@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}
}

@{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},
	booktitle = {Drosophila Oogenesis: Methods and Protocols},
	doi = {10.1007/978-1-0716-2970-3_16},
	unique-id = {34600487},
	year = {2023},
	pages = {309-321}
}

@{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},
	booktitle = {Drosophila Oogenesis: Methods and Protocols},
	doi = {10.1007/978-1-0716-2970-3_19},
	unique-id = {34600475},
	year = {2023},
	pages = {353-364}
}

@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: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:31788305,
	title = {Novel perspectives of target-binding by the evolutionarily conserved PP4 phosphatase},
	url = {https://m2.mtmt.hu/api/publication/31788305},
	author = {Kármán, Zoltán and Réthi-Nagy, Zsuzsánna and Ábrahám, Edit and Ördögh, Lilla and Csonka, Ákos and Vilmos, Péter and Debski, Janusz and Dadlez, Michal and Glover, David M. and Lipinszki, Zoltán},
	doi = {10.1098/rsob.200343},
	journal-iso = {OPEN BIOL},
	journal = {OPEN BIOLOGY},
	volume = {10},
	unique-id = {31788305},
	abstract = {Protein phosphatase 4 (PP4) is an evolutionarily conserved and essential Ser/Thr phosphatase that regulates cell division, development and DNA repair in eukaryotes. The major form of PP4, present from yeast to human, is the PP4c-R2-R3 heterotrimeric complex. The R3 subunit is responsible for substrate-recognition via its EVH1 domain. In typical EVH1 domains, conserved phenylalanine, tyrosine and tryptophan residues form the specific recognition site for their target's proline-rich sequences. Here, we identify novel binding partners of the EVH1 domain of the Drosophila R3 subunit, Falafel, and demonstrate that instead of binding to proline-rich sequences this EVH1 variant specifically recognizes atypical ligands, namely the FxxP and MxPP short linear consensus motifs. This interaction is dependent on an exclusively conserved leucine that replaces the phenylalanine invariant of all canonical EVH1 domains. We propose that the EVH1 domain of PP4 represents a new class of the EVH1 family that can accommodate low proline content sequences, such as the FxxP motif. Finally, our data implicate the conserved Smk-1 domain of Falafel in target-binding. These findings greatly enhance our understanding of the substrate-recognition mechanisms and function of PP4. © 2020 The Authors.},
	year = {2020},
	eissn = {2046-2441},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832}
}

@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}
}

@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}
}