TY - JOUR AU - Péter, Mária AU - Gudmann, Péter AU - Kóta, Zoltán AU - Török, Zsolt AU - Vigh, László AU - Glatz, Attila AU - Balogh, Gábor TI - Lipids and Trehalose Actively Cooperate in Heat Stress Management of Schizosaccharomyces pombe JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 22 PY - 2021 IS - 24 SN - 1661-6596 DO - 10.3390/ijms222413272 UR - https://m2.mtmt.hu/api/publication/32531214 ID - 32531214 N1 - Cited By :3 Export Date: 20 September 2022 LA - English DB - MTMT ER - TY - JOUR AU - Makarova, Maria AU - Péter, Mária AU - Balogh, Gábor AU - Glatz, Attila AU - MacRae, James I. AU - Lopez Mora, Nestor AU - Booth, Paula AU - Makeyev, Eugene AU - Vigh, László AU - Oliferenko, Snezhana TI - Delineating the Rules for Structural Adaptation of Membrane-Associated Proteins to Evolutionary Changes in Membrane Lipidome JF - CURRENT BIOLOGY J2 - CURR BIOL VL - 30 PY - 2020 IS - 3 SP - 367 EP - 380 PG - 14 SN - 0960-9822 DO - 10.1016/j.cub.2019.11.043 UR - https://m2.mtmt.hu/api/publication/31134487 ID - 31134487 N1 - Összes idézések száma a WoS-ban: 0 The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences, King's College London, Guy's Campus, London, SE1 1UL, United Kingdom Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged, 6726, Hungary Department of Chemistry, King's College London, Britannia House, London, SE1 1DB, United Kingdom MRC Centre for Developmental Neurobiology, King's College London, Guy's Campus, London, SE1 1UL, United Kingdom Cited By :1 Export Date: 3 April 2020 CODEN: CUBLE Correspondence Address: Oliferenko, S.; The Francis Crick Institute, 1 Midland Road, United Kingdom; email: snezhka.oliferenko@crick.ac.uk The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences, King's College London, Guy's Campus, London, SE1 1UL, United Kingdom Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged, 6726, Hungary Department of Chemistry, King's College London, Britannia House, London, SE1 1DB, United Kingdom MRC Centre for Developmental Neurobiology, King's College London, Guy's Campus, London, SE1 1UL, United Kingdom Cited By :1 Export Date: 4 April 2020 CODEN: CUBLE Correspondence Address: Oliferenko, S.; The Francis Crick Institute, 1 Midland Road, United Kingdom; email: snezhka.oliferenko@crick.ac.uk LA - English DB - MTMT ER - TY - JOUR AU - Benkő, Sándor AU - Balogh, Gábor AU - Péter, Mária AU - Török, Zsolt AU - Gombos, Imre AU - Glatz, Attila AU - Horváth, Ibolya AU - Vigh, László TI - Miért csillapított a stresszválasz az öregedés során, avagy a dajkafehérje expresszió és a membrán-fluiditás kapcsolata JF - IDŐSGYÓGYÁSZAT J2 - IDŐSGYÓGYÁSZAT VL - 3 PY - 2018 IS - 2 SP - 42 EP - 47 PG - 6 SN - 2498-8057 UR - https://m2.mtmt.hu/api/publication/31665750 ID - 31665750 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Péter, Mária AU - Glatz, Attila AU - Gudmann, Péter AU - Gombos, Imre AU - Török, Zsolt AU - Horváth, Ibolya AU - Vigh, László AU - Balogh, Gábor TI - Metabolic crosstalk between membrane and storage lipids facilitates heat stress management in Schizosaccharomyces pombe. JF - PLOS ONE J2 - PLOS ONE VL - 12 PY - 2017 IS - 3 PG - 22 SN - 1932-6203 DO - 10.1371/journal.pone.0173739 UR - https://m2.mtmt.hu/api/publication/3200680 ID - 3200680 N1 - Cited By :19 Export Date: 27 May 2021 CODEN: POLNC AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Glatz, Attila AU - Pilbat, Ana Maria AU - Nemeth, GL AU - Kontár, Katalin AU - Jósvay, Katalin AU - Hunya, Ákos AU - Udvardy, Andor AU - Gombos, Imre AU - Péter, Mária AU - Balogh, Gábor AU - Horváth, Ibolya AU - Vigh, László AU - Török, Zsolt TI - Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe. JF - CELL STRESS & CHAPERONES J2 - CELL STRESS CHAPERON VL - 21 PY - 2016 IS - 2 SP - 327 EP - 338 PG - 12 SN - 1355-8145 DO - 10.1007/s12192-015-0662-4 UR - https://m2.mtmt.hu/api/publication/2990307 ID - 2990307 N1 - Export Date: 20 June 2019 CODEN: CSCHF Cited By :24 Export Date: 27 May 2021 CODEN: CSCHF Correspondence Address: Török, Z.; Institute of Biochemistry, Hungary; email: torok.zsolt@brc.mta.hu AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Török, Zsolt AU - Crul, Tim AU - Maresca, B AU - Schutz, GJ AU - Viana, F AU - Dindia, L AU - Piotto, S AU - Brameshuber, M AU - Balogh, Gábor AU - Péter, Mária AU - Porta, A AU - Trapani, A AU - Gombos, Imre AU - Glatz, Attila AU - Güngör, Burcin AU - Peksel, Begüm AU - Vígh, László Jr. AU - Csoboz, Bálint AU - Horváth, Ibolya AU - Vijayan, MM AU - Hooper, PL AU - Harwood, JL AU - Vigh, László TI - Plasma membranes as heat stress sensors: From lipid-controlled molecular switches to therapeutic applications JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES J2 - BBA-BIOMEMBRANES VL - 1838 PY - 2014 IS - 6 SP - 1594 EP - 1618 PG - 25 SN - 0005-2736 DO - 10.1016/j.bbamem.2013.12.015 UR - https://m2.mtmt.hu/api/publication/2599676 ID - 2599676 N1 - Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Temesvari krt. 62, 6726-Szeged, Hungary Department of Pharmacy, University of Salerno, Via Giovanni Paolo II, 132, 84084 Fisciano, Salerno, Italy Institute of Applied Physics, Vienna University of Technology, Wiedner Hauptstrasse 8-10, 1040 Vienna, Austria Instituto de Neurociencias de Alicante, Universidad Miguel Hernández-CSIC, 03550 San Juan de Alicante, Spain Department of Biology, University of Waterloo, Waterloo, ON, Canada Department of Biological Sciences, University of Calgary, Calgary, AB, Canada Department of Medicine, University of Colorado Medical School, Anschutz Medical Campus, Aurora, CO 80045, United States School of Biosciences, Cardiff University, Cardiff CF10 3AX, United Kingdom Cited By :78 Export Date: 26 May 2022 CODEN: BBBMB Correspondence Address: Török, Z.; Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Temesvari krt. 62, 6726-Szeged, Hungary; email: tzsolt@brc.hu AB - 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. LA - English DB - MTMT ER - TY - CHAP AU - Glatz, Attila AU - Török, Zsolt AU - Vigh, László AU - Horváth, Ibolya ED - Srivastava, AK ED - Rai, AN ED - Neilan, BA TI - Heat stress management in Synechocystis PCC 6803: the interplay between membranes and stress protein molecular chaperones T2 - Stress biology of Cyanobacteria PB - CRC Press CY - Boca Raton, Florida SN - 9781466504783 PY - 2013 SP - 145 EP - 153 PG - 9 DO - 10.1201/b13853 UR - https://m2.mtmt.hu/api/publication/2500236 ID - 2500236 N1 - Export Date: 23 September 2019 Correspondence Address: Glatz, A.; Institute of Biochemistry, Biological Research Centre, Hungarian Academy of SciencesHungary; email: attila@brc.hu Export Date: 24 September 2019 Correspondence Address: Glatz, A.; Institute of Biochemistry, Biological Research Centre, Hungarian Academy of SciencesHungary; email: attila@brc.hu Export Date: 26 September 2019 Correspondence Address: Glatz, A.; Institute of Biochemistry, Biological Research Centre, Hungarian Academy of SciencesHungary; email: attila@brc.hu Export Date: 27 September 2019 Correspondence Address: Glatz, A.; Institute of Biochemistry, Biological Research Centre, Hungarian Academy of SciencesHungary; email: attila@brc.hu Export Date: 1 April 2020 Correspondence Address: Glatz, A.; Institute of Biochemistry, Biological Research Centre, Hungarian Academy of SciencesHungary; email: attila@brc.hu Export Date: 2 April 2020 Correspondence Address: Glatz, A.; Institute of Biochemistry, Biological Research Centre, Hungarian Academy of SciencesHungary; email: attila@brc.hu Export Date: 13 January 2021 Correspondence Address: Glatz, A.; Institute of Biochemistry, Biological Research Centre, Hungarian Academy of SciencesHungary; email: attila@brc.hu Export Date: 14 January 2021 Correspondence Address: Glatz, A.; Institute of Biochemistry, Biological Research Centre, Hungarian Academy of SciencesHungary; email: attila@brc.hu LA - English DB - MTMT ER - TY - JOUR AU - Balogh, Gábor AU - Péter, Mária AU - Glatz, Attila AU - Gombos, Imre AU - Török, Zsolt AU - Horváth, Ibolya AU - Harwood, JL AU - Vigh, László TI - Key role of lipids in heat stress management JF - FEBS LETTERS J2 - FEBS LETT VL - 587 PY - 2013 IS - 13 SP - 1970 EP - 1980 PG - 11 SN - 0014-5793 DO - 10.1016/j.febslet.2013.05.016 UR - https://m2.mtmt.hu/api/publication/2372382 ID - 2372382 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Crul, Tim AU - Crul-Tóth, Noémi AU - Piotto, S AU - Literáti-Nagy, Péter AU - Tory, K AU - Haldimann, P AU - Kalmar, B AU - Greensmith, L AU - Török, Zsolt AU - Balogh, Gábor AU - Gombos, Imre AU - Campana, F AU - Concilio, S AU - Gallyas, Ferenc AU - Nagy, G AU - Berente, Zoltán AU - Güngör, Burcin AU - Péter, Mária AU - Glatz, Attila AU - Hunya, Ákos AU - Literáti-Nagy, Zsuzsanna AU - Vígh, László Jr. AU - Hoogstra-Berends, F AU - Heeres, A AU - Kuipers, I AU - Loen, L AU - Seerden, JP AU - Zhang, D AU - Meijering, RA AU - Henning, RH AU - Brundel, BJ AU - Kampinga, HH AU - Korányi, László AU - Szilvássy, Zoltán AU - Mandl, József AU - Sümegi, Balázs AU - Febbraio, MA AU - Horváth, Ibolya AU - Hooper, PL AU - Vigh, László TI - Hydroximic Acid Derivatives: Pleiotropic Hsp Co-Inducers Restoring Homeostasis and Robustness JF - CURRENT PHARMACEUTICAL DESIGN J2 - CURR PHARM DESIGN VL - 19 PY - 2013 IS - 3 SP - 309 EP - 346 PG - 38 SN - 1381-6128 DO - 10.2174/1381612811306030309 UR - https://m2.mtmt.hu/api/publication/2096112 ID - 2096112 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Horváth, Ibolya AU - Glatz, Attila AU - Nakamoto, H AU - Mishkind, M L AU - Munnik, T AU - Saidi, Y AU - Goloubinoff, P AU - Harwood, J L AU - Vigh, László TI - Heat shock response in photosynthetic organisms: Membrane and lipid connections JF - PROGRESS IN LIPID RESEARCH J2 - PROG LIPID RES VL - 51 PY - 2012 IS - 3 SP - 208 EP - 220 PG - 13 SN - 0163-7827 DO - 10.1016/j.plipres.2012.02.002 UR - https://m2.mtmt.hu/api/publication/1995801 ID - 1995801 AB - 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. LA - English DB - MTMT ER -