {Moesin contributes to heat shock gene response through direct binding to the Med15 subunit of the Mediator complex in the nucleus},
	url = {https://m2.mtmt.hu/api/publication/35464318},
	author = {Kristó, Ildikó and Kovács, Zoltán and Szabó, Anikó and Borkúti, Péter and Gráf, Alexandra and Sánta, Ádám and Pettkó-Szandtner, Aladár and Ábrahám, Edit and Honti, Viktor and Lipinszki, Zoltán and Vilmos, Péter},
	doi = {10.1098/rsob.240110},
	journal-iso = {OPEN BIOL},
	journal = {OPEN BIOLOGY},
	volume = {14},
	unique-id = {35464318},
	abstract = {The members of the evolutionary conserved actin-binding Ezrin, Radixin and Moesin (ERM) protein family are involved in numerous key cellular processes in the cytoplasm. In the last decades, ERM proteins, like actin and other cytoskeletal components, have also been shown to be functional components of the nucleus; however, the molecular mechanism behind their nuclear activities remained unclear. Therefore, our primary aim was to identify the nuclear protein interactome of the single Drosophila ERM protein, Moesin. We demonstrate that Moesin directly interacts with the Mediator complex through direct binding to its Med15 subunit, and the presence of Moesin at the regulatory regions of the Hsp70Ab heat shock gene was found to be Med15-dependent. Both Moesin and Med15 bind to heat shock factor (Hsf), and they are required for proper Hsp gene expression under physiological conditions. Moreover, we confirmed that Moesin, Med15 and Hsf are able to bind the monomeric form of actin and together they form a complex in the nucleus. These results elucidate a mechanism by which ERMs function within the nucleus. Finally, we present the direct interaction of the human orthologues of Drosophila Moesin and Med15, which highlights the evolutionary significance of our finding.},
	keywords = {ACTIVATION; TRANSCRIPTION FACTOR; NUCLEUS; RECRUITMENT; DROSOPHILA; MEDIATOR; ACTIN; ACTIN; Gene Expression; HYBRIDIZATION; PRENATAL-DIAGNOSIS; ERM PROTEINS; moesin; 22q11.2 Deletion syndrome},
	year = {2024},
	eissn = {2046-2441},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832}
}

@article{MTMT:34743202,
	title = {A bipartite NLS motif mediates the nuclear import of Drosophila moesin},
	url = {https://m2.mtmt.hu/api/publication/34743202},
	author = {Kovács, Zoltán and Bajusz, Csaba and Szabó, Anikó and Borkúti, Péter and Vedelek, Balázs and Benke, Reka and Lipinszki, Zoltán and Kristó, Ildikó and Vilmos, Péter},
	doi = {10.3389/fcell.2024.1206067},
	journal-iso = {FRONT CELL DEV BIOL},
	journal = {FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY},
	volume = {12},
	unique-id = {34743202},
	issn = {2296-634X},
	abstract = {The ERM protein family, which consists of three closely related proteins in vertebrates, ezrin, radixin, and moesin (ERM), is an ancient and important group of cytoplasmic actin-binding and organizing proteins. With their FERM domain, ERMs bind various transmembrane proteins and anchor them to the actin cortex through their C-terminal F-actin binding domain, thus they are major regulators of actin dynamics in the cell. ERMs participate in many fundamental cellular processes, such as phagocytosis, microvilli formation, T-cell activation and tumor metastasis. We have previously shown that, besides its cytoplasmic activities, the single ERM protein of Drosophila melanogaster, moesin, is also present in the cell nucleus, where it participates in gene expression and mRNA export. Here we study the mechanism by which moesin enters the nucleus. We show that the nuclear import of moesin is an NLS-mediated, active process. The nuclear localization sequence of the moesin protein is an evolutionarily highly conserved, conventional bipartite motif located on the surface of the FERM domain. Our experiments also reveal that the nuclear import of moesin does not require PIP2 binding or protein activation, and occurs in monomeric form. We propose, that the balance between the phosphorylated and non-phosphorylated protein pools determines the degree of nuclear import of moesin.},
	keywords = {PHOSPHORYLATION; BINDING; LOCALIZATION; IDENTIFICATION; NUCLEUS; STRUCTURAL BASIS; DROSOPHILA; CELL BIOLOGY; ERM PROTEINS; ezrin; moesin; CYTOPLASMIC TAIL; ERM; PIP2; importin; MERLIN; LINKS ACTIN},
	year = {2024},
	eissn = {2296-634X},
	orcid-numbers = {Vedelek, Balázs/0000-0001-6981-0026; Lipinszki, Zoltán/0000-0002-2067-0832}
}

@article{MTMT:34575638,
	title = {FERM domain-containing proteins are active components of the cell nucleus},
	url = {https://m2.mtmt.hu/api/publication/34575638},
	author = {Borkúti, Péter and Kristó, Ildikó and Szabó, Anikó and Kovács, Zoltán and Vilmos, Péter},
	doi = {10.26508/lsa.202302489},
	journal-iso = {LIFE SCI ALLIANCE},
	journal = {LIFE SCIENCE ALLIANCE},
	volume = {7},
	unique-id = {34575638},
	abstract = {The FERM domain is a conserved and widespread protein module that appeared in the common ancestor of amoebae, fungi, and animals, and is therefore now found in a wide variety of species. The primary function of the FERM domain is localizing to the plasma membrane through binding lipids and proteins of the membrane; thus, for a long time, FERM domain-containing proteins (FDCPs) were considered exclusively cytoskeletal. Although their role in the cytoplasm has been extensively studied, the recent discovery of the presence and importance of cytoskeletal proteins in the nucleus suggests that FDCPs might also play an important role in nuclear function. In this review, we collected data on their nuclear localization, transport, and possible functions, which are still scattered throughout the literature, with special regard to the role of the FERM domain in these processes. With this, we would like to draw attention to the exciting, new dimension of the role of FDCPs, their nuclear activity, which could be an interesting novel direction for future research.},
	keywords = {GENE-EXPRESSION; STRUCTURAL BASIS; FOCAL ADHESION; TERMINAL DOMAIN; SUBCELLULAR-LOCALIZATION; Export signal; Ankyrin Repeat; FAK INTERACTION; KINDLIN FAMILY},
	year = {2024},
	eissn = {2575-1077}
}

@article{MTMT:34575637,
	title = {Direct interaction of Su(var)2-10 via the SIM-binding site of the Piwi protein is required for transposon silencing in Drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/34575637},
	author = {Bence, Melinda and Jankovics, Ferenc and Kristó, Ildikó and Gyetvai, Akos and Vértessy, Beáta (Grolmuszné) and Erdélyi, Miklós},
	doi = {10.1111/febs.17073},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	volume = {291},
	unique-id = {34575637},
	issn = {1742-464X},
	abstract = {Nuclear Piwi/Piwi-interacting RNA complexes mediate co-transcriptional silencing of transposable elements by inducing local heterochromatin formation. In Drosophila, sumoylation plays an essential role in the assembly of the silencing complex; however, the molecular mechanism by which the sumoylation machinery is recruited to the transposon loci is poorly understood. Here, we show that the Drosophila E3 SUMO-ligase Su(var)2-10 directly binds to the Piwi protein. This interaction is mediated by the SUMO-interacting motif-like (SIM-like) structure in the C-terminal domain of Su(var)2-10. We demonstrated that the SIM-like structure binds to a special region found in the MID domain of the Piwi protein, the structure of which is highly similar to the SIM-binding pocket of SUMO proteins. Abrogation of the Su(var)2-10-binding surface of the Piwi protein resulted in transposon derepression in the ovary of adult flies. Based on our results, we propose a model in which the Piwi protein initiates local sumoylation in the silencing complex by recruiting Su(var)2-10 to the transposon loci.},
	keywords = {SUBSTRATE; Drosophila melanogaster; Defense; MOTIF; Sumoylation; Sumoylation; SUMO; piRNA pathway; Su(var)2-10; PIWI/piRNA; ENFORCES},
	year = {2024},
	eissn = {1742-4658},
	pages = {1759-1779}
}

@article{MTMT:34600487,
	title = {Measuring Transposable Element Activity in Adult Drosophila Ovaries},
	url = {https://m2.mtmt.hu/api/publication/34600487},
	author = {Szabó, Anikó and Borkúti, Péter and Kovács, Zoltán and Kristó, Ildikó and Abonyi, Csilla and Vilmos, Péter},
	doi = {10.1007/978-1-0716-2970-3_16},
	journal-iso = {METHODS MOL BIOL},
	journal = {METHODS IN MOLECULAR BIOLOGY},
	volume = {2626},
	unique-id = {34600487},
	issn = {1064-3745},
	year = {2023},
	eissn = {1940-6029},
	pages = {309-321}
}

@article{MTMT:34600475,
	title = {Detection of Actin in Nuclear Protein Fraction Isolated from Adult Drosophila Ovary},
	url = {https://m2.mtmt.hu/api/publication/34600475},
	author = {Kristó, Ildikó and Borkúti, Péter and Kovács, Zoltán and Szabó, Anikó and Szikora, Szilárd and Vilmos, Péter},
	doi = {10.1007/978-1-0716-2970-3_19},
	journal-iso = {METHODS MOL BIOL},
	journal = {METHODS IN MOLECULAR BIOLOGY},
	volume = {2626},
	unique-id = {34600475},
	issn = {1064-3745},
	year = {2023},
	eissn = {1940-6029},
	pages = {353-364}
}

@article{MTMT:33133586,
	title = {Parallel import mechanisms ensure the robust nuclear localization of actin in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/33133586},
	author = {Borkúti, Péter and Kristó, Ildikó and Szabó, Anikó and Bajusz, Csaba and Kovács, Zoltán and Réthi-Nagy, Zsuzsánna and Lipinszki, Zoltán and Lukacsovich, Tamas and Bogdan, Sven and Vilmos, Péter},
	doi = {10.3389/fmolb.2022.963635},
	journal-iso = {FRONT MOL BIOSCI},
	journal = {FRONTIERS IN MOLECULAR BIOSCIENCES},
	volume = {9},
	unique-id = {33133586},
	abstract = {Actin, as an ancient and fundamental protein, participates in various cytoplasmic as well as nuclear functions in eukaryotic cells. Based on its manifold tasks in the nucleus, it is a reasonable assumption that the nuclear presence of actin is essential for the cell, and consequently, its nuclear localization is ensured by a robust system. However, today only a single nuclear import and a single nuclear export pathway is known which maintain the dynamic balance between cytoplasmic and nuclear actin pools. In our work, we tested the robustness of the nuclear import of actin, and investigated whether the perturbations of nuclear localization affect the viability of the whole organism. For this aim, we generated a genetic system in Drosophila, in which we rescued the lethal phenotype of the null mutation of the Actin5C gene with transgenes that express different derivatives of actin, including a Nuclear Export Signal (NES)-tagged isoform which ensures forced nuclear export of the protein. We also disrupted the SUMOylation site of actin, suggested earlier to be responsible for nuclear retention, and eliminated the activity of the single nuclear import factor dedicated to actin. We found that, individually, none of the above mentioned manipulations led to a notable reduction in nuclear actin levels and thus, fully rescued lethality. However, the NES tagging of actin, together with the knock out of its importin, significantly reduced the amount of nuclear actin and induced lethality, confirming that the presence of actin in the nucleus is essential, and thereby, over-secured. Supporting this, we identified novel nuclear importins specific to actin, which sheds light on the mechanism behind the robustness of nuclear localization of actin, and supports the idea of essentiality of its nuclear functions.},
	keywords = {GENE; PROTEIN; TRANSCRIPTION; NUCLEUS; ENCODES; HOMOLOG; COLLECTION; ACTIN; FRAGMENTS; EXPORT; Sumoylation; NUCLEAR TRANSPORT; importin},
	year = {2022},
	eissn = {2296-889X},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832}
}

@article{MTMT:31909117,
	title = {The nuclear activity of the actin‐binding Moesin protein is necessary for gene expression in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/31909117},
	author = {Bajusz, Csaba and Kristó, Ildikó and Abonyi, Csilla and Venit, Tomáš and Vedelek, Viktor and Lukácsovich, Tamás and Farkas, Attila and Borkúti, Péter and Kovács, Zoltán and Bajusz, Izabella and Marton, Annamária and Vizler, Csaba and Lipinszki, Zoltán and Sinka, Rita and Percipalle, Piergiorgio and Vilmos, Péter},
	doi = {10.1111/febs.15779},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	volume = {288},
	unique-id = {31909117},
	issn = {1742-464X},
	year = {2021},
	eissn = {1742-4658},
	pages = {4812-4832},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832; Sinka, Rita/0000-0003-4040-4184; Vilmos, Péter/0000-0001-5692-8818}
}

@article{MTMT:30819399,
	title = {Cellular Immune Response Involving Multinucleated Giant Hemocytes with Two-Step Genome Amplification in the Drosophilid Zaprionus indianus},
	url = {https://m2.mtmt.hu/api/publication/30819399},
	author = {Cinege, Gyöngyi Ilona and Lerner, Zita and Magyar, Lilla Brigitta and Soós, Bálint and Tóth, Renáta and Kristó, Ildikó and Vilmos, Péter and Juhász, Gábor and Kovács, Attila Lajos and Hegedűs, Zoltán and Sensen, Christoph W. and Kurucz, Judit Éva and Andó, István},
	doi = {10.1159/000502646},
	journal-iso = {J INNATE IMMUN},
	journal = {JOURNAL OF INNATE IMMUNITY},
	volume = {12},
	unique-id = {30819399},
	issn = {1662-811X},
	year = {2020},
	eissn = {1662-8128},
	pages = {257-272},
	orcid-numbers = {Juhász, Gábor/0000-0001-8548-8874; Andó, István/0000-0002-4648-9396}
}