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7 results on '"Giannattasio S"'

1. Proteome and metabolome profiling of wild-type and YCA1-knock-out yeast cells during acetic acid-induced programmed cell death.

Author

Longo V, Ždralević M, Guaragnella N, Giannattasio S, Zolla L, and Timperio AM

Subjects
Cellular Senescence drug effects, Gene Knockout Techniques, Metabolome drug effects, Metabolome physiology, Saccharomyces cerevisiae cytology, Saccharomyces cerevisiae drug effects, Acetic Acid administration & dosage, Caspases metabolism, Cellular Senescence physiology, Proteome metabolism, Saccharomyces cerevisiae physiology, Saccharomyces cerevisiae Proteins metabolism
Abstract

Unlabelled: Caspase proteases are responsible for the regulated disassembly of the cell into apoptotic bodies during mammalian apoptosis. Structural homologues of the caspase family (called metacaspases) are involved in programmed cell death in single-cell eukaryotes, yet the molecular mechanisms that contribute to death are currently undefined. Recent evidence revealed that a programmed cell death process is induced by acetic acid (AA-PCD) in Saccharomyces cerevisiae both in the presence and absence of metacaspase encoding gene YCA1. Here, we report an unexpected role for the yeast metacaspase in protein quality and metabolite control. By using an "omics" approach, we focused our attention on proteins and metabolites differentially modulated en route to AA-PCD either in wild type or YCA1-lacking cells. Quantitative proteomic and metabolomic analyses of wild type and Δyca1 cells identified significant alterations in carbohydrate catabolism, lipid metabolism, proteolysis and stress-response, highlighting the main roles of metacaspase in AA-PCD. Finally, deletion of YCA1 led to AA-PCD pathway through the activation of ceramides, whereas in the presence of the gene yeast cells underwent an AA-PCD pathway characterized by the shift of the main glycolytic pathway to the pentose phosphate pathway and a proteolytic mechanism to cope with oxidative stress., Significance: The yeast metacaspase regulates both proteolytic activities through the ubiquitin-proteasome system and ceramide metabolism as revealed by proteome and metabolome profiling of YCA1-knock-out cells during acetic-acid induced programmed cell death., (Copyright © 2015 Elsevier B.V. All rights reserved.)

Published
2015
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2. Differential proteome-metabolome profiling of YCA1-knock-out and wild type cells reveals novel metabolic pathways and cellular processes dependent on the yeast metacaspase.

Author

Ždralević M, Longo V, Guaragnella N, Giannattasio S, Timperio AM, and Zolla L

Subjects
Caspases metabolism, Gene Knockout Techniques, Metabolomics, Protein Interaction Maps genetics, Proteome analysis, Proteomics, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins metabolism, Caspases genetics, Metabolome genetics, Proteome genetics, Proteome metabolism, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins genetics
Abstract

The yeast Saccharomyces cerevisiae expresses one member of the metacaspase Cys protease family, encoded by the YCA1 gene. Combination of proteomics and metabolomics data showed that YCA1 deletion down-regulated glycolysis, the TCA cycle and alcoholic fermentation as compared with WT cells. Δyca1 cells also showed a down-regulation of the pentose phosphate pathway and accumulation of pyruvate, correlated with higher levels of certain amino acids found in these cells. Accordingly, there is a decrease in protein biosynthesis, and up-regulation of specific stress response proteins like Ahp1p, which possibly provides these cells with a better protection against stress. Moreover, in agreement with the down-regulation of protein biosynthesis machinery in Δyca1 cells, we have found that regulation of transcription, co-translational protein folding and protein targeting to different subcellular locations were also down-regulated. Metabolomics analysis of the nucleotide content showed a significant reduction in Δyca1 cells in comparison with the WT, except for GTP content which remained unchanged. Thus, our combined proteome-metabolome approach added a new dimension to the non-apoptotic function of yeast metacaspase, which can specifically affect cell metabolism through as yet unknown mechanisms and possibly stress-response pathways, like HOG and cell wall integrity pathways. Certainly, YCA1 deletion may induce compensatory changes in stress response proteins offering a better protection against apoptosis to Δyca1 cells rather than a loss in pro-apoptotic YCA1-associated activity.

Published
2015
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3. The N-acetylcysteine-insensitive acetic acid-induced yeast programmed cell death occurs without macroautophagy.

Author

Antonacci L, Guaragnella N, Ždralevic M, Passarella S, Marra E, and Giannattasio S

Subjects
Acetylcysteine pharmacology, Alkaline Phosphatase metabolism, Antioxidants pharmacology, Caspases genetics, Cytochromes c genetics, In Situ Nick-End Labeling, Saccharomyces cerevisiae drug effects, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins genetics, Acetic Acid pharmacology, Caspases metabolism, Cytochromes c metabolism, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins metabolism
Abstract

Programmed cell death can occur through two separate pathways caused by treatment of Saccharomyces cerevisiae with acetic acid (AA-PCD), which differ from one another essentially with respect to their sensitivity to N-acetylcysteine (NAC) and to the role played by cytochrome c and metacaspase YCA1. Moreover, yeast can also undergo macroautophagy which occurs in NAC-insensitive manner. In order to gain some insight into the relationship between AA-PCD and macroautophagy use was made of WT and knock-out cells lacking YCA1 and/or cytochrome c. We show that i. macroautophagy is modulated by YCA1 and by cytochrome c in a negative and positive manner, respectively, ii. the NAC-insensitive AA-PCD and macroautophagy differ from one another and iii. NAC-insensitive AA-PCD pathway takes place essentially without macroautophagy, even if the shift of extracellular pH to acidic values required for AA-PCD to occur leads itself to increased or decreased macroautophagy in YCA1 or cytochrome c-lacking cells.

Published
2012
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4. Yeast acetic acid-induced programmed cell death can occur without cytochrome c release which requires metacaspase YCA1.

Author

Guaragnella N, Bobba A, Passarella S, Marra E, and Giannattasio S

Subjects
Acetic Acid pharmacology, Caspases genetics, Cytochromes c genetics, Hydrogen Peroxide metabolism, Saccharomyces cerevisiae drug effects, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins genetics, Apoptosis, Caspases metabolism, Cytochromes c metabolism, Saccharomyces cerevisiae enzymology, Saccharomyces cerevisiae Proteins metabolism
Abstract

To investigate the role of cytochrome c (cyt c) release in yeast acetic acid-induced programmed cell death (AA-PCD), wild type (wt) and cells lacking metacaspase (Deltayca1), cytochrome c (Deltacyc1,7) and both (Deltacyc1,7Deltayca1) were compared for AA-PCD occurrence, hydrogen peroxide (H(2)O(2)) production and caspase activity. AA-PCD occurs in Deltacyc1,7 and Deltacyc1,7Deltayca1 cells slower than in wt, but similar to that in Deltayca1 cells, in which no cytochrome c release occurs. Both H(2)O(2) production and caspase activation occur in these cells with early and extra-activation in Deltacyc1,7 cells. We conclude that alternative death pathways can be activated in yeast AA-PCD, one dependent on cyt c release, which requires YCA1, and the other(s) independent on it.

Published
2010
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5. YCA1 participates in the acetic acid induced yeast programmed cell death also in a manner unrelated to its caspase-like activity.

Author

Guaragnella N, Pereira C, Sousa MJ, Antonacci L, Passarella S, Côrte-Real M, Marra E, and Giannattasio S

Subjects
Amino Acid Chloromethyl Ketones pharmacology, Caspases deficiency, Caspases genetics, Gene Deletion, Saccharomyces cerevisiae drug effects, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins genetics, Acetic Acid pharmacology, Apoptosis drug effects, Caspases metabolism, Saccharomyces cerevisiae cytology, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins metabolism
Abstract

Yeast cells lacking the metacaspase-encoding gene YCA1 (Deltayca1) were compared with wild-type (WT) cells with respect to the occurrence, nature and time course of acetic-acid triggered death. We show that Deltayca1 cells undergo programmed cell death (PCD) with a rate lower than that of the WT and that PCD in WT cells is caused at least in part by the caspase activity of Yca1p. Since in Deltayca1 cells this effect is lost, but z-VAD-fmk does not prevent both WT and Deltayca1 cell death, PCD in WT cells occurs via a Yca1p caspase and a non-caspase route with similar characteristics.

Published
2006
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6. Early release and subsequent caspase-mediated degradation of cytochrome c in apoptotic cerebellar granule cells.

Author

Bobba A, Atlante A, Giannattasio S, Sgaramella G, Calissano P, and Marra E

Subjects
Adenylate Kinase metabolism, Amino Acid Chloromethyl Ketones pharmacology, Animals, Apoptosis drug effects, Cells, Cultured, Cysteine Proteinase Inhibitors pharmacology, Cytosol metabolism, Glutamate Dehydrogenase metabolism, Immunoblotting, Mitochondria metabolism, Oxygen Consumption, Polarography, Rats, Time Factors, Apoptosis physiology, Caspases metabolism, Cerebellum metabolism, Cytochrome c Group metabolism
Abstract

Cytochrome c (cyt c) release was investigated in cerebellar granule cells used as an in vitro neuronal model of apoptosis. We have found that cyt c is released into the cytoplasm as an intact, functionally active protein, that this event occurs early, in the commitment phase of the apoptotic process, and that after accumulation, this protein is progressively degraded. Degradation, but not release, is fully blocked by benzyloxycarbonyl-Val-Ala-Asp-fluoromethylchetone (z-VAD-fmk). On the basis of previous findings obtained in the same neuronal population undergoing excitotoxic death, it is hypothesized that release of cyt c may be part of a cellular attempt to maintain production of ATP via cytochrome oxidase, which is reduced by cytosolic NADH in a cytochrome b5-soluble cyt c-mediated fashion.

Published
1999
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7. Guidelines and recommendations on yeast cell death nomenclature

Author

Cornelia Sommer-Ruck, Michel Mb Toledano, Guido Kroemer, María Segovia, Christa Meisinger, Jens Nielsen, Stéphane Picot, Campbell W. Gourlay, Antonio Jiménez-Ruiz, Raffael Schaffrath, Manuela Côrte-Real, Richard Y. Zhao, Didac Carmona-Gutierrez, Frank Madeo, Zhaojie J Zhang, Maria A. Bauer, F-Nora Vögtle, Andrés Aguilera, Ali Gargouri, Kathryn R. Ayscough, Nicolas Fasel, Paula Ludovico, Maria João Sousa, Patrick Rockenfeller, Stéphen Manon, Johannes M. Herrmann, Dina Petranovic, Vítor Costa, Lorenzo Galluzzi, Nicoletta Guaragnella, Benedikt Westermann, Marc Blondel, Christophe Cullin, Lynn La Megeney, William Wc Burhans, Michael Breitenbach, Peter Polčic, Jürgen J. Heinisch, Thomas Heger, Katrina Kf Cooper, Tiago Tf Outeiro, Birthe Fahrenkrog, Stephan J. Sigrist, Antonio Barrientos, Andreas Zimmermann, Michael Chang, Paola Goffrini, Michael Mt Greenwood, Amir Sharon, Bing Zhou, Shoshana Bar-Nun, Sabrina Büttner, Ian W. Dawes, Rena Balzan, Karin Thevissen, Duccio Cavalieri, Eva Herker, Joris Winderickx, Tobias Eisenberg, Nicanor Austriaco, Ted Powers, Tobias Pendl, Kai-Uwe Fröhlich, Vladimir I. Titorenko, Stefan Wölfl, Martin Mb Dickman, Sebastian J. Hofer, Thomas Nyström, Sergio Giannattasio, Cristina Mazzoni, Johan Jm Thevelein, Silke Wissing, Mick F. Tuite, Peter Belenky, Heinz Hd Osiewacz, Mark Rinnerthaler, Helmut Jungwirth, Christoph Ruckenstuhl, Fedor Ff Severin, Mark Ramsdale, Enzo Martegani, Chris M. Grant, Dimitrios P. Kontoyiannis, Jörn Dengjel, Hay-Oak Park, Ralf J. Braun, Katharina Kainz, NOVA Medical School|Faculdade de Ciências Médicas (NMS|FCM), Centro de Estudos de Doenças Crónicas (CEDOC), Universidade do Minho, Chimie et Biologie des Membranes et des Nanoobjets (CBMN), Université Sciences et Technologies - Bordeaux 1-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Centre National de la Recherche Scientifique (CNRS), Institute of Molecular Biosciences, Karl-Franzens University Graz, (IMB), Karl-Franzens-Universität Graz, Department of Biochemistry - George S. Wise Faculty of Life Sciences, Tel Aviv University (TAU), Universidad Politécnica de Madrid (UPM), Molécules et cibles thérapeutiques (MCT), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), BayerCropScience AG, Università degli Studi di Firenze = University of Florence (UniFI), Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Landesbetrieb Hessisches Landeslabor, Centre de Biotechnologie de Sfax (CBS), Institute of Biomembranes and Bioenergetics, CNR - Bari, Heinrich Pette Institute [Hamburg], Institut für Molekulare Biowissenschaften [Graz], University of Texas Health Science Center, The University of Texas Health Science Center at Houston (UTHealth), School of Health Sciences, University of Minho [Braga], Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Department of Biology and Biotechnology 'Charles Darwin', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome] (UNIROMA), Institute of Molecular Medicine and Cell Research (ZBMZ), University of Freiburg [Freiburg], Systems Biology, Chalmers University of Technology [Göteborg], Radicaux Libres, Substrats Énergétiques et Physiopathologie Cérébrale, Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Synthèse de Molécules d'Intérêt Thérapeutique (SMITh), Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université de Lyon-Université de Lyon-École Supérieure de Chimie Physique Électronique de Lyon (CPE)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Universität Kassel [Kassel], Department of Cellular Machines, BioTechnological Center, Technische Universität Dresden = Dresden University of Technology (TU Dresden), Department of Molecular Microbiology and Biotechnology, Charité - UniversitätsMedizin = Charité - University Hospital [Berlin], Center of Microbial and Plant Genetics (CMPG), Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), Concordia University [Montreal], Commissariat à l'énergie atomique et aux énergies alternatives (CEA), University of Kent [Canterbury], Q2S [NTNU], Norwegian University of Science and Technology [Trondheim] (NTNU), Norwegian University of Science and Technology (NTNU)-Norwegian University of Science and Technology (NTNU)-The Research Council of Norway, Functional Biology, School of Life Sciences, Peking- Tsinghua Center for Life Sciences, Apoptose, cancer et immunité (U848), Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Institut National de la Santé et de la Recherche Médicale (INSERM), Plateforme de métabolomique, Direction de la recherche [Gustave Roussy], Institut Gustave Roussy (IGR)-Institut Gustave Roussy (IGR), Immunopathologie et immunointervention thérapeutique (CRC - Inserm U1138), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Tel Aviv University [Tel Aviv], Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff (SBR), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Firenze [Firenze], Department of Biology and Biotechnologies 'Charles Darwin', Università degli Studi di Roma 'La Sapienza' [Rome]-Réseau International des Instituts Pasteur (RIIP)-Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP), Albert-Ludwigs University, Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Centre National de la Recherche Scientifique (CNRS), Charité - Universitätsmedizin Berlin / Charite - University Medicine Berlin, Norwegian University of Science and Technology [Trondheim] (NTNU)-The Research Council of Norway, École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Università degli Studi di Firenze = University of Florence [Firenze] (UNIFI), École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-École pratique des hautes études (EPHE), Carmona-Gutierrez, D, Bauer, M, Zimmermann, A, Aguilera, A, Austriaco, N, Ayscough, K, Balzan, R, Bar-Nun, S, Barrientos, A, Belenky, P, Blondel, M, Braun, R, Breitenbach, M, Burhans, W, Buettner, S, Cavalieri, D, Chang, M, Cooper, K, Côrte-Real, M, Costa, V, Cullin, C, Dawes, I, Dengjel, J, Dickman, M, Eisenberg, T, Fahrenkrog, B, Fasel, N, Froehlich, K, Gargouri, A, Giannattasio, S, Goffrini, P, Gourlay, C, Grant, C, Greenwood, M, Guaragnella, N, Heger, T, Heinisch, J, Herker, E, Herrmann, J, Hofer, S, Jiménez-Ruiz, A, Jungwirth, H, Kainz, K, Kontoyiannis, D, Ludovico, P, Manon, S, Martegani, E, Mazzoni, C, Megeney, L, Meisinger, C, Nielsen, J, Nystroem, T, Osiewacz, H, Outeiro, T, Park, H, Pendl, T, Petranovic, D, Picot, S, Polčic, P, Powers, T, Ramsdale, M, Rinnerthaler, M, Rockenfeller, P, Ruckenstuhl, C, Schaffrath, R, Segovia, M, Severin, F, Sharon, A, Sigrist, S, Sommer-Ruck, C, Sousa, M, Thevelein, J, Thevissen, K, Titorenko, V, Toledano, M, Tuite, M, Voegtle, F, Westermann, B, Winderickx, J, Wissing, S, Woelfl, S, Zhang, Z, Zhao, R, Zhou, B, Galluzzi, L, Kroemer, G, and Madeo, F

Subjects
0301 basic medicine, Applied Microbiology, [SDV]Life Sciences [q-bio], ved/biology.organism_classification_rank.species, Mitochondrial membrane permeabilization, Regulated cell death, Apoptosis, Review, mitochondrial membrane permeabilization, Applied Microbiology and Biotechnology, necrosis, Immunology and Microbiology (miscellaneous), lcsh:QH301-705.5, ComputingMilieux_MISCELLANEOUS, reactive oxygen species, biology, Model organism, apoptosis, regulated cell death, [CHIM.MATE]Chemical Sciences/Material chemistry, Sciences bio-médicales et agricoles, accidental cell death, Necrosi, 3. Good health, caspases, autophagic cell death, Caspases, Reactive oxygen specie, Saccharomyces cerevisiae, Programmed cell death, autophagy, caspase, mitotic catastrophe, model organism, Regulated necrosis, Computational biology, Microbiology, Biochemistry, Genetics and Molecular Biology (miscellaneous), 03 medical and health sciences, Necrosis, Accidental cell death, Virology, Genetics, Journal Article, Autophagy, Molecular Biology, Science & Technology, ved/biology, Apoptosi, Cell Biology, biology.organism_classification, Yeast, Mitotic catastrophe, 030104 developmental biology, Autophagic cell death, lcsh:Biology (General), Parasitology, Guidelines, yeast, cell death, Reactive oxygen species
Abstract

Elucidating the biology of yeast in its full complexity has major implications for science, medicine and industry. One of the most critical processes determining yeast life and physiology is cel-lular demise. However, the investigation of yeast cell death is a relatively young field, and a widely accepted set of concepts and terms is still missing. Here, we propose unified criteria for the defi-nition of accidental, regulated, and programmed forms of cell death in yeast based on a series of morphological and biochemical criteria. Specifically, we provide consensus guidelines on the differ-ential definition of terms including apoptosis, regulated necrosis, and autophagic cell death, as we refer to additional cell death rou-tines that are relevant for the biology of (at least some species of) yeast. As this area of investigation advances rapidly, changes and extensions to this set of recommendations will be implemented in the years to come. Nonetheless, we strongly encourage the au-thors, reviewers and editors of scientific articles to adopt these collective standards in order to establish an accurate framework for yeast cell death research and, ultimately, to accelerate the pro-gress of this vibrant field of research., info:eu-repo/semantics/published

Published
2018
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