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7 results on '"Fahrenkrog, B"'

1. Loss of histone H3 methylation at lysine 4 triggers apoptosis in Saccharomyces cerevisiae.

Author

Walter D, Matter A, and Fahrenkrog B

Subjects
Cell Survival genetics, DNA Damage genetics, Jumonji Domain-Containing Histone Demethylases genetics, Lysine genetics, Methylation, Saccharomyces cerevisiae, Ubiquitination genetics, Apoptosis genetics, Histone-Lysine N-Methyltransferase genetics, Histones genetics, Nuclear Proteins genetics, Saccharomyces cerevisiae Proteins genetics
Abstract

Monoubiquitination of histone H2B lysine 123 regulates methylation of histone H3 lysine 4 (H3K4) and 79 (H3K79) and the lack of H2B ubiquitination in Saccharomyces cerevisiae coincides with metacaspase-dependent apoptosis. Here, we discovered that loss of H3K4 methylation due to depletion of the methyltransferase Set1p (or the two COMPASS subunits Spp1p and Bre2p, respectively) leads to enhanced cell death during chronological aging and increased sensitivity to apoptosis induction. In contrast, loss of H3K79 methylation due to DOT1 disruption only slightly affects yeast survival. SET1 depleted cells accumulate DNA damage and co-disruption of Dot1p, the DNA damage adaptor protein Rad9p, the endonuclease Nuc1p, and the metacaspase Yca1p, respectively, impedes their early death. Furthermore, aged and dying wild-type cells lose H3K4 methylation, whereas depletion of the H3K4 demethylase Jhd2p improves survival, indicating that loss of H3K4 methylation is an important trigger for cell death in S. cerevisiae. Given the evolutionary conservation of H3K4 methylation this likely plays a role in apoptosis regulation in a wide range of organisms.

Published
2014
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2. Nuclear localisation is crucial for the proapoptotic activity of the HtrA-like serine protease Nma111p.

Author

Belanger KD, Walter D, Henderson TA, Yelton AL, O'Brien TG, Belanger KG, Geier SJ, and Fahrenkrog B

Subjects
Amino Acid Motifs, Cell Nucleus chemistry, Cell Nucleus genetics, Nuclear Localization Signals, Protein Transport, Saccharomyces cerevisiae chemistry, Saccharomyces cerevisiae cytology, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins genetics, Serine Endopeptidases genetics, Apoptosis, Cell Nucleus enzymology, Saccharomyces cerevisiae enzymology, Saccharomyces cerevisiae Proteins chemistry, Saccharomyces cerevisiae Proteins metabolism, Serine Endopeptidases chemistry, Serine Endopeptidases metabolism
Abstract

Programmed cell death is induced by the activation of a subset of intracellular proteins in response to specific extra- and intracellular signals. In the yeast Saccharomyces cerevisiae, Nma111p functions as a nuclear serine protease that is necessary for apoptosis under cellular stress conditions, such as elevated temperature or treatment of cells with hydrogen peroxide to induce cell death. We have examined the role of nuclear protein import in the function of Nma111p in apoptosis. Nma111p contains two small clusters of basic residues towards its N-terminus, both of which are necessary for efficient translocation into the nucleus. Nma111p does not shuttle between the nucleus and cytoplasm during either normal growth conditions or under environmental stresses that induce apoptosis. The N-terminal half of Nma111p is sufficient to provide the apoptosis-inducing activity of the protein, and the nuclear-localisation signal (NLS) sequences and catalytic serine 235 are both necessary for this function. We provide compelling evidence that intranuclear Nma111p activity is necessary for apoptosis in yeast.

Published
2009
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3. Negative regulation of apoptosis in yeast.

Author

Owsianowski E, Walter D, and Fahrenkrog B

Subjects
Adenosine Triphosphatases metabolism, Antioxidants metabolism, Cell Cycle Proteins metabolism, Fungal Proteins metabolism, Mitochondrial Proteins metabolism, Peptide Elongation Factor 2 metabolism, Reactive Oxygen Species metabolism, Saccharomyces cerevisiae cytology, Saccharomyces cerevisiae physiology, Saccharomyces cerevisiae Proteins metabolism, Schizosaccharomyces cytology, Schizosaccharomyces physiology, Valosin Containing Protein, Voltage-Dependent Anion Channels metabolism, Yeasts cytology, Apoptosis physiology, Apoptosis Regulatory Proteins metabolism, Yeasts physiology
Abstract

In recent years, yeast has been proven to be a useful model organism for studying programmed cell death. It not only exhibits characteristic markers of apoptotic cell death when heterologous inducers of apoptosis are expressed or when treated with apoptosis inducing drugs such as hydrogen peroxide (H(2)O(2)) or acetic acid, but contains homologues of several components of the apoptotic machinery identified in mammals, flies and nematodes, such as caspases, apoptosis inducing factor (AIF), Omi/HtrA2 and inhibitor-of-apoptosis proteins (IAPs). In this review, we focus on the role of negative regulators of apoptosis in yeasts. Bir1p is the only IAP protein in Saccharomyces cerevisiae and has long been known to play a role in cell cycle progression by acting as kinetochore and chromosomal passenger protein. Recent data established Bir1p's protective function against programmed cell death induced by H(2)O(2) treatment and in chronological ageing. Other factors that have a direct or indirect influence on intracellular levels of reactive oxygen species (ROS) and thus lead to apoptosis if they are misregulated or non-functional will be discussed.

Published
2008
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4. The inhibitor-of-apoptosis protein Bir1p protects against apoptosis in S. cerevisiae and is a substrate for the yeast homologue of Omi/HtrA2.

Author

Walter D, Wissing S, Madeo F, and Fahrenkrog B

Subjects
Aging physiology, Animals, Fungal Proteins genetics, High-Temperature Requirement A Serine Peptidase 2, Humans, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Saccharomyces cerevisiae ultrastructure, Saccharomyces cerevisiae Proteins genetics, Saccharomyces cerevisiae Proteins metabolism, Serine Endopeptidases genetics, Apoptosis physiology, Fungal Proteins metabolism, Mitochondrial Proteins metabolism, Saccharomyces cerevisiae physiology, Serine Endopeptidases metabolism
Abstract

Inhibitor-of-apoptosis proteins (IAPs) play a crucial role in the regulation of metazoan apoptosis. IAPs are typically characterized by the presence of one to three baculovirus IAP repeat (BIR) domains that are essential for their anti-apoptotic activity. Bir1p is the sole BIR-protein in yeast and has been shown to participate in chromosome segregation events. Here, we show that Bir1p is a substrate for Nma111p, which is the homologue of the human pro-apoptotic serine protease Omi/HtrA2 and which is known to mediate apoptosis in yeast. Bir1p is a cytoplasmic and nuclear protein, and yeast cells lacking bir1 are more sensitive to apoptosis induced by oxidative stress. Consistently, overexpression of Bir1p reduces apoptosis-like cell death, whereas this protective effect can be antagonized in vivo by simultaneous overexpression of Nma111p. Moreover, chronologically aged cells that constitutively overexpress Bir1p show a delayed onset of cell death. Therefore, Bir1p, like its closest metazoan homologues deterin and survivin, has dual functions: it participates in chromosome segregation events and cytokinesis and exhibits anti-apoptotic activity.

Published
2006
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5. The nuclear pore complex, nuclear transport, and apoptosis.

Author

Fahrenkrog B

Subjects
Active Transport, Cell Nucleus, Animals, Humans, Nuclear Pore Complex Proteins metabolism, Apoptosis, Nuclear Pore metabolism, Nuclear Proteins metabolism
Abstract

The nuclear pore complex (NPC) is the sole gateway between the nucleus and the cytoplasm of interphase eukaryotic cells, and it mediates all trafficking between these 2 cellular compartments. As such, the NPC and nuclear transport play central roles in translocating death signals from the cell membrane to the nucleus where they initiate biochemical and morphological changes occurring during apoptosis. Recent findings suggest that the correlation between the NPC, nuclear transport, and apoptosis goes beyond the simple fact that NPCs mediate nuclear transport of key players involved in the cell death program. In this context, the accessibility of key regulators of apoptosis appears to be highly modulated by nuclear transport (e.g., impaired nuclear import might be an apoptotic trigger). In this review, recent findings concerning the unexpected tight link between NPCs, nuclear transport, and apoptosis will be presented and critically discussed.

Published
2006
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6. The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine protease that mediates yeast apoptosis.

Author

Fahrenkrog B, Sauder U, and Aebi U

Subjects
Cell Nucleus metabolism, Cloning, Molecular, High-Temperature Requirement A Serine Peptidase 2, Microscopy, Electron, Microscopy, Fluorescence, Mitochondria metabolism, Mitochondrial Proteins, Mutation, Saccharomyces cerevisiae cytology, Saccharomyces cerevisiae physiology, X-Linked Inhibitor of Apoptosis Protein, Apoptosis physiology, Nuclear Proteins metabolism, Proteins metabolism, Saccharomyces cerevisiae Proteins metabolism, Serine Endopeptidases genetics, Serine Endopeptidases metabolism
Abstract

The yeast S. cerevisiae can undergo programmed cell death that exhibits the typical cellular markers of apoptosis. The mammalian HtrA2 protein was recently reported to mediate apoptosis in a serine-protease-dependent manner owing to its ability to antagonise the inhibitor of apoptosis protein XIAP. Here, we report the identification and characterisation of the S. cerevisiae HtrA-like protein, which we termed Nma111p (for nuclear mediator of apoptosis), as a mediator of yeast apoptosis. Nma111p is a nuclear protein that, under cellular stress conditions (i.e. at elevated temperature or after induction of apoptosis by H2O2), tends to aggregate inside the nucleus without its expression level being upregulated, suggesting that aggregation of Nma111p is correlated to its death-mediating character. Nma111p belongs to the HtrA family of serine proteases and its pro-apoptotic activity depends on its serine-protease activity. Yeast cells that lack Nma111p survive better at 50 degrees C than wild-type cells and the cells show no apoptotic hallmarks, such as chromatin condensation and fragmentation, or accumulation of reactive oxygen species, after the induction of apoptosis by H2O2. By contrast, overexpression of Nma111p enhances apoptotic-like cell death. Therefore, Nma111p, like its mammalian homologue HtrA2, mediates apoptosis.

Published
2004
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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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