TY - JOUR AU - Kovács, Zoltán AU - Bajusz, Csaba AU - Szabó, Anikó AU - Borkúti, Péter AU - Vedelek, Balázs AU - Benke, Reka AU - Lipinszki, Zoltán AU - Kristó, Ildikó AU - Vilmos, Péter TI - A bipartite NLS motif mediates the nuclear import of Drosophila moesin JF - FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY J2 - FRONT CELL DEV BIOL VL - 12 PY - 2024 PG - 14 SN - 2296-634X DO - 10.3389/fcell.2024.1206067 UR - https://m2.mtmt.hu/api/publication/34743202 ID - 34743202 N1 - Funding Agency and Grant Number: NKFIH (Hungarian National Research, Development and Innovation Office) through the National Laboratory for Biotechnology program [PD127968, LP2017-7/2017]; Hungarian Academy of Sciences Lendulet Grant; [2022-2.1.1-NL-2022-00008] Funding text: This work was supported by NKFIH (Hungarian National Research, Development and Innovation Office) through the National Laboratory for Biotechnology program, grant 2022-2.1.1-NL-2022-00008 (PV), and PD127968 (IK), and the Hungarian Academy of Sciences Lendulet Grant LP2017-7/2017 (ZL). AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Borkúti, Péter AU - Kristó, Ildikó AU - Szabó, Anikó AU - Kovács, Zoltán AU - Vilmos, Péter TI - FERM domain-containing proteins are active components of the cell nucleus JF - LIFE SCIENCE ALLIANCE J2 - LIFE SCI ALLIANCE VL - 7 PY - 2024 IS - 4 PG - 15 SN - 2575-1077 DO - 10.26508/lsa.202302489 UR - https://m2.mtmt.hu/api/publication/34575638 ID - 34575638 N1 - Funding Agency and Grant Number: NKFIH (Hungarian National Research, Development and Innovation Office) through the National Laboratory for Biotechnology program [2022-2.1.1-NL-2022-00008] Funding text: This work was supported by NKFIH (Hungarian National Research, Development and Innovation Office) through the National Laboratory for Biotechnology program, grant 2022-2.1.1-NL-2022-00008 (to P Vilmos) . AB - 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. LA - English DB - MTMT ER - TY - CHAP AU - Szabó, Anikó AU - Borkúti, Péter AU - Kovács, Zoltán AU - Kristó, Ildikó AU - Abonyi, Csilla AU - Vilmos, Péter ED - Tootle, Tina L. ED - Giedt, Michelle S. TI - Measuring Transposable Element Activity in Adult Drosophila Ovaries T2 - Drosophila Oogenesis: Methods and Protocols PB - Springer US CY - New York, New York SN - 9781071629703 T3 - Methods in Molecular Biology, ISSN 1064-3745 ; 2626. PY - 2023 SP - 309 EP - 321 PG - 13 DO - 10.1007/978-1-0716-2970-3_16 UR - https://m2.mtmt.hu/api/publication/34600487 ID - 34600487 LA - English DB - MTMT ER - TY - CHAP AU - Kristó, Ildikó AU - Borkúti, Péter AU - Kovács, Zoltán AU - Szabó, Anikó AU - Szikora, Szilárd AU - Vilmos, Péter ED - Tootle, Tina L. ED - Giedt, Michelle S. TI - Detection of Actin in Nuclear Protein Fraction Isolated from Adult Drosophila Ovary T2 - Drosophila Oogenesis: Methods and Protocols PB - Springer US CY - New York, New York SN - 9781071629703 T3 - Methods in Molecular Biology, ISSN 1064-3745 ; 2626. PY - 2023 SP - 353 EP - 364 PG - 12 DO - 10.1007/978-1-0716-2970-3_19 UR - https://m2.mtmt.hu/api/publication/34600475 ID - 34600475 LA - English DB - MTMT ER - TY - JOUR AU - Ábrahám, Edit AU - Réthi-Nagy, Zsuzsánna AU - Vilmos, Péter AU - Sinka, Rita AU - Lipinszki, Zoltán TI - Plk4 Is a Novel Substrate of Protein Phosphatase 5 JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 24 PY - 2023 IS - 3 PG - 22 SN - 1661-6596 DO - 10.3390/ijms24032033 UR - https://m2.mtmt.hu/api/publication/33723350 ID - 33723350 N1 - Funding Agency and Grant Number: National Research, Development and Innovation Office [K132155]; National Laboratory for Biotechnology Program Grant [2022-2.1.1-NL-2022-00008]; Hungarian Academy of Sciences [BO/00329/15]; Lenduelet Program Grant [LP2017-7/2017] Funding text: This research was funded by the National Research, Development and Innovation Office to R.S. and Z.L. (K132155) and to P.V. and Z.L. (National Laboratory for Biotechnology Program Grant (2022-2.1.1-NL-2022-00008)), and the Hungarian Academy of Sciences (Bolyai Fellowship (BO/00329/15) and Lenduelet Program Grant (LP2017-7/2017)) to Z.L. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Borkúti, Péter AU - Kristó, Ildikó AU - Szabó, Anikó AU - Bajusz, Csaba AU - Kovács, Zoltán AU - Réthi-Nagy, Zsuzsánna AU - Lipinszki, Zoltán AU - Lukacsovich, Tamas AU - Bogdan, Sven AU - Vilmos, Péter TI - Parallel import mechanisms ensure the robust nuclear localization of actin in Drosophila JF - FRONTIERS IN MOLECULAR BIOSCIENCES J2 - FRONT MOL BIOSCI VL - 9 PY - 2022 PG - 16 SN - 2296-889X DO - 10.3389/fmolb.2022.963635 UR - https://m2.mtmt.hu/api/publication/33133586 ID - 33133586 N1 - Funding Agency and Grant Number: NKFIH (National Research, Development and Innovation Office); Dr. Rollin D. Hotchkiss Foundation [NKFIH-871-3/2020, PD127968]; Hungarian Academy of Sciences Lenduelet Grant; [LP2017-7/2017] Funding text: This work was supported by NKFIH (National Research, Development and Innovation Office) through the National Laboratory for Biotechnology program, grant NKFIH-871-3/2020 (PV), and PD127968 (IK), the Dr. Rollin D. Hotchkiss Foundation (PB), and the Hungarian Academy of Sciences Lenduelet Grant LP2017-7/2017 (ZL). AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Bajusz, Csaba AU - Kristó, Ildikó AU - Abonyi, Csilla AU - Venit, Tomáš AU - Vedelek, Viktor AU - Lukácsovich, Tamás AU - Farkas, Attila AU - Borkúti, Péter AU - Kovács, Zoltán AU - Bajusz, Izabella AU - Marton, Annamária AU - Vizler, Csaba AU - Lipinszki, Zoltán AU - Sinka, Rita AU - Percipalle, Piergiorgio AU - Vilmos, Péter TI - The nuclear activity of the actin‐binding Moesin protein is necessary for gene expression in Drosophila JF - FEBS JOURNAL J2 - FEBS J VL - 288 PY - 2021 IS - 16 SP - 4812 EP - 4832 PG - 21 SN - 1742-464X DO - 10.1111/febs.15779 UR - https://m2.mtmt.hu/api/publication/31909117 ID - 31909117 N1 - Eötvös Loránd Research Network (ELKH), Biological Research Centre, Szeged, Hungary Doctoral School of Biology, University of Szeged, Hungary Department of Genetics, University of Szeged, Hungary Doctoral School of Multidisciplinary Medical Science, University of Szeged, Hungary Lendület Laboratory of Cell Cycle Regulation, ELKH, Biological Research Centre, Szeged, Hungary LA - English DB - MTMT ER - TY - JOUR AU - Kármán, Zoltán AU - Réthi-Nagy, Zsuzsánna AU - Ábrahám, Edit AU - Ördögh, Lilla AU - Csonka, Ákos AU - Vilmos, Péter AU - Debski, Janusz AU - Dadlez, Michal AU - Glover, David M. AU - Lipinszki, Zoltán TI - Novel perspectives of target-binding by the evolutionarily conserved PP4 phosphatase JF - OPEN BIOLOGY J2 - OPEN BIOL VL - 10 PY - 2020 IS - 12 PG - 12 SN - 2046-2441 DO - 10.1098/rsob.200343 UR - https://m2.mtmt.hu/api/publication/31788305 ID - 31788305 N1 - Biological Research Centre, Institute of Biochemistry, Mta Lendület Laboratory of Cell Cycle Regulation, Szeged, H-6726, Hungary Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, H-6726, Hungary Department of Traumatology, University of Szeged, Szeged, H-6726, Hungary Biological Research Centre, Institute of Genetics, Szeged, H-6726, Hungary Laboratory of Mass Spectrometry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, 02-106, Poland Department of Genetics, University of Cambridge, Cambridge, CB2 3EH, United Kingdom California Institute of Technology, Pasadena, CA 91125, United States Cited By :1 Export Date: 31 May 2022 Correspondence Address: Lipinszki, Z.; Biological Research Centre, Hungary; email: lipinszki.zoltan@brc.hu AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Kiss, Viktória AU - Jipa, András AU - Varga, Kata AU - Takáts, Szabolcs AU - Maruzs, Tamás AU - Lőrincz, Péter AU - Simon-Vecsei, Zsófia Judit AU - Szikora, Szilárd AU - Földi, István AU - Bajusz, Csaba AU - Tóth, Dávid AU - Vilmos, Péter AU - Gáspár, Imre AU - Ronchi, Paolo AU - Mihály, József AU - Juhász, Gábor TI - Drosophila Atg9 regulates the actin cytoskeleton via interactions with profilin and Ena JF - CELL DEATH AND DIFFERENTIATION J2 - CELL DEATH DIFFER VL - 27 PY - 2020 IS - 5 SP - 1677 EP - 1692 PG - 16 SN - 1350-9047 DO - 10.1038/s41418-019-0452-0 UR - https://m2.mtmt.hu/api/publication/30969186 ID - 30969186 N1 - Institute of Genetics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary Doctoral School of Biology, University of Szeged, Szeged, Hungary Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary Premium Postdoctoral Program, Hungarian Academy of Sciences, Szeged, Hungary Developmental Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany Electron Microscopy Core Facility, European Molecular Biology Laboratory, Heidelberg, Germany Export Date: 21 January 2020 CODEN: CDDIE Correspondence Address: Juhász, G.; Institute of Genetics, Biological Research Centre, Hungarian Academy of SciencesHungary; email: szmrt@elte.hu Institute of Genetics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary Doctoral School of Biology, University of Szeged, Szeged, Hungary Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary Premium Postdoctoral Program, Hungarian Academy of Sciences, Szeged, Hungary Developmental Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany Electron Microscopy Core Facility, European Molecular Biology Laboratory, Heidelberg, Germany Export Date: 31 January 2020 CODEN: CDDIE Correspondence Address: Juhász, G.; Institute of Genetics, Biological Research Centre, Hungarian Academy of SciencesHungary; email: szmrt@elte.hu Institute of Genetics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary Doctoral School of Biology, University of Szeged, Szeged, Hungary Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary Premium Postdoctoral Program, Hungarian Academy of Sciences, Szeged, Hungary Developmental Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany Electron Microscopy Core Facility, European Molecular Biology Laboratory, Heidelberg, Germany Cited By :4 Export Date: 21 January 2021 CODEN: CDDIE Correspondence Address: Juhász, G.; Institute of Genetics, Hungary; email: szmrt@elte.hu AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Cinege, Gyöngyi Ilona AU - Lerner, Zita AU - Magyar, Lilla Brigitta AU - Soós, Bálint AU - Tóth, Renáta AU - Kristó, Ildikó AU - Vilmos, Péter AU - Juhász, Gábor AU - Kovács, Attila Lajos AU - Hegedűs, Zoltán AU - Sensen, Christoph W. AU - Kurucz, Judit Éva AU - Andó, István TI - Cellular Immune Response Involving Multinucleated Giant Hemocytes with Two-Step Genome Amplification in the Drosophilid Zaprionus indianus JF - JOURNAL OF INNATE IMMUNITY J2 - J INNATE IMMUN VL - 12 PY - 2020 IS - 3 SP - 257 EP - 272 PG - 16 SN - 1662-811X DO - 10.1159/000502646 UR - https://m2.mtmt.hu/api/publication/30819399 ID - 30819399 N1 - * Megosztott szerzőség LA - English DB - MTMT ER -