@article{MTMT:2871663,
	title = {Role of the Deubiquitylating Enzyme DmUsp5 in Coupling Ubiquitin Equilibrium to Development and Apoptosis in Drosophila melanogaster.},
	url = {https://m2.mtmt.hu/api/publication/2871663},
	author = {Kovács, Levente and Nagy, Olga Mária and Pál, Margit and Udvardy, Andor and Popescu, O and Deák, Péter},
	doi = {10.1371/journal.pone.0120875},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {10},
	unique-id = {2871663},
	issn = {1932-6203},
	year = {2015},
	eissn = {1932-6203},
	orcid-numbers = {Kovács, Levente/0000-0002-3226-3740; Nagy, Olga Mária/0000-0003-1471-5165}
}

@article{MTMT:1921997,
	title = {Overexpression of Dsk2/dUbqln results in severe developmental defects and lethality in Drosophila melanogaster that can be rescued by overexpression of the p54/Rpn10/S5a proteasomal subunit.},
	url = {https://m2.mtmt.hu/api/publication/1921997},
	author = {Lipinszki, Zoltán and Pál, Margit and Nagy, Olga Mária and Deák, Péter and Hunyadi-Gulyás Éva, Csilla and Udvardy, Andor},
	doi = {10.1111/j.1742-4658.2011.08383.x},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	volume = {278},
	unique-id = {1921997},
	issn = {1742-464X},
	abstract = {Polyubiquitin receptors execute the targeting of polyubiquitylated proteins to the 26S proteasome. In vitro studies indicate that disturbance of the physiological balance among different receptor proteins impairs the proteasomal degradation of polyubiquitylated proteins. To study the physiological consequences of shifting the in vivo equilibrium between the p54/Rpn10 proteasomal and the Dsk2/dUbqln extraproteasomal polyubiquitin receptors, transgenic Drosophila lines were constructed in which the overexpression or RNA interference-mediated silencing of these receptors can be induced. Flies overexpressing Flag-p54 were viable and fertile, without any detectable morphological abnormalities, although detectable accumulation of polyubiquitylated proteins demonstrated a certain level of proteolytic disturbance. Flag-p54 was assembled into the 26S proteasome and could fully complement the lethal phenotype of a p54 null mutant Drosophila line. The overexpression of Dsk2 caused severe morphological abnormalities in the late pupal stages, leading to pharate adult lethality, accompanied by a huge accumulation of highly polyubiquitylated proteins. The lethal phenotype of Dsk2 overexpression could be rescued in a double transgenic line coexpressing Flag-Dsk2 and Flag-p54. Although the double transgenic line was viable and fertile, it did not restore the proteolytic defects; the accumulation of the highly polyubiquitylated proteins was even more severe in the double transgenic line. Significant differences were found in the Dsk2-26S proteasome interaction in Drosophila melanogaster as compared with Saccharomyces cerevisiae. In yeast, Dsk2 can interact only with DeltaRpn10 proteasomes and not with the wild-type one. In Drosophila, Dsk2 does not interact with Deltap54 proteasomes, but the interaction can be fully restored by complementing the Deltap54 deletion with Flag-p54. Structured digital abstract * Dsk2 physically interacts with p54 by pull down (View Interaction: 1, 2) * p54 binds to Dsk2 by pull down (View interaction).},
	keywords = {Animals; ARTICLE; Saccharomyces cerevisiae; Saccharomyces cerevisiae; priority journal; controlled study; nonhuman; developmental biology; Cell Cycle Proteins; RNA Interference; Animals, Genetically Modified; Drosophila melanogaster; Drosophila melanogaster; Drosophila melanogaster; unclassified drug; protein protein interaction; Proteasome Endopeptidase Complex; proteasome; 26S PROTEASOME; 26S PROTEASOME; Carrier Proteins; transgenic animal; gene overexpression; lethality; protein degradation; Drosophila Proteins; Ubiquitination; larval development; Pupa; Ubiquitylation; Dsk2/dUbqln; p54/Rpn10/S5a; polyubiquitin receptors; Dsk2 protein; polyubiquitin; polyubiquitin; protein p54; pupa (life cycle stage)},
	year = {2011},
	eissn = {1742-4658},
	pages = {4833-4844},
	orcid-numbers = {Lipinszki, Zoltán/0000-0002-2067-0832; Nagy, Olga Mária/0000-0003-1471-5165}
}

@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}
}