@article{MTMT:34804520,
	title = {Cellular Immunity of Drosophila willistoni Reveals Novel Complexity in Insect Anti-Parasitoid Defense},
	url = {https://m2.mtmt.hu/api/publication/34804520},
	author = {Cinege, Gyöngyi Ilona and Fodor, K. and Magyar, Lilla Brigitta and Lipinszki, Zoltán and Hultmark, D. and Andó, István},
	doi = {10.3390/cells13070593},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {13},
	unique-id = {34804520},
	year = {2024},
	eissn = {2073-4409},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832; Andó, István/0000-0002-4648-9396}
}

@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}
}

@{MTMT:34723493,
	title = {Mikovírusok azonosítása Rhizopus fajokban},
	url = {https://m2.mtmt.hu/api/publication/34723493},
	author = {Sávai, Gergő and Kartali, Tünde and Benci, Dániel Attila and Patai, Roland and Lipinszki, Zoltán and Vágvölgyi, Csaba and Papp, Tamás},
	booktitle = {Biotechnológiai Szakmai Nap Absztraktfüzet},
	unique-id = {34723493},
	year = {2024},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832; Vágvölgyi, Csaba/0000-0003-0009-7773; Papp, Tamás/0000-0001-8211-5431}
}

@article{MTMT:34575640,
	title = {Expression and purification of the receptor-binding domain of SARS-CoV-2 spike protein in mammalian cells for immunological assays},
	url = {https://m2.mtmt.hu/api/publication/34575640},
	author = {Ábrahám, Edit and Bajusz, Csaba and Marton, Annamária and Borics, Attila and Mdluli, Thandiswa and Pardi, Norbert and Lipinszki, Zoltán},
	doi = {10.1002/2211-5463.13754},
	journal-iso = {FEBS OPEN BIO},
	journal = {FEBS OPEN BIO},
	volume = {14},
	unique-id = {34575640},
	issn = {2211-5463},
	abstract = {The receptor-binding domain (RBD) of the spike glycoprotein of SARS-CoV-2 virus mediates the interaction with the host cell and is required for virus internalization. It is, therefore, the primary target of neutralizing antibodies. The receptor-binding domain soon became the major target for COVID-19 research and the development of diagnostic tools and new-generation vaccines. Here, we provide a detailed protocol for high-yield expression and one-step affinity purification of recombinant RBD from transiently transfected Expi293F cells. Expi293F mammalian cells can be grown to extremely high densities in a specially formulated serum-free medium in suspension cultures, which makes them an excellent tool for secreted protein production. The highly purified RBD is glycosylated, structurally intact, and forms homomeric complexes. With this quick and easy method, we are able to produce large quantities of RBD (80 mg center dot L-1 culture) that we have successfully used in immunological assays to examine antibody titers and seroconversion after mRNA-based vaccination of mice.},
	keywords = {ELISA; protein purification; recombinant rbd; Expi293F mammalian cells; mRNA-LNP vaccination},
	year = {2024},
	eissn = {2211-5463},
	pages = {380-389},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832}
}

@article{MTMT:34129677,
	title = {Protein Phosphatase 4 Is Required for Centrobin Function in DNA Damage Repair},
	url = {https://m2.mtmt.hu/api/publication/34129677},
	author = {Réthi-Nagy, Zsuzsánna and Ábrahám, Edit and Sinka, Rita and Juhász, Szilvia and Lipinszki, Zoltán},
	doi = {10.3390/cells12182219},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {12},
	unique-id = {34129677},
	abstract = {Genome stability in human cells relies on the efficient repair of double-stranded DNA breaks, which is mainly achieved by homologous recombination (HR). Among the regulators of various cellular functions, Protein phosphatase 4 (PP4) plays a pivotal role in coordinating cellular response to DNA damage. Meanwhile, Centrobin (CNTRB), initially recognized for its association with centrosomal function and microtubule dynamics, has sparked interest due to its potential contribution to DNA repair processes. In this study, we investigate the involvement of PP4 and its interaction with CNTRB in HR-mediated DNA repair in human cells. Employing a range of experimental strategies, we investigate the physical interaction between PP4 and CNTRB and shed light on the importance of two specific motifs in CNTRB, the PP4-binding FRVP and the ATR kinase recognition SQ sequences, in the DNA repair process. Moreover, we examine cells depleted of PP4 or CNTRB and cells harboring FRVP and SQ mutations in CNTRB, which result in similar abnormal chromosome morphologies. This phenomenon likely results from the impaired resolution of Holliday junctions, which serve as crucial intermediates in HR. Taken together, our results provide new insights into the intricate mechanisms of PP4 and CNTRB-regulated HR repair and their interrelation.},
	year = {2023},
	eissn = {2073-4409},
	orcid-numbers = {Sinka, Rita/0000-0003-4040-4184; Lipinszki, Zoltán/0000-0002-2067-0832}
}

@article{MTMT:33744872,
	title = {Evolution of insect innate immunity through domestication of bacterial toxins},
	url = {https://m2.mtmt.hu/api/publication/33744872},
	author = {Verster, Kirsten I. and Cinege, Gyöngyi Ilona and Lipinszki, Zoltán and Magyar, Lilla Brigitta and Kurucz, Judit Éva and Tarnopol, Rebecca L. and Ábrahám, Edit and Darula, Zsuzsanna and Karageorgi, Marianthi and Tamsil, Josephine A. and Akalu, Saron M. and Andó, István and Whiteman, Noah K.},
	doi = {10.1073/pnas.2218334120},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {120},
	unique-id = {33744872},
	issn = {0027-8424},
	abstract = {Toxin cargo genes are often horizontally transferred by phages between bacterial species and are known to play an important role in the evolution of bacterial pathogenesis. Here, we show how these same genes have been horizontally transferred from phage or bacteria to animals and have resulted in novel adaptations. We discovered that two widespread bacterial genes encoding toxins of animal cells, cytolethal distending toxin subunit B ( cdtB ) and apoptosis-inducing protein of 56 kDa ( aip56) , were captured by insect genomes through horizontal gene transfer from bacteria or phages. To study the function of these genes in insects, we focused on Drosophila ananassae as a model. In the D. ananassae subgroup species, cdtB and aip56 are present as singular ( cdtB ) or fused copies ( cdtB::aip56 ) on the second chromosome. We found that cdtB and aip56 genes and encoded proteins were expressed by immune cells, some proteins were localized to the wasp embryo’s serosa, and their expression increased following parasitoid wasp infection. Species of the ananassae subgroup are highly resistant to parasitoid wasps, and we observed that D. ananassae lines carrying null mutations in cdtB and aip56 toxin genes were more susceptible to parasitoids than the wild type. We conclude that toxin cargo genes were captured by these insects millions of years ago and integrated as novel modules into their innate immune system. These modules now represent components of a heretofore undescribed defense response and are important for resistance to parasitoid wasps. Phage or bacterially derived eukaryotic toxin genes serve as macromutations that can spur the instantaneous evolution of novelty in animals.},
	year = {2023},
	eissn = {1091-6490},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832; Tarnopol, Rebecca L./0000-0001-5675-8513; Karageorgi, Marianthi/0000-0003-2934-7019; Tamsil, Josephine A./0000-0002-3173-1848; Andó, István/0000-0002-4648-9396; Whiteman, Noah K./0000-0003-1448-4678}
}

@article{MTMT:33723350,
	title = {Plk4 Is a Novel Substrate of Protein Phosphatase 5},
	url = {https://m2.mtmt.hu/api/publication/33723350},
	author = {Ábrahám, Edit and Réthi-Nagy, Zsuzsánna and Vilmos, Péter and Sinka, Rita and Lipinszki, Zoltán},
	doi = {10.3390/ijms24032033},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33723350},
	issn = {1661-6596},
	abstract = {The conserved Ser/Thr protein phosphatase 5 (PP5) is involved in the regulation of key cellular processes, including DNA damage repair and cell division in eukaryotes. As a co-chaperone of Hsp90, PP5 has been shown to modulate the maturation and activity of numerous oncogenic kinases. Here, we identify a novel substrate of PP5, the Polo-like kinase 4 (Plk4), which is the master regulator of centriole duplication in animal cells. We show that PP5 specifically interacts with Plk4, and is able to dephosphorylate the kinase in vitro and in vivo, which affects the interaction of Plk4 with its partner proteins. In addition, we provide evidence that PP5 and Plk4 co-localize to the centrosomes in Drosophila embryos and cultured cells. We demonstrate that PP5 is not essential; the null mutant flies are viable without a severe mitotic phenotype; however, its loss significantly reduces the fertility of the animals. Our results suggest that PP5 is a novel regulator of the Plk4 kinase in Drosophila.},
	keywords = {PHOSPHORYLATION; COMPLEXES; DROSOPHILA; DROSOPHILA; tetratricopeptide repeat; centrosome; centrosome; Autoinhibition; CENTRIOLE BIOGENESIS; Biochemistry & Molecular Biology; PP5; PROTEIN PHOSPHATASE 5; Polo-like kinase 4; SERINE/THREONINE PHOSPHATASE},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Sinka, Rita/0000-0003-4040-4184; Lipinszki, Zoltán/0000-0002-2067-0832}
}

@article{MTMT:33194158,
	title = {Molecular Characterization of Novel Mycoviruses in Seven Umbelopsis Strains},
	url = {https://m2.mtmt.hu/api/publication/33194158},
	author = {Kartali, Tünde and Zsindely, Nóra and Nyilasi, Ildikó and Németh, Orsolya and Sávai, Gergő and Kocsubé, Sándor and Lipinszki, Zoltán and Patai, Roland and Spisák, Krisztina and Nagy, Gábor and Bodai, László and Vágvölgyi, Csaba and Papp, Tamás},
	doi = {10.3390/v14112343},
	journal-iso = {VIRUSES-BASEL},
	journal = {VIRUSES},
	volume = {14},
	unique-id = {33194158},
	abstract = {The presence of viruses is less explored in Mucoromycota as compared to other fungal groups such as Ascomycota and Basidiomycota. Recently, more and more mycoviruses are identified from the early-diverging lineages of fungi. We have determined the genome of 11 novel dsRNA viruses in seven different Umbelopsis strains with next-generation sequencing (NGS). The identified viruses were named Umbelopsis ramanniana virus 5 (UrV5), 6a (UrV6a); 6b (UrV6b); 7 (UrV7); 8a (UrV8a); 8b (UrV8b); Umbelopsis gibberispora virus 1 (UgV1); 2 (UgV2) and Umbelopsis dimorpha virus 1a (UdV1a), 1b (UdV1b) and 2 (UdV2). All the newly identified viruses contain two open reading frames (ORFs), which putatively encode the coat protein (CP) and the RNA-dependent RNA polymerase (RdRp), respectively. Based on the phylogeny inferred from the RdRp sequences, eight viruses (UrV7, UrV8a, UrV8b, UgV1, UgV2, UdV1a, UdV1b and UdV2) belong to the genus Totivirus, while UrV5, UrV6a and UrV6b are placed into a yet unclassified but well-defined Totiviridae-related group. In UrV5, UgV1, UgV2, UrV8b, UdV1a, UdV2 and UdV1b, ORF2 is predicted to be translated as a fusion protein via a rare +1 (or-2) ribosomal frameshift, which is not characteristic to most members of the Totivirus genus. Virus particles 31 to 32 nm in diameter could be detected in the examined fungal strains by transmission electron microscopy. Through the identification and characterization of new viruses of Mucoromycota fungi, we can gain insight into the diversity of mycoviruses, as well as into their phylogeny and genome organization.},
	year = {2022},
	eissn = {1999-4915},
	orcid-numbers = {Zsindely, Nóra/0000-0002-6189-3100; Kocsubé, Sándor/0000-0001-7839-0510; Lipinszki, Zoltán/0000-0002-2067-0832; Nagy, Gábor/0000-0001-5464-1135; Bodai, László/0000-0001-8411-626X; Vágvölgyi, Csaba/0000-0003-0009-7773; Papp, Tamás/0000-0001-8211-5431}
}

@article{MTMT:33133587,
	title = {RESEARCH PROTOCOL GST-IVTT pull-down: a fast and versatile in vitro method for validating and mapping protein-protein interactions},
	url = {https://m2.mtmt.hu/api/publication/33133587},
	author = {Réthi-Nagy, Zsuzsánna and Ábrahám, Edit and Lipinszki, Zoltán},
	doi = {10.1002/2211-5463.13485},
	journal-iso = {FEBS OPEN BIO},
	journal = {FEBS OPEN BIO},
	volume = {12},
	unique-id = {33133587},
	issn = {2211-5463},
	abstract = {Over the past few decades, dozens of in vitro methods have been developed to map, investigate and validate protein-protein interactions. However, most of these approaches are time-consuming and labour-intensive or require specialised equipment or substantial amounts of purified proteins. Here, we describe a fast and versatile research protocol that is suitable for the in vitro analysis of the physical interaction between proteins or for mapping the binding surfaces. The principle of this method is based on the immobilisation of the protein/domain of interest to a carrier followed by its incubation with a labelled putative binding partner, which is generated by a coupled in vitro transcription/translation reaction. Interacting proteins are removed from the carrier, fractionated and visualised by SDS/PAGE autoradiography (or western blotting). This simple and cheap method can be easily carried out in every wet lab.},
	keywords = {Mapping; Protein-protein interaction; GST pull-down; HYDROGEN-ION BUFFERS; IVTT},
	year = {2022},
	eissn = {2211-5463},
	pages = {1988-1995},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832}
}

@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}
}