@article{MTMT:32531214, title = {Lipids and Trehalose Actively Cooperate in Heat Stress Management of Schizosaccharomyces pombe}, url = {https://m2.mtmt.hu/api/publication/32531214}, author = {Péter, Mária and Gudmann, Péter and Kóta, Zoltán and Török, Zsolt and Vigh, László and Glatz, Attila and Balogh, Gábor}, doi = {10.3390/ijms222413272}, journal-iso = {INT J MOL SCI}, journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES}, volume = {22}, unique-id = {32531214}, issn = {1661-6596}, year = {2021}, eissn = {1422-0067}, orcid-numbers = {Kóta, Zoltán/0000-0003-2420-8773} } @article{MTMT:31134487, title = {Delineating the Rules for Structural Adaptation of Membrane-Associated Proteins to Evolutionary Changes in Membrane Lipidome}, url = {https://m2.mtmt.hu/api/publication/31134487}, author = {Makarova, Maria and Péter, Mária and Balogh, Gábor and Glatz, Attila and MacRae, James I. and Lopez Mora, Nestor and Booth, Paula and Makeyev, Eugene and Vigh, László and Oliferenko, Snezhana}, doi = {10.1016/j.cub.2019.11.043}, journal-iso = {CURR BIOL}, journal = {CURRENT BIOLOGY}, volume = {30}, unique-id = {31134487}, issn = {0960-9822}, year = {2020}, eissn = {1879-0445}, pages = {367-380} } @article{MTMT:31665750, title = {Miért csillapított a stresszválasz az öregedés során, avagy a dajkafehérje expresszió és a membrán-fluiditás kapcsolata}, url = {https://m2.mtmt.hu/api/publication/31665750}, author = {Benkő, Sándor and Balogh, Gábor and Péter, Mária and Török, Zsolt and Gombos, Imre and Glatz, Attila and Horváth, Ibolya and Vigh, László}, journal-iso = {IDŐSGYÓGYÁSZAT}, journal = {IDŐSGYÓGYÁSZAT}, volume = {3}, unique-id = {31665750}, issn = {2498-8057}, year = {2018}, pages = {42-47}, orcid-numbers = {Benkő, Sándor/0000-0002-9379-8503} } @article{MTMT:3200680, title = {Metabolic crosstalk between membrane and storage lipids facilitates heat stress management in Schizosaccharomyces pombe.}, url = {https://m2.mtmt.hu/api/publication/3200680}, author = {Péter, Mária and Glatz, Attila and Gudmann, Péter and Gombos, Imre and Török, Zsolt and Horváth, Ibolya and Vigh, László and Balogh, Gábor}, doi = {10.1371/journal.pone.0173739}, journal-iso = {PLOS ONE}, journal = {PLOS ONE}, volume = {12}, unique-id = {3200680}, issn = {1932-6203}, abstract = {Cell membranes actively participate in stress sensing and signalling. Here we present the first in-depth lipidomic analysis to characterize alterations in the fission yeast Schizosaccharomyces pombe in response to mild heat stress (HS). The lipidome was assessed by a simple one-step methanolic extraction. Genetic manipulations that altered triglyceride (TG) content in the absence or presence of HS gave rise to distinct lipidomic fingerprints for S. pombe. Cells unable to produce TG demonstrated long-lasting growth arrest and enhanced signalling lipid generation. Our results reveal that metabolic crosstalk between membrane and storage lipids facilitates homeostatic maintenance of the membrane physical/chemical state that resists negative effects on cell growth and viability in response to HS. We propose a novel stress adaptation mechanism in which heat-induced TG synthesis contributes to membrane rigidization by accommodating unsaturated fatty acids of structural lipids, enabling their replacement by newly synthesized saturated fatty acids.}, year = {2017}, eissn = {1932-6203} } @article{MTMT:2990307, title = {Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe.}, url = {https://m2.mtmt.hu/api/publication/2990307}, author = {Glatz, Attila and Pilbat, Ana Maria and Nemeth, GL and Kontár, Katalin and Jósvay, Katalin and Hunya, Ákos and Udvardy, Andor and Gombos, Imre and Péter, Mária and Balogh, Gábor and Horváth, Ibolya and Vigh, László and Török, Zsolt}, doi = {10.1007/s12192-015-0662-4}, journal-iso = {CELL STRESS CHAPERON}, journal = {CELL STRESS & CHAPERONES}, volume = {21}, unique-id = {2990307}, issn = {1355-8145}, abstract = {Changes in the levels of three structurally and functionally different important thermoprotectant molecules, namely small heat shock proteins (sHsps), trehalose, and lipids, have been investigated upon heat shock in Schizosaccharomyces pombe. Both alpha-crystallin-type sHsps (Hsp15.8 and Hsp16) were induced after prolonged high-temperature treatment but with different kinetic profiles. The shsp null mutants display a weak, but significant, heat sensitivity indicating their importance in the thermal stress management. The heat induction of sHsps is different in wild type and in highly heat-sensitive trehalose-deficient (tps1Delta) cells; however, trehalose level did not show significant alteration in shsp mutants. The altered timing of trehalose accumulation and induction of sHsps suggest that the disaccharide might provide protection at the early stage of the heat stress while elevated amount of sHsps are required at the later phase. The cellular lipid compositions of two different temperature-adapted wild-type S. pombe cells are also altered according to the rule of homeoviscous adaptation, indicating their crucial role in adapting to the environmental temperature changes. Both Hsp15.8 and Hsp16 are able to bind to different lipids isolated from S. pombe, whose interaction might provide a powerful protection against heat-induced damages of the membranes. Our data suggest that all the three investigated thermoprotectant macromolecules play a pivotal role during the thermal stress management in the fission yeast.}, year = {2016}, eissn = {1466-1268}, pages = {327-338}, orcid-numbers = {Hunya, Ákos/0000-0002-4547-9284} } @article{MTMT:2599676, title = {Plasma membranes as heat stress sensors: From lipid-controlled molecular switches to therapeutic applications}, url = {https://m2.mtmt.hu/api/publication/2599676}, author = {Török, Zsolt and Crul, Tim and Maresca, B and Schutz, GJ and Viana, F and Dindia, L and Piotto, S and Brameshuber, M and Balogh, Gábor and Péter, Mária and Porta, A and Trapani, A and Gombos, Imre and Glatz, Attila and Güngör, Burcin and Peksel, Begüm and Vígh, László Jr. and Csoboz, Bálint and Horváth, Ibolya and Vijayan, MM and Hooper, PL and Harwood, JL and Vigh, László}, doi = {10.1016/j.bbamem.2013.12.015}, journal-iso = {BBA-BIOMEMBRANES}, journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES}, volume = {1838}, unique-id = {2599676}, issn = {0005-2736}, abstract = {The classic heat shock (stress) response (HSR) Was originally attributed to protein denaturation. However, heat shock protein (Hsp) induction occurs in many circumstances where no protein denaturation is observed. Recently considerable evidence has been accumulated to the favor of the "Membrane Sensor Hypothesis" which predicts that the level of Hsps can be changed as a result of alterations to the plasma membrane. This is especially pertinent to mild heat shock, such as occurs in fever. In this condition the sensitivity of many transient receptor potential (TRP) channels is particularly notable. Small temperature stresses can modulate TRP gating significantly and this is influenced by lipids. In addition, stress hormones often modify plasma membrane structure and function and thus initiate a cascade of events, which may affect HSR. The major transactivator heat shock factor-1 integrates the signals originating from the plasma membrane and orchestrates the expression of individual heat shock genes. We describe how these observations can be tested at the molecular level, for example, with the use of membrane perturbers and through computational calculations. An important fact which now starts to be addressed is that membranes are not homogeneous nor do all cells react identically. Lipidomics and cell profiling are beginning to address the above two points. Finally, we observe that a deregulated HSR is found in a large number of important diseases Where more detailed knowledge of the molecular mechanisms involved may offer timely opportunities for clinical interventions and new, innovative drug treatments. This article is part of a Special Issue entitled: Membrane Structure and Function: Relevance in the Cell's Physiology, Pathology and Therapy. (C) 2013 The Authors. Published by Elsevier B.V. All rights reserved.}, year = {2014}, eissn = {1879-2642}, pages = {1594-1618}, orcid-numbers = {Crul, Tim/0000-0002-6053-7016} } @{MTMT:2500236, title = {Heat stress management in Synechocystis PCC 6803: the interplay between membranes and stress protein molecular chaperones}, url = {https://m2.mtmt.hu/api/publication/2500236}, author = {Glatz, Attila and Török, Zsolt and Vigh, László and Horváth, Ibolya}, booktitle = {Stress biology of Cyanobacteria}, doi = {10.1201/b13853}, unique-id = {2500236}, year = {2013}, pages = {145-153} } @article{MTMT:2372382, title = {Key role of lipids in heat stress management}, url = {https://m2.mtmt.hu/api/publication/2372382}, author = {Balogh, Gábor and Péter, Mária and Glatz, Attila and Gombos, Imre and Török, Zsolt and Horváth, Ibolya and Harwood, JL and Vigh, László}, doi = {10.1016/j.febslet.2013.05.016}, journal-iso = {FEBS LETT}, journal = {FEBS LETTERS}, volume = {587}, unique-id = {2372382}, issn = {0014-5793}, abstract = {Heat stress is a common and, therefore, an important environmental impact on cells and organisms. While much attention has been paid to severe heat stress, moderate temperature elevations are also important. Here we discuss temperature sensing and how responses to heat stress are not necessarily dependent on denatured proteins. Indeed, it is clear that membrane lipids have a pivotal function. Details of membrane lipid changes and the associated production of signalling metabolites are described and suggestions made as to how the interconnected signalling network could be modified for helpful intervention in disease. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.}, keywords = {PLASMA-MEMBRANE; ESCHERICHIA-COLI; CYTOCHROME-C; Heat stress; SACCHAROMYCES-CEREVISIAE; membrane lipid; ARACHIDONIC-ACID; Molecular Chaperones; Cellular networks; SHOCK TRANSCRIPTION FACTOR; THERMOSENSOR CONTROLS EXPRESSION; Signalling network; Membrane sensor; Temperature sensing; Mild heat exposure; Oxidative stress}, year = {2013}, eissn = {1873-3468}, pages = {1970-1980} } @article{MTMT:2096112, title = {Hydroximic Acid Derivatives: Pleiotropic Hsp Co-Inducers Restoring Homeostasis and Robustness}, url = {https://m2.mtmt.hu/api/publication/2096112}, author = {Crul, Tim and Crul-Tóth, Noémi and Piotto, S and Literáti-Nagy, Péter and Tory, K and Haldimann, P and Kalmar, B and Greensmith, L and Török, Zsolt and Balogh, Gábor and Gombos, Imre and Campana, F and Concilio, S and Gallyas, Ferenc and Nagy, G and Berente, Zoltán and Güngör, Burcin and Péter, Mária and Glatz, Attila and Hunya, Ákos and Literáti-Nagy, Zsuzsanna and Vígh, László Jr. and Hoogstra-Berends, F and Heeres, A and Kuipers, I and Loen, L and Seerden, JP and Zhang, D and Meijering, RA and Henning, RH and Brundel, BJ and Kampinga, HH and Korányi, László and Szilvássy, Zoltán and Mandl, József and Sümegi, Balázs and Febbraio, MA and Horváth, Ibolya and Hooper, PL and Vigh, László}, doi = {10.2174/1381612811306030309}, journal-iso = {CURR PHARM DESIGN}, journal = {CURRENT PHARMACEUTICAL DESIGN}, volume = {19}, unique-id = {2096112}, issn = {1381-6128}, abstract = {According to the "membrane sensor" hypothesis, the membranes physical properties and microdomain organization play an initiating role in the heat shock response. Clinical conditions such as cancer, diabetes and neurodegenerative diseases are all coupled with specific changes in the physical state and lipid composition of cellular membranes and characterized by altered heat shock protein levels in cells suggesting that these "membrane defects" can cause suboptimal hsp-gene expression. Such observations provide a new rationale for the introduction of novel, heat shock protein modulating drug candidates. Intercalating compounds can be used to alter membrane properties and by doing so normalize dysregulated expression of heat shock proteins, resulting in a beneficial therapeutic effect for reversing the pathological impact of disease. The membrane (and lipid) interacting hydroximic acid (HA) derivatives discussed in this review physiologically restore the heat shock protein stress response, creating a new class of "membrane-lipid therapy" pharmaceuticals. The diseases that HA derivatives potentially target are diverse and include, among others, insulin resistance and diabetes, neuropathy, atrial fibrillation, and amyotrophic lateral sclerosis. At a molecular level HA derivatives are broad spectrum, multi-target compounds as they fluidize yet stabilize membranes and remodel their lipid rafts while otherwise acting as PARP inhibitors. The HA derivatives have the potential to ameliorate disparate conditions, whether of acute or chronic nature. Many of these diseases presently are either untreatable or inadequately treated with currently available pharmaceuticals. Ultimately, the HA derivatives promise to play a major role in future pharmacotherapy.}, year = {2013}, eissn = {1873-4286}, pages = {309-346}, orcid-numbers = {Crul, Tim/0000-0002-6053-7016; Gallyas, Ferenc/0000-0002-1906-4333; Hunya, Ákos/0000-0002-4547-9284; Mandl, József/0000-0001-9172-7202} } @article{MTMT:1995801, title = {Heat shock response in photosynthetic organisms: Membrane and lipid connections}, url = {https://m2.mtmt.hu/api/publication/1995801}, author = {Horváth, Ibolya and Glatz, Attila and Nakamoto, H and Mishkind, M L and Munnik, T and Saidi, Y and Goloubinoff, P and Harwood, J L and Vigh, László}, doi = {10.1016/j.plipres.2012.02.002}, journal-iso = {PROG LIPID RES}, journal = {PROGRESS IN LIPID RESEARCH}, volume = {51}, unique-id = {1995801}, issn = {0163-7827}, abstract = {The ability of photosynthetic organisms to adapt to increases in environmental temperatures is becoming more important with climate change. Heat stress is known to induce heat-shock proteins (HSPs) many of which act as chaperones. Traditionally, it has been thought that protein denaturation acts as a trigger for HSP induction. However, increasing evidence has shown that many stress events cause HSP induction without commensurate protein denaturation. This has led to the membrane sensor hypothesis where the membrane's physical and structural properties play an initiating role in the heat shock response. In this review, we discuss heat-induced modulation of the membrane's physical state and changes to these properties which can be brought about by interaction with HSPs. Heat stress also leads to changes in lipid-based signaling cascades and alterations in calcium transport and availability. Such observations emphasize the importance of membranes and their lipids in the heat shock response and provide a new perspective for guiding further studies into the mechanisms that mediate cellular and organismal responses to heat stress. © 2012 Elsevier Ltd. All rights reserved.}, keywords = {heat shock response; Molecular Chaperones; Phosphatidic acid; Transient Ca; Small heat shock proteins; Signaling lipids; Phosphatidylinositol 4,5-bisphosphate; Membrane sensor hypothesis; Membrane fluidizer}, year = {2012}, eissn = {1873-2194}, pages = {208-220} }