TY - JOUR AU - Vedelek, Viktor AU - Jankovics, Ferenc AU - Zádori, János AU - Sinka, Rita TI - Mitochondrial Differentiation during Spermatogenesis: Lessons from Drosophila melanogaster JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 25 PY - 2024 IS - 7 PG - 25 SN - 1661-6596 DO - 10.3390/ijms25073980 UR - https://m2.mtmt.hu/api/publication/34772438 ID - 34772438 N1 - Funding Agency and Grant Number: National Research, Development and Innovation Office Funding text: No Statement Available AB - Numerous diseases can arise as a consequence of mitochondrial malfunction. Hence, there is a significant focus on studying the role of mitochondria in cancer, ageing, neurodegenerative diseases, and the field of developmental biology. Mitochondria could exist as discrete organelles in the cell; however, they have the ability to fuse, resulting in the formation of interconnected reticular structures. The dynamic changes between these forms correlate with mitochondrial function and mitochondrial health, and consequently, there is a significant scientific interest in uncovering the specific molecular constituents that govern these transitions. Moreover, the specialized mitochondria display a wide array of variable morphologies in their cristae formations. These inner mitochondrial structures are closely associated with the specific functions performed by the mitochondria. In multiple cases, the presence of mitochondrial dysfunction has been linked to male sterility, as it has been observed to cause a range of abnormal spermatogenesis and sperm phenotypes in different species. This review aims to elucidate the dynamic alterations and functions of mitochondria in germ cell development during the spermatogenesis of Drosophila melanogaster. LA - English DB - MTMT ER - TY - JOUR AU - Bence, Melinda AU - Jankovics, Ferenc AU - Kristó, Ildikó AU - Gyetvai, Akos AU - Vértessy, Beáta (Grolmuszné) AU - Erdélyi, Miklós TI - Direct interaction of Su(var)2-10 via the SIM-binding site of the Piwi protein is required for transposon silencing in Drosophila melanogaster JF - FEBS JOURNAL J2 - FEBS J PY - 2024 PG - 21 SN - 1742-464X DO - 10.1111/febs.17073 UR - https://m2.mtmt.hu/api/publication/34575637 ID - 34575637 N1 - Funding Agency and Grant Number: National Research, Development and Innovation Office [K132384, PD124446]; Janos Bolyai Fellowship of Hungarian Academy of Sciences [BO/00599/17]; UNKP New National Excellence Program of the Ministry of Human Capacities of Hungary [UNKP-19-4-SZTE-5]; National Research, Development and Innovation Office (National Laboratory for Biotechnology) [2022-2.1.1-NL-2022-00008]; National Research, Development and Innovation Office [K135231, K146890, FK137867, VEKOP-2.3.2-16-2017-00013, NKP-2018-1.2.1-NKP-2018-00005]; Ministry for Innovation and Technology of Hungary from the National Research, Development and Innovation Fund; [TKP2021-EGA-02] AB - 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. LA - English DB - MTMT ER - TY - CONF AU - Kúthy-Sutus, Enikő AU - Gábor, Erika AU - Kharrat, Bayan AU - Jankovics, Ferenc AU - Sinka, Rita AU - Honti, Viktor TI - Studying Drosophila blood cell plasticity using primary blood cell cultures T2 - Straub-Napok 2022 PY - 2022 SP - 1 UR - https://m2.mtmt.hu/api/publication/34689202 ID - 34689202 LA - English DB - MTMT ER - TY - JOUR AU - Takács, Tamás AU - Németh, Tibor Mihály AU - Bohner, Flóra AU - Vágvölgyi, Csaba AU - Jankovics, Ferenc AU - Wilson, Duncan AU - Gácser, Attila TI - Characterization and functional analysis of zinc trafficking in the human fungal pathogen Candida parapsilosis JF - OPEN BIOLOGY J2 - OPEN BIOL VL - 12 PY - 2022 IS - 7 PG - 16 SN - 2046-2441 DO - 10.1098/rsob.220077 UR - https://m2.mtmt.hu/api/publication/33025619 ID - 33025619 N1 - Funding Agency and Grant Number: Wellcome Trust Senior Research Fellowship [214317/Z/18/Z]; MRC [MR/N006364/2]; University of Exeter Funding text: D.W. is supported by a Wellcome Trust Senior Research Fellowship (grant no. 214317/Z/18/Z) and the MRC and University of Exeter (grant no. MR/N006364/2). AB - The zinc restriction and zinc toxicity are part of host defence, called nutritional immunity. The crucial role of zinc homeostasis in microbial survival within a host is established, but little is known about these processes in the opportunistic human fungal pathogen Candida parapsilosis. Our in silico predictions suggested the presence of at least six potential zinc transporters (ZnTs) in C. parapsilosis-orthologues of ZRC1, ZRT3 and ZRT101-but an orthologue of PRA1 zincophore was not found. In addition, we detected a species-specific gene expansion of the novel ZnT ZRT2, as we identified three orthologue genes in the genome of C. parapsilosis. Based on predictions, we created homozygous mutant strains of the potential ZnTs and characterized them. Despite the apparent gene expansion of ZRT2 in C. parapsilosis, only CpZRT21 was essential for growth in a zinc-depleted acidic environment, in addition we found that CpZrc1 is essential for zinc detoxification and also protects the fungi against the elimination of murine macrophages. Significantly, we demonstrated that C. parapsilosis forms zincosomes in a Zrc1-independent manner and zinc detoxification is mediated by the vacuolar importer CpZrc1. Our study defines the functions of C. parapsilosis ZnTs, including a species-specific survival and zinc detoxification system. LA - English DB - MTMT ER - TY - JOUR AU - Szarka-Kovács, Alexandra Brigitta AU - Takács, Zsanett AU - Bence, Melinda AU - Erdélyi, Miklós AU - Jankovics, Ferenc TI - Drosophila MESR4 Gene Ensures Germline Stem Cell Differentiation by Promoting the Transcription of bag of marbles JF - CELLS J2 - CELLS-BASEL VL - 11 PY - 2022 IS - 13 PG - 13 SN - 2073-4409 DO - 10.3390/cells11132056 UR - https://m2.mtmt.hu/api/publication/32990099 ID - 32990099 N1 - Funding Agency and Grant Number: Hungarian Scientific Research Fund (OTKA) [K132384, PD124446]; National Research, Development, and Innovation Office [NKFIH-469-3/2020]; Rollin D. Hotchkiss Foundation; Janos Bolyai Fellowship Funding text: This research was funded by the Hungarian Scientific Research Fund (OTKA) (K132384 to M.E. and PD124446 to M.B.), and the National Research, Development, and Innovation Office (NKFIH-469-3/2020 to M.E.). A.B.S.-K. was supported by the Rollin D. Hotchkiss Foundation. M.B. was supported by a Janos Bolyai Fellowship. AB - Ovarian germline stem cells (GSCs) of Drosophila melanogaster provide a valuable in vivo model to investigate how the adult stem cell identity is maintained and the differentiation of the daughter cells is regulated. GSCs are embedded into a specialized cellular microenvironment, the so-called stem cell niche. Besides the complex signaling interactions between the germ cells and the niche cells, the germ cell intrinsic mechanisms, such as chromatin regulation and transcriptional control, are also crucial in the decision about self-renewal and differentiation. The key differentiation regulator gene is the bag of marbles (bam), which is transcriptionally repressed in the GSCs and de-repressed in the differentiating daughter cell. Here, we show that the transcription factor MESR4 functions in the germline to promote GSC daughter differentiation. We find that the loss of MESR4 results in the accumulation of GSC daughter cells which fail to transit from the pre-cystoblast (pre-CB) to the differentiated cystoblast (CB) stage. The forced expression of bam can rescue this differentiation defect. By a series of epistasis experiments and a transcriptional analysis, we demonstrate that MESR4 positively regulates the transcription of bam. Our results suggest that lack of repression alone is not sufficient, but MESR4-mediated transcriptional activation is also required for bam expression. LA - English DB - MTMT ER - TY - JOUR AU - Ninova, Maria AU - Godneeva, Baira AU - Chen, Yung-Chia Ariel AU - Luo, Yicheng AU - Prakash, Sharan J AU - Jankovics, Ferenc AU - Erdélyi, Miklós AU - Aravin, Alexei A AU - Fejes Tóth, Katalin TI - The SUMO Ligase Su(var)2-10 Controls Hetero- and Euchromatic Gene Expression via Establishing H3K9 Trimethylation and Negative Feedback Regulation. JF - MOLECULAR CELL J2 - MOL CELL VL - 77 PY - 2020 IS - 3 SP - 571 EP - 585 PG - 15 SN - 1097-2765 DO - 10.1016/j.molcel.2019.09.033 UR - https://m2.mtmt.hu/api/publication/31148157 ID - 31148157 N1 - Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, United States Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, 123182, Russian Federation Institute of Genetics, Biological Research Centre, Szeged, 6726, Hungary Cited By :1 Export Date: 21 February 2020 CODEN: MOCEF Correspondence Address: Aravin, A.A.; Division of Biology and Biological Engineering, California Institute of TechnologyUnited States; email: aaa@caltech.edu WoS:hiba:000512932100012 2020-03-09 18:51 kötet nem egyezik, első oldal nem egyezik Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, United States Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, 123182, Russian Federation Institute of Genetics, Biological Research Centre, Szeged, 6726, Hungary Cited By :8 Export Date: 20 April 2021 CODEN: MOCEF Correspondence Address: Aravin, A.A.; Division of Biology and Biological Engineering, United States; email: aaa@caltech.edu AB - Сhromatin is critical for genome compaction and gene expression. On a coarse scale, the genome is divided into euchromatin, which harbors the majority of genes and is enriched in active chromatin marks, and heterochromatin, which is gene-poor but repeat-rich. The conserved molecular hallmark of heterochromatin is the H3K9me3 modification, which is associated with gene silencing. We found that in Drosophila, deposition of most of the H3K9me3 mark depends on SUMO and the SUMO ligase Su(var)2-10, which recruits the histone methyltransferase complex SetDB1/Wde. In addition to repressing repeats, H3K9me3 influences expression of both hetero- and euchromatic host genes. High H3K9me3 levels in heterochromatin are required to suppress spurious transcription and ensure proper gene expression. In euchromatin, a set of conserved genes is repressed by Su(var)2-10/SetDB1-induced H3K9 trimethylation, ensuring tissue-specific gene expression. Several components of heterochromatin are themselves repressed by this pathway, providing a negative feedback mechanism to ensure chromatin homeostasis. LA - English DB - MTMT ER - TY - JOUR AU - Varga, Gergely István AU - Csordás, Gábor AU - Cinege, Gyöngyi Ilona AU - Jankovics, Ferenc AU - Sinka, Rita AU - Kurucz, Judit Éva AU - Andó, István AU - Honti, Viktor TI - Headcase is a Repressor of Lamellocyte Fate in Drosophila melanogaster JF - GENES J2 - GENES-BASEL VL - 10 PY - 2019 IS - 3 PG - 17 SN - 2073-4425 DO - 10.3390/genes10030173 UR - https://m2.mtmt.hu/api/publication/30585796 ID - 30585796 N1 - Laboratory of Immunology, Institute of Genetics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, 6726, Hungary Laboratory of Drosophila Germ Cell Differentiation, Institute of Genetics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, 6726, Hungary Department of Genetics, Faculty of Science and Informatics, University of Szeged, Szeged, 6726, Hungary Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, 50931, Germany Cited By :3 Export Date: 19 January 2022 Correspondence Address: Andó, I.; Laboratory of Immunology, Hungary; email: ando.istvan@brc.mta.hu AB - Due to the evolutionary conservation of the regulation of hematopoiesis, Drosophila provides an excellent model organism to study blood cell differentiation and hematopoietic stem cell (HSC) maintenance. The larvae of Drosophila melanogaster respond to immune induction with the production of special effector blood cells, the lamellocytes, which encapsulate and subsequently kill the invader. Lamellocytes differentiate as a result of a concerted action of all three hematopoietic compartments of the larva: the lymph gland, the circulating hemocytes, and the sessile tissue. Within the lymph gland, the communication of the functional zones, the maintenance of HSC fate, and the differentiation of effector blood cells are regulated by a complex network of signaling pathways. Applying gene conversion, mutational analysis, and a candidate based genetic interaction screen, we investigated the role of Headcase (Hdc), the homolog of the tumor suppressor HECA in the hematopoiesis of Drosophila. We found that naive loss-of-function hdc mutant larvae produce lamellocytes, showing that Hdc has a repressive role in effector blood cell differentiation. We demonstrate that hdc genetically interacts with the Hedgehog and the Decapentaplegic pathways in the hematopoietic niche of the lymph gland. By adding further details to the model of blood cell fate regulation in the lymph gland of the larva, our findings contribute to the better understanding of HSC maintenance. LA - English DB - MTMT ER - TY - JOUR AU - Jankovics, Ferenc AU - Bence, Melinda AU - Sinka, Rita AU - Faragó, Anikó AU - Bodai, László AU - Pettkó-Szandtner, Aladár AU - Ibrahim, Karam AU - Takács, Zsanett AU - Szarka-Kovács, Alexandra Brigitta AU - Erdélyi, Miklós TI - Drosophila small ovary gene is required for transposon silencing and heterochromatin organization, and ensures germline stem cell maintenance and differentiation JF - DEVELOPMENT J2 - DEVELOPMENT VL - 145 PY - 2018 IS - 23 PG - 13 SN - 0950-1991 DO - 10.1242/dev.170639 UR - https://m2.mtmt.hu/api/publication/30377083 ID - 30377083 N1 - Funding Agency and Grant Number: Nemzeti Kutatasi, Fejlesztesies Innovacios Hivatal; Orszagos Tudomanyos Kutatasi Alapprogramok [NKFIH-K112294, NKFIH-K117010, OTKA-K108538, NKFIH-PD124446, GINOP-2.3.2-15-2016-00032, GINOP-2.3.2.-15-2016-00001]; Janos Bolyai Fellowship Funding text: This work was supported by grants from the Nemzeti Kutatasi, Fejlesztesies Innovacios Hivatal and the Orszagos Tudomanyos Kutatasi Alapprogramok (NKFIH-K112294, NKFIH-K117010, OTKA-K108538, NKFIH-PD124446, GINOP-2.3.2-15-2016-00032 and GINOP-2.3.2.-15-2016-00001). M.B. is supported by a Janos Bolyai Fellowship. Institute of Genetics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, 6726, Hungary Department of Genetics, University of Szeged, Szeged, 6726, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Laboratory of Proteomics Research, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, 6726, Hungary Cited By :9 Export Date: 20 April 2021 CODEN: DEVPE Correspondence Address: Jankovics, F.; Institute of Genetics, Hungary; email: jankovics.ferenc@brc.mta.hu AB - Self-renewal and differentiation of stem cells is one of the fundamental biological phenomena relying on proper chromatin organization. In our study, we describe a novel chromatin regulator encoded by the Drosophila small ovary (sov) gene. We demonstrate that soy is required in both the germline stem cells (GSCs) and the surrounding somatic niche cells to ensure GSC survival and differentiation. soy maintains niche integrity and function by repressing transposon mobility, not only in the germline, but also in the soma. Protein interactome analysis of Sov revealed an interaction between Sov and HP1a. In the germ cell nuclei, Soy colocalizes with HP1a, suggesting that Sov affects transposon repression as a component of the heterochromatin. In a position-effect variegation assay, we found a dominant genetic interaction between soy and HP1a, indicating their functional cooperation in promoting the spread of heterochromatin. An in vivo tethering assay and FRAP analysis revealed that Sov enhances heterochromatin formation by supporting the recruitment of HP1a to the chromatin. We propose a model in which soy maintains GSC niche integrity by regulating transposon silencing and heterochromatin formation. LA - English DB - MTMT ER - TY - JOUR AU - Varga, Gergely István AU - Csordás, Gábor AU - Jankovics, Ferenc AU - Lukacsovich, Tamás AU - Cinege, Gyöngyi Ilona AU - Sinka, Rita AU - Kurucz, Judit Éva AU - Andó, István AU - Honti, Viktor TI - Headcase, a novel regulator of hemocyte differentiation in Drosophila Melanogaster JF - IMMUNOLÓGIAI SZEMLE J2 - IMMUNOLÓGIAI SZEMLE VL - 10 PY - 2018 IS - 3 SP - 51 EP - 51 PG - 1 SN - 2061-0203 UR - https://m2.mtmt.hu/api/publication/30362934 ID - 30362934 LA - English DB - MTMT ER - TY - JOUR AU - Kristó, Ildikó AU - Bajusz, Csaba AU - Borsos, Barbara Nikolett AU - Pankotai, Tibor AU - Dopie, Joseph AU - Jankovics, Ferenc AU - Vartiainen, Maria K AU - Erdélyi, Miklós AU - Vilmos, Péter TI - The actin binding cytoskeletal protein Moesin is involved in nuclear mRNA export JF - BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH J2 - BBA-MOL CELL RES VL - 1864 PY - 2017 IS - 10 SP - 1589 EP - 1604 PG - 16 SN - 0167-4889 DO - 10.1016/j.bbamcr.2017.05.020 UR - https://m2.mtmt.hu/api/publication/3232089 ID - 3232089 N1 - Megjegyzés-26673593 N1 Funding details: ESF, European Social Fund N1 Funding text: This work was supported by the National Research, Development and Innovation Office – NKFIH (GINOP-2.3.2-15-2016-00001, GINOP-2.3.2-15-2016-00032, PD112118 and K117010). TP was supported by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences. The research was supported also by the European Union, State of Hungary, and the European Social Fund in the framework of TÁMOP-4.2.4.A/2-11/1-2012-0001 ‘National Excellence Program’. Biological Research Center of the Hungarian Academy of Sciences, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary University of Helsinki, Institute of Biotechnology, Helsinki, Finland Joseph Dopie, University of Illinois, Urbana, United States Cited By :2 Export Date: 2 September 2019 CODEN: BAMRD Correspondence Address: Vilmos, P.; Biological Research Center of the Hungarian Academy of SciencesHungary; email: vilmos.peter@brc.mta.hu Chemicals/CAS: protein, 67254-75-5; Cytoskeletal Proteins; Drosophila Proteins; ezrin; Membrane Proteins; messenger ribonucleoprotein; Microfilament Proteins; moesin; Nuclear Matrix-Associated Proteins; nuclear pore complex protein 98; Nuclear Pore Complex Proteins; Nucleocytoplasmic Transport Proteins; radixin; Rae1 protein, Drosophila; Ribonucleoproteins; RNA, Messenger Funding details: European Social Fund, ESF, A/2-11/1-2012-0001 Funding details: European Commission Funding details: Magyar Tudományos Akadémia, MTA Funding details: Office of Research, Innovation and Economic Development, California State Polytechnic University, Pomona, PD112118, K117010, GINOP-2.3.2-15-2016-00032, GINOP-2.3.2-15-2016-00001 Funding text 1: This work was supported by the National Research, Development and Innovation Office ? NKFIH (GINOP-2.3.2-15-2016-00001, GINOP-2.3.2-15-2016-00032, PD112118 and K117010). TP was supported by the J?nos Bolyai Research Scholarship of the Hungarian Academy of Sciences. The research was supported also by the European Union, State of Hungary, and the European Social Fund in the framework of T?MOP-4.2.4.A/2-11/1-2012-0001 ?National Excellence Program?. Biological Research Center of the Hungarian Academy of Sciences, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary University of Helsinki, Institute of Biotechnology, Helsinki, Finland Joseph Dopie, University of Illinois, Urbana, United States Cited By :3 Export Date: 10 March 2021 CODEN: BAMRD Correspondence Address: Vilmos, P.; Biological Research Center of the Hungarian Academy of SciencesHungary; email: vilmos.peter@brc.mta.hu Biological Research Center of the Hungarian Academy of Sciences, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary University of Helsinki, Institute of Biotechnology, Helsinki, Finland Joseph Dopie, University of Illinois, Urbana, United States Cited By :4 Export Date: 20 April 2021 CODEN: BAMRD Correspondence Address: Vilmos, P.; Biological Research Center of the Hungarian Academy of SciencesHungary; email: vilmos.peter@brc.mta.hu LA - English DB - MTMT ER -