@article{MTMT:2879395,
	title = {Mutation in the Drosophila melanogaster adenosine receptor gene selectively decreases the mosaic hyperplastic epithelial outgrowth rates in wts or dco heterozygous flies},
	url = {https://m2.mtmt.hu/api/publication/2879395},
	author = {Sidorov, R and Kucerova, L and Kiss, István and Zurovec, M},
	doi = {10.1007/s11302-014-9435-2},
	journal-iso = {PURINERG SIGNAL},
	journal = {PURINERGIC SIGNALLING},
	volume = {11},
	unique-id = {2879395},
	issn = {1573-9538},
	abstract = {Adenosine (Ado) is a ubiquitous metabolite that plays a prominent role as a paracrine homeostatic signal of metabolic imbalance within tissues. It quickly responds to various stress stimuli by adjusting energy metabolism and influencing cell growth and survival. Ado is also released by dead or dying cells and is present at significant concentrations in solid tumors. Ado signaling is mediated by Ado receptors (AdoR) and proteins modulating its concentration, including nucleoside transporters and Ado deaminases. We examined the impact of genetic manipulations of three Drosophila genes involved in Ado signaling on the incidence of somatic mosaic clones formed by the loss of heterozygosity (LOH) of tumor suppressor and marker genes. We show here that genetic manipulations with the AdoR, equilibrative nucleoside transporter 2 (Ent2), and Ado deaminase growth factor-A (Adgf-A) cause dramatic changes in the frequency of hyperplastic outgrowth clones formed by LOH of the warts (wts) tumor suppressor, while they have almost no effect on control yellow (y) clones. In addition, the effect of AdoR is dose-sensitive and its overexpression leads to the increase in wts hyperplastic epithelial outgrowth rates. Consistently, the frequency of mosaic hyperplastic outgrowth clones generated by the LOH of another tumor suppressor, discs overgrown (dco), belonging to the wts signaling pathway is also dependent on AdoR. Our results provide interesting insight into the maintenance of tissue homeostasis at a cellular level.},
	year = {2015},
	eissn = {1573-9546},
	pages = {95-105}
}

@article{MTMT:2839637,
	title = {Drosophila Spag Is the Homolog of RNA Polymerase II-associated Protein 3 (RPAP3) and Recruits the Heat Shock Proteins 70 and 90 (Hsp70 and Hsp90) during the Assembly of Cellular Machineries},
	url = {https://m2.mtmt.hu/api/publication/2839637},
	author = {Benbahouche, NE and Iliopoulos, I and Torok, I and Marhold, J and Henri, J and Kajava, AV and Farkas, R and Kempf, T and Schnolzer, M and Meyer, P and Kiss, István and Bertrand, E and Mechler, BM and Pradet-Balade, B},
	doi = {10.1074/jbc.M113.499608},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {289},
	unique-id = {2839637},
	issn = {0021-9258},
	abstract = {Background: Mammalian RNA polymerase II-associated protein 3 (RPAP3) recruits heat shock protein 90 (Hsp90) to assemble cellular machineries such as RNA polymerases. Results:Spaghetti encodes the Drosophila homolog of RPAP3. Spaghetti is essential for development. Spag protein binds and stimulates Hsp90 and Hsp70. Conclusion: RPAP3 function is conserved among metazoans. Significance: Our data suggest that Hsp70 assists RPAP3 in complex assembly. The R2TP is a recently identified Hsp90 co-chaperone, composed of four proteins as follows: Pih1D1, RPAP3, and the AAA(+)-ATPases RUVBL1 and RUVBL2. In mammals, the R2TP is involved in the biogenesis of cellular machineries such as RNA polymerases, small nucleolar ribonucleoparticles and phosphatidylinositol 3-kinase-related kinases. Here, we characterize the spaghetti (spag) gene of Drosophila, the homolog of human RPAP3. This gene plays an essential function during Drosophila development. We show that Spag protein binds Drosophila orthologs of R2TP components and Hsp90, like its yeast counterpart. Unexpectedly, Spag also interacts and stimulates the chaperone activity of Hsp70. Using null mutants and flies with inducible RNAi, we show that spaghetti is necessary for the stabilization of snoRNP core proteins and target of rapamycin activity and likely the assembly of RNA polymerase II. This work highlights the strong conservation of both the HSP90/R2TP system and its clients and further shows that Spag, unlike Saccharomyces cerevisiae Tah1, performs essential functions in metazoans. Interaction of Spag with both Hsp70 and Hsp90 suggests a model whereby R2TP would accompany clients from Hsp70 to Hsp90 to facilitate their assembly into macromolecular complexes.},
	keywords = {GENE; MELANOGASTER; Hsp70; HSP90; chaperone; BINDING-PROTEIN; protein assembly; RNA polymerase II; INTERACTION NETWORK; R2TP COMPLEX; 2ND CHROMOSOME; IMAGINAL DISCS; REACTION CYCLE; HUMAN TRANSCRIPTION MACHINERY; Spaghetti Gene; RPAP3; TOR Complex (TORC); Small Nucleolar RNA (snoRNA)},
	year = {2014},
	eissn = {1083-351X},
	pages = {6236-6247}
}

@article{MTMT:2383668,
	title = {Selective elimination/RNAi silencing of FMRF-related peptides and their receptors decreases the locomotor activity in Drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/2383668},
	author = {Kiss, Brigitta and Szlanka, Tamás and Zvara, Ágnes and Michal, Žurovec and Michal, Sery and Štefan, Kakaš and Ramasz, Beáta and Hegedűs, Zoltán and Tamás, Lukacsovich and Puskás, László and Fónagy, Adrien and Kiss, István},
	doi = {10.1016/j.ygcen.2013.05.023},
	journal-iso = {GEN COMP ENDOCR},
	journal = {GENERAL AND COMPARATIVE ENDOCRINOLOGY},
	volume = {191},
	unique-id = {2383668},
	issn = {0016-6480},
	year = {2013},
	eissn = {1095-6840},
	pages = {137-145}
}

@article{MTMT:2034630,
	title = {Uracil-Containing DNA in Drosophila: Stability, Stage-Specific Accumulation, and Developmental Involvement},
	url = {https://m2.mtmt.hu/api/publication/2034630},
	author = {Muha, Villő and Horváth, András and Békési, Angéla and Pukáncsik, Mária and Hodoscsek, B and Merényi, Gábor and Róna, Gergely and Batki, J and Kiss, István and Jankovics, Ferenc and Vilmos, Péter and Erdélyi, Miklós and Vértessy, Beáta (Grolmuszné)},
	doi = {10.1371/journal.pgen.1002738},
	journal-iso = {PLOS GENET},
	journal = {PLOS GENETICS},
	volume = {8},
	unique-id = {2034630},
	issn = {1553-7390},
	abstract = {Base-excision repair and control of nucleotide pools safe-guard against permanent uracil accumulation in DNA relying on two key enzymes: uracil-DNA glycosylase and dUTPase. Lack of the major uracil-DNA glycosylase UNG gene from the fruit fly genome and dUTPase from fruit fly larvae prompted the hypotheses that i) uracil may accumulate in Drosophila genomic DNA where it may be well tolerated, and ii) this accumulation may affect development. Here we show that i) Drosophila melanogaster tolerates high levels of uracil in DNA; ii) such DNA is correctly interpreted in cell culture and embryo; and iii) under physiological spatio-temporal control, DNA from fruit fly larvae, pupae, and imago contain greatly elevated levels of uracil (200-2,000 uracil/million bases, quantified using a novel real-time PCR-based assay). Uracil is accumulated in genomic DNA of larval tissues during larval development, whereas DNA from imaginal tissues contains much less uracil. Upon pupation and metamorphosis, uracil content in DNA is significantly decreased. We propose that the observed developmental pattern of uracil-DNA is due to the lack of the key repair enzyme UNG from the Drosophila genome together with down-regulation of dUTPase in larval tissues. In agreement, we show that dUTPase silencing increases the uracil content in DNA of imaginal tissues and induces strong lethality at the early pupal stages, indicating that tolerance of highly uracil-substituted DNA is also stage-specific. Silencing of dUTPase perturbs the physiological pattern of uracil-DNA accumulation in Drosophila and leads to a strongly lethal phenotype in early pupal stages. These findings suggest a novel role of uracil-containing DNA in Drosophila development and metamorphosis and present a novel example for developmental effects of dUTPase silencing in multicellular eukaryotes. Importantly, we also show lack of the UNG gene in all available genomes of other Holometabola insects, indicating a potentially general tolerance and developmental role of uracil-DNA in this evolutionary clade.},
	year = {2012},
	eissn = {1553-7404},
	orcid-numbers = {Békési, Angéla/0000-0003-2294-3002; Róna, Gergely/0000-0003-3222-7261}
}

@article{MTMT:1922090,
	title = {Specific Cooperation Between Imp­α2 and Imp­β/Ketel in Spindle assembly during Drosophila Early Nuclear Divisions},
	url = {https://m2.mtmt.hu/api/publication/1922090},
	author = {Virágh, Eszter Erika and Gorjánácz, Mátyás and Török, István and Eichhorn, T and Kallakuri, S and Szlanka, Tamás and Kiss, István and Mechler, BM},
	doi = {10.1534/g3.111.001073},
	journal-iso = {G3-GENES GENOM GENET},
	journal = {G3-GENES GENOMES GENETICS},
	volume = {2},
	unique-id = {1922090},
	issn = {2160-1836},
	year = {2012},
	eissn = {2160-1836},
	pages = {1-14}
}

@article{MTMT:1916849,
	title = {High-resolution, high-throughput SNP mapping in Drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/1916849},
	author = {Chen, D and Ahlford, A and Schnorrer, F and Kalchhauser, I and Fellner, M and Virágh, Eszter Erika and Kiss, István and Syvanen, AC and Dickson, BJ},
	doi = {10.1038/NMETH.1191},
	journal-iso = {NAT METHODS},
	journal = {NATURE METHODS},
	volume = {5},
	unique-id = {1916849},
	issn = {1548-7091},
	abstract = {Single nucleotide polymorphisms (SNPs) are useful markers for genetic mapping experiments in model organisms. Here we report the establishment of a high-density SNP map and high-throughput genotyping assays for Drosophila melanogaster. Our map comprises 27,367 SNPs in common laboratory Drosophila stocks. These SNPs were clustered within 2,238 amplifiable markers at an average density of 1 marker every 50.3 kb, or 6.3 genes. We have also constructed a set of 62 Drosophila stocks, each of which facilitates the generation of recombinants within a defined genetic interval of 1-2 Mb. For flexible, high-throughput SNP genotyping, we used fluorescent tag-array mini-sequencing (TAMS) assays. We designed and validated TAMS assays for 293 SNPs at an average resolution of 391.3 kb, and demonstrated the utility of these tools by rapidly mapping 14 mutations that disrupt embryonic muscle patterning. These resources enable high-resolution high-throughput genetic mapping in Drosophila.},
	year = {2008},
	eissn = {1548-7105},
	pages = {323-329}
}

@article{MTMT:1915394,
	title = {The toxic effect of aluminium and its supposable mechanism in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/1915394},
	author = {Kiss, AS and Kiss, István and Csikkel-Szolnoki, A},
	journal-iso = {ACTA PHYTOPATHOL ENTOMOL HUNG},
	journal = {ACTA PHYTOPATHOLOGICA ET ENTOMOLOGICA HUNGARICA},
	volume = {12},
	unique-id = {1915394},
	issn = {0238-1249},
	year = {2007},
	eissn = {1588-2691},
	pages = {281-285}
}

@article{MTMT:1914423,
	title = {Domains of importin-alpha 2 required for ring canal assembly during Drosophila oogenesis},
	url = {https://m2.mtmt.hu/api/publication/1914423},
	author = {Gorjánácz, Mátyás and Török, István and Pomozi, István and Garab, Győző and Szlanka, Tamás and Kiss, István and Mechler, BM},
	doi = {10.1016/j.jsb.2005.12.007},
	journal-iso = {J STRUCT BIOL},
	journal = {JOURNAL OF STRUCTURAL BIOLOGY},
	volume = {154},
	unique-id = {1914423},
	issn = {1047-8477},
	year = {2006},
	eissn = {1095-8657},
	pages = {27-41}
}

@article{MTMT:1914329,
	title = {Spotted-dick, a zinc-finger protein of Drosophila required for expression of Orc4 and S phase},
	url = {https://m2.mtmt.hu/api/publication/1914329},
	author = {Page, AR and Kovacs, A and Deák, Péter and Török, Tibor and Kiss, István and Dario, P and Bastos, C and Batista, P and Gomes, R and Ohkura, H and Russell, S and Glover, DM},
	doi = {10.1038/sj.emboj.7600890},
	journal-iso = {EMBO J},
	journal = {EMBO JOURNAL},
	volume = {24},
	unique-id = {1914329},
	issn = {0261-4189},
	year = {2005},
	eissn = {1460-2075},
	pages = {4304-4315},
	orcid-numbers = {Török, Tibor/0000-0002-2128-1126}
}

@article{MTMT:1912844,
	title = {Deletion of proteasomal subunit S5a/Rpn10/p54 causes lethality, multiple mitotic defects and overexpression of proteasomal genes in Drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/1912844},
	author = {Szlanka, Tamás and Haracska, Lajos and Kiss, István and Deák, Péter and Kurucz, Judit Éva and Andó, István and Virágh, Eszter Erika and Udvardy, Andor},
	doi = {10.1242/jcs.00332},
	journal-iso = {J CELL SCI},
	journal = {JOURNAL OF CELL SCIENCE},
	volume = {116},
	unique-id = {1912844},
	issn = {0021-9533},
	abstract = {The regulatory complex of the 26S proteasome is responsible for the selective recognition and binding of multiubiquitinated proteins. It was earlier shown that the subunit S5a/Rpn10/p54 of the regulatory complex is the only cellular protein capable of binding multiubiquitin chains in an in vitro overlay assay. The role of this subunit in substrate selection, however, is a subject of debate, following the observation that its deletion in Saccharomyces cerevisiae is not lethal and instead causes only a mild phenotype. To study the function of this subunit in higher eukaryotes, a mutant Drosophila strain was constructed by deleting the single copy gene encoding subunit S5a/Rpn10/p54. This deletion caused larval-pupal polyphasic lethality, multiple mitotic defects, the accumulation of higher multimers of ubiquitinated proteins and a huge accumulation of defective 26S proteasome particles. Deletion of the subunit S5a/Rpn10/p54 does not destabilise the regulatory complex and does not disturb the assembly of the regulatory complex and the catalytic core. The pupal lethality is a consequence of the depletion of the maternally provided 26S proteasome during the larval stages and a sudden increase in the proteasomal activity demands during the first few hours of pupal development. The huge accumulation of the fully assembled 26S proteasome in the deletion mutant and the lack of free subunits or partially assembled particles indicate that there is a highly coordinated accumulation of all the subunits of the 26S proteasome. This suggests that in higher eukaryotes, as with yeast, a feedback circuit coordinately regulates the expression of the proteasomal genes, and this adjusts the actual proteasome concentration in the cells according to the temporal and/or spatial proteolytic demands.},
	keywords = {Animals; Female; Female; Male; Male; PHENOTYPE; PHENOTYPE; YEAST; INSECT; MUTAGENESIS; review; Eukaryota; gene expression regulation; Saccharomyces cerevisiae; Saccharomyces cerevisiae; priority journal; controlled study; nonhuman; animal tissue; animal experiment; larva; larva; Animalia; MELANOGASTER; Protein Binding; in vitro study; enzyme activity; MOLECULAR RECOGNITION; Mitosis; Mitosis; Gene Expression Regulation, Developmental; Drosophila melanogaster; Drosophila melanogaster; Drosophila melanogaster; Gene Deletion; Gene Deletion; insecta; embryo; UBIQUITIN; Proteasome Endopeptidase Complex; proteasome; 26S PROTEASOME; concentration (parameters); Carrier Proteins; enzyme substrate; enzyme subunit; gene overexpression; lethality; eukaryote; protein degradation; feedback system; Peptide Hydrolases; Drosophila Proteins; protein assembly; Saccharomyces cerevisiae Proteins; Genes, Lethal; Pupa; Mitotic phenotype; Multiubiquitin binding subunit; Regulatory complex; S5a/Rpn10/p54 subunit},
	year = {2003},
	eissn = {1477-9137},
	pages = {1023-1033},
	orcid-numbers = {Andó, István/0000-0002-4648-9396}
}