TY - JOUR AU - Szabó, Krisztina AU - Miskei, Márton AU - Farkas, Ilona AU - Dombrádi, Viktor Béla TI - The phosphatome of opportunistic pathogen Candida species JF - FUNGAL BIOLOGY REVIEWS J2 - FUNG BIOL REV VL - 35 PY - 2021 SP - 40 EP - 51 PG - 12 SN - 1749-4613 DO - 10.1016/j.fbr.2020.12.002 UR - https://m2.mtmt.hu/api/publication/31815661 ID - 31815661 N1 - Funding Agency and Grant Number: Hungarian National Research, Development and Innovation Office [NKFIH K108989]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; New National Excellence Program of the Ministry for Innovation and Technology, Hungary [UNKP-20-5] Funding text: The expert technical assistance of Ms. Andrea Tankane-Farkas is acknowledged. This work was supported by the Hungarian National Research, Development and Innovation Office (grant number NKFIH K108989). MM was supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences, and by the New National Excellence Program of the Ministry for Innovation and Technology, Hungary (grant number UNKP-20-5). AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Szabó, Krisztina AU - Kónya, Zoltán AU - Erdődi, Ferenc AU - Farkas, Ilona AU - Dombrádi, Viktor Béla TI - Dissection of the regulatory role for the N-terminal domain in Candida albicans protein phosphatase Z1 JF - PLOS ONE J2 - PLOS ONE VL - 14 PY - 2019 IS - 2 PG - 16 SN - 1932-6203 DO - 10.1371/journal.pone.0211426 UR - https://m2.mtmt.hu/api/publication/30421124 ID - 30421124 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Szabó, K AU - Kónya, Zoltán AU - Dombrádi, Viktor Béla AU - Farkas, Ilona TI - Functional investigation of the unstructured N-terminal domain of protein phosphatase Z1 JF - BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA J2 - BIOKÉMIA VL - 40 PY - 2016 SP - 46 SN - 0133-8455 UR - https://m2.mtmt.hu/api/publication/3117563 ID - 3117563 LA - English DB - MTMT ER - TY - JOUR AU - Ábrahám, Edit AU - Yu, Ping AU - Farkas, Ilona AU - Darula, Zsuzsanna AU - Varga, Erzsébet AU - Lukács, Noémi AU - Ayaydin, Ferhan AU - Medzihradszky F., Katalin AU - Dombrádi, Viktor Béla AU - Dudits, Dénes AU - Horváth V., Gábor TI - The B″ regulatory subunit of protein phosphatase 2A mediates the dephosphorylation of rice retinoblastoma‑related protein‑1 JF - PLANT MOLECULAR BIOLOGY J2 - PLANT MOL BIOL VL - 87 PY - 2015 IS - 1-2 SP - 125 EP - 141 PG - 17 SN - 0167-4412 DO - 10.1007/s11103-014-0265-y UR - https://m2.mtmt.hu/api/publication/2814667 ID - 2814667 LA - English DB - MTMT ER - TY - JOUR AU - Leiter, Éva Juliánna AU - González, A AU - Erdei, É AU - Casado, C AU - Kovács, László AU - Ádám, Csaba AU - Oláh, J AU - Miskei, Márton AU - Molnár, Mónika AU - Farkas, Ilona AU - Kozma-Bognárné Hamari, Zsuzsanna AU - Arino, J AU - Pócsi, István AU - Dombrádi, Viktor Béla TI - Protein phosphatase Z modulates oxidative stress response in fungi JF - FUNGAL GENETICS AND BIOLOGY J2 - FUNGAL GENET BIOL VL - 49 PY - 2012 SP - 708 EP - 716 PG - 9 SN - 1087-1845 DO - 10.1016/j.fgb.2012.06.010 UR - https://m2.mtmt.hu/api/publication/2040975 ID - 2040975 N1 - Department of Microbial Biotechnology and Cell Biology, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Cerdanyola del Vallès 08193, Barcelona, Spain Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, Nagyerdei krt. 98, H-4032 Debrecen, Hungary Department of Microbiology, Faculty of Science, University of Szeged, Középfasor 52, H-6726 Szeged, Hungary Cited By :26 Export Date: 30 May 2023 CODEN: FGBIF Correspondence Address: Pócsi, I.; Department of Microbial Biotechnology and Cell Biology, P.O. Box 63, H-4010 Debrecen, Hungary; email: istvan.pocsi@science.unideb.hu LA - English DB - MTMT ER - TY - JOUR AU - Ádám, Csaba AU - Erdei, É AU - Casado, C AU - Kovács, László AU - González, A AU - Majoros, László AU - Petrényi, Katalin AU - Bagossi, P AU - Farkas, Ilona AU - Molnár, Mónika AU - Pócsi, István AU - Arino, J AU - Dombrádi, Viktor Béla TI - Protein phosphatase CaPpz1 is involved in cation homeostasis, cell wall integrity and virulence of Candida albicans JF - MICROBIOLOGY-SGM J2 - MICROBIOL-SGM VL - 158 PY - 2012 IS - 5 SP - 1258 EP - 1267 PG - 10 SN - 1350-0872 DO - 10.1099/mic.0.057075-0 UR - https://m2.mtmt.hu/api/publication/1856931 ID - 1856931 N1 - Besorolás Név: JOUR idéző Cím: Protein phosphatase CaPpz1 is involved in cation homeostasis, cell wall integrity and virulence of Candida albicans idéző Cím: Microbiology idéző Folyóirat/Könyv cím/Szabadalmi szám: Microbiology idéző Kötet: 158 Jelleg Műfaj: JOUR LA - English DB - MTMT ER - TY - JOUR AU - Bíró, Judit AU - Farkas, Ilona AU - Domoki, Mónika AU - Ötvös, Krisztina AU - Bottka, Sándor Előd AU - Dombrádi, Viktor Béla AU - Fehér, Attila TI - The histone phosphatase inhibitory property of plant nucleosome assembly protein-related proteins (NRPs) JF - PLANT PHYSIOLOGY AND BIOCHEMISTRY J2 - PLANT PHYSIOL BIOCH (PPB) VL - 52 PY - 2012 SP - 162 EP - 168 PG - 7 SN - 0981-9428 DO - 10.1016/j.plaphy.2011.12.010 UR - https://m2.mtmt.hu/api/publication/1847601 ID - 1847601 LA - English DB - MTMT ER - TY - BOOK ED - Farkas, Ilona ED - Ábrahám, E ED - Yu, P ED - Dombrádi, Viktor Béla ED - Dudits, D ED - Horváth, GV TI - The B" subunit of protein phosphatase 2A interacts with a retinoblastoma-related protein in Oryza sativa ET - 0 PY - 2011 UR - https://m2.mtmt.hu/api/publication/1818470 ID - 1818470 LA - English DB - MTMT ER - TY - BOOK ED - Ádám, Cs ED - Kovács, L ED - Casado, C ED - Erdei, A ED - González, A ED - Majoros, László ED - Bagossi, P ED - Farkas, Ilona ED - Molnár, M ED - Pócsi, István ED - Arino, J ED - Dombrádi, Viktor Béla TI - Functional analysis of protein phosphatase Z in the pathogenic fungus Candida albicans ET - 0 PY - 2011 UR - https://m2.mtmt.hu/api/publication/1818466 ID - 1818466 LA - English DB - MTMT ER - TY - JOUR AU - Farkas, Ilona AU - Ábrahám, E AU - Yu, P AU - Dombrádi, Viktor Béla AU - Dudits, D AU - Horváth, VG TI - A protein foszfatáz 2A B" alegysége kölcsönhatásba lép a rizs retinoblasztóma-szerű fehérjével JF - BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA J2 - BIOKÉMIA VL - 35 PY - 2011 IS - 3 SP - 33 EP - 33 PG - 1 SN - 0133-8455 UR - https://m2.mtmt.hu/api/publication/1818446 ID - 1818446 LA - Hungarian DB - MTMT ER -