@article{MTMT:31815661, title = {The phosphatome of opportunistic pathogen Candida species}, url = {https://m2.mtmt.hu/api/publication/31815661}, author = {Szabó, Krisztina and Miskei, Márton and Farkas, Ilona and Dombrádi, Viktor Béla}, doi = {10.1016/j.fbr.2020.12.002}, journal-iso = {FUNG BIOL REV}, journal = {FUNGAL BIOLOGY REVIEWS}, volume = {35}, unique-id = {31815661}, issn = {1749-4613}, abstract = {Several Candida species, the best known example of which is Candida albicans, are opportunistic human pathogens that are responsible for frequent nosocomial infections. A worrisome aspect of the currently available treatments of candidemia is the steady development of resistance to antifungals among these potentially life threatening fungi. Under these circumstances the search for novel drug targets is a well justified research direction. We propose that the principles of signal transduction therapy by targeting protein phosphatases can be adopted as these enzymes carry out important physiological functions in Candida. We demonstrate that C. tropicalis, C. albicans, C. dubliniensis, and S. cerevisiae exhibit the largest repertoire of protein phosphatases among the investigated fungi. Together with other opportunistic pathogen Candida species and the members of the Saccharomycetales order, they expanded their phosphatome by repeated gene duplications. We noted that evolution generated a set of fungus specific phosphatases which can be targeted without the danger of causing undesirable side effects in the human body. Based on the conflicting criteria of effectiveness and selectivity, we identified and characterized 7 phosphatases that are potent virulence determinants and may be utilized as potential antifungal drug targets. (C) 2020 The Authors. Published by Elsevier Ltd on behalf of British Mycological Society.}, keywords = {EVOLUTION; PROTEIN PHOSPHATASES; Protein Domains; PATHOGENIC FUNGI; Candida albicans; Enzyme phylogeny}, year = {2021}, eissn = {1878-0253}, pages = {40-51}, orcid-numbers = {Szabó, Krisztina/0000-0002-8461-9294} } @article{MTMT:30421124, title = {Dissection of the regulatory role for the N-terminal domain in Candida albicans protein phosphatase Z1}, url = {https://m2.mtmt.hu/api/publication/30421124}, author = {Szabó, Krisztina and Kónya, Zoltán and Erdődi, Ferenc and Farkas, Ilona and Dombrádi, Viktor Béla}, doi = {10.1371/journal.pone.0211426}, journal-iso = {PLOS ONE}, journal = {PLOS ONE}, volume = {14}, unique-id = {30421124}, issn = {1932-6203}, abstract = {The novel type, fungus specific protein phosphatase Z1 of the opportunistic pathogen, Candida albicans (CaPpz1) has several important physiological roles. It consists of a conserved C-terminal catalytic domain and a variable, intrinsically disordered, N-terminal regulatory domain. To test the function of these domains we modified the structure of CaPpz1 by in vitro mutagenesis. The two main domains were separated, four potential protein binding regions were deleted, and the myristoylation site as well as the active site of the enzyme was crippled by point mutations G2A and R262L, respectively. The in vitro phosphatase activity assay of the bacterially expressed recombinant proteins indicated that the N-terminal domain was inactive, while the C-terminal domain became highly active against myosin light chain substrate. The deletion of the N-terminal 1-16 amino acids and the G2A mutation significantly decreased the specific activity of the enzyme. Complementation of the ppz1 Saccharomyces cerevisiae deletion mutant strain with the different CaPpz1 forms demonstrated that the scission of the main domains, the two point mutations and the N-terminal 1-16 deletion rendered the phosphatase incompetent in the in vivo assays of LiCl tolerance and caffeine sensitivity. Thus our results confirmed the functional role of the N-terminal domain and highlighted the significance of the very N-terminal part of the protein in the regulation of CaPpz1.}, year = {2019}, eissn = {1932-6203} } @article{MTMT:3117563, title = {Functional investigation of the unstructured N-terminal domain of protein phosphatase Z1}, url = {https://m2.mtmt.hu/api/publication/3117563}, author = {Szabó, K and Kónya, Zoltán and Dombrádi, Viktor Béla and Farkas, Ilona}, journal-iso = {BIOKÉMIA}, journal = {BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA}, volume = {40}, unique-id = {3117563}, issn = {0133-8455}, year = {2016}, eissn = {2060-8152}, pages = {46} } @article{MTMT:2814667, title = {The B″ regulatory subunit of protein phosphatase 2A mediates the dephosphorylation of rice retinoblastoma‑related protein‑1}, url = {https://m2.mtmt.hu/api/publication/2814667}, author = {Ábrahám, Edit and Yu, Ping and Farkas, Ilona and Darula, Zsuzsanna and Varga, Erzsébet and Lukács, Noémi and Ayaydin, Ferhan and Medzihradszky F., Katalin and Dombrádi, Viktor Béla and Dudits, Dénes and Horváth V., Gábor}, doi = {10.1007/s11103-014-0265-y}, journal-iso = {PLANT MOL BIOL}, journal = {PLANT MOLECULAR BIOLOGY}, volume = {87}, unique-id = {2814667}, issn = {0167-4412}, year = {2015}, eissn = {1573-5028}, pages = {125-141} } @article{MTMT:2040975, title = {Protein phosphatase Z modulates oxidative stress response in fungi}, url = {https://m2.mtmt.hu/api/publication/2040975}, author = {Leiter, Éva Juliánna and González, A and Erdei, É and Casado, C and Kovács, László and Ádám, Csaba and Oláh, J and Miskei, Márton and Molnár, Mónika and Farkas, Ilona and Kozma-Bognárné Hamari, Zsuzsanna and Arino, J and Pócsi, István and Dombrádi, Viktor Béla}, doi = {10.1016/j.fgb.2012.06.010}, journal-iso = {FUNGAL GENET BIOL}, journal = {FUNGAL GENETICS AND BIOLOGY}, volume = {49}, unique-id = {2040975}, issn = {1087-1845}, year = {2012}, eissn = {1096-0937}, pages = {708-716}, orcid-numbers = {Kozma-Bognárné Hamari, Zsuzsanna/0000-0001-6374-5083} } @article{MTMT:1856931, title = {Protein phosphatase CaPpz1 is involved in cation homeostasis, cell wall integrity and virulence of Candida albicans}, url = {https://m2.mtmt.hu/api/publication/1856931}, author = {Ádám, Csaba and Erdei, É and Casado, C and Kovács, László and González, A and Majoros, László and Petrényi, Katalin and Bagossi, P and Farkas, Ilona and Molnár, Mónika and Pócsi, István and Arino, J and Dombrádi, Viktor Béla}, doi = {10.1099/mic.0.057075-0}, journal-iso = {MICROBIOL-SGM}, journal = {MICROBIOLOGY-SGM}, volume = {158}, unique-id = {1856931}, issn = {1350-0872}, year = {2012}, eissn = {1465-2080}, pages = {1258-1267} } @article{MTMT:1847601, title = {The histone phosphatase inhibitory property of plant nucleosome assembly protein-related proteins (NRPs)}, url = {https://m2.mtmt.hu/api/publication/1847601}, author = {Bíró, Judit and Farkas, Ilona and Domoki, Mónika and Ötvös, Krisztina and Bottka, Sándor Előd and Dombrádi, Viktor Béla and Fehér, Attila}, doi = {10.1016/j.plaphy.2011.12.010}, journal-iso = {PLANT PHYSIOL BIOCH (PPB)}, journal = {PLANT PHYSIOLOGY AND BIOCHEMISTRY}, volume = {52}, unique-id = {1847601}, issn = {0981-9428}, year = {2012}, eissn = {1873-2690}, pages = {162-168}, orcid-numbers = {Ötvös, Krisztina/0000-0002-5503-4983; Fehér, Attila/0000-0002-4183-3696} } @misc{MTMT:1818470, title = {The B" subunit of protein phosphatase 2A interacts with a retinoblastoma-related protein in Oryza sativa}, url = {https://m2.mtmt.hu/api/publication/1818470}, editor = {Farkas, Ilona and Ábrahám, E and Yu, P and Dombrádi, Viktor Béla and Dudits, D and Horváth, GV}, unique-id = {1818470}, year = {2011} } @misc{MTMT:1818466, title = {Functional analysis of protein phosphatase Z in the pathogenic fungus Candida albicans}, url = {https://m2.mtmt.hu/api/publication/1818466}, editor = {Ádám, Cs and Kovács, L and Casado, C and Erdei, A and González, A and Majoros, László and Bagossi, P and Farkas, Ilona and Molnár, M and Pócsi, István and Arino, J and Dombrádi, Viktor Béla}, unique-id = {1818466}, year = {2011} } @article{MTMT:1818446, title = {A protein foszfatáz 2A B" alegysége kölcsönhatásba lép a rizs retinoblasztóma-szerű fehérjével}, url = {https://m2.mtmt.hu/api/publication/1818446}, author = {Farkas, Ilona and Ábrahám, E and Yu, P and Dombrádi, Viktor Béla and Dudits, D and Horváth, VG}, journal-iso = {BIOKÉMIA}, journal = {BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA}, volume = {35}, unique-id = {1818446}, issn = {0133-8455}, year = {2011}, eissn = {2060-8152}, pages = {33-33} }