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227 results on '"Dixon, Scott J."'

1. Integrated molecular and functional characterization of the intrinsic apoptotic machinery identifies therapeutic vulnerabilities in glioma

Author

Fernandez, Elizabeth G., Mai, Wilson X., Song, Kai, Bayley, Nicholas A., Kim, Jiyoon, Zhu, Henan, Pioso, Marissa, Young, Pauline, Andrasz, Cassidy L., Cadet, Dimitri, Liau, Linda M., Li, Gang, Yong, William H., Rodriguez, Fausto J., Dixon, Scott J., Souers, Andrew J., Li, Jingyi Jessica, Graeber, Thomas G., Cloughesy, Timothy F., and Nathanson, David A.

Published
2024
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5. Apoptotic cell death in disease—Current understanding of the NCCD 2023

Author

Vitale, Ilio, Pietrocola, Federico, Guilbaud, Emma, Aaronson, Stuart A, Abrams, John M, Adam, Dieter, Agostini, Massimiliano, Agostinis, Patrizia, Alnemri, Emad S, Altucci, Lucia, Amelio, Ivano, Andrews, David W, Aqeilan, Rami I, Arama, Eli, Baehrecke, Eric H, Balachandran, Siddharth, Bano, Daniele, Barlev, Nickolai A, Bartek, Jiri, Bazan, Nicolas G, Becker, Christoph, Bernassola, Francesca, Bertrand, Mathieu JM, Bianchi, Marco E, Blagosklonny, Mikhail V, Blander, J Magarian, Blandino, Giovanni, Blomgren, Klas, Borner, Christoph, Bortner, Carl D, Bove, Pierluigi, Boya, Patricia, Brenner, Catherine, Broz, Petr, Brunner, Thomas, Damgaard, Rune Busk, Calin, George A, Campanella, Michelangelo, Candi, Eleonora, Carbone, Michele, Carmona-Gutierrez, Didac, Cecconi, Francesco, Chan, Francis K-M, Chen, Guo-Qiang, Chen, Quan, Chen, Youhai H, Cheng, Emily H, Chipuk, Jerry E, Cidlowski, John A, Ciechanover, Aaron, Ciliberto, Gennaro, Conrad, Marcus, Cubillos-Ruiz, Juan R, Czabotar, Peter E, D’Angiolella, Vincenzo, Daugaard, Mads, Dawson, Ted M, Dawson, Valina L, De Maria, Ruggero, De Strooper, Bart, Debatin, Klaus-Michael, Deberardinis, Ralph J, Degterev, Alexei, Del Sal, Giannino, Deshmukh, Mohanish, Di Virgilio, Francesco, Diederich, Marc, Dixon, Scott J, Dynlacht, Brian D, El-Deiry, Wafik S, Elrod, John W, Engeland, Kurt, Fimia, Gian Maria, Galassi, Claudia, Ganini, Carlo, Garcia-Saez, Ana J, Garg, Abhishek D, Garrido, Carmen, Gavathiotis, Evripidis, Gerlic, Motti, Ghosh, Sourav, Green, Douglas R, Greene, Lloyd A, Gronemeyer, Hinrich, Häcker, Georg, Hajnóczky, György, Hardwick, J Marie, Haupt, Ygal, He, Sudan, Heery, David M, Hengartner, Michael O, Hetz, Claudio, Hildeman, David A, Ichijo, Hidenori, Inoue, Satoshi, Jäättelä, Marja, Janic, Ana, Joseph, Bertrand, Jost, Philipp J, and Kanneganti, Thirumala-Devi

Subjects
Biochemistry and Cell Biology, Biological Sciences, 1.1 Normal biological development and functioning, 2.1 Biological and endogenous factors, Generic health relevance, Good Health and Well Being, Animals, Humans, Apoptosis, Cell Death, Caspases, Carcinogenesis, Mammals, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Health sciences
Abstract

Apoptosis is a form of regulated cell death (RCD) that involves proteases of the caspase family. Pharmacological and genetic strategies that experimentally inhibit or delay apoptosis in mammalian systems have elucidated the key contribution of this process not only to (post-)embryonic development and adult tissue homeostasis, but also to the etiology of multiple human disorders. Consistent with this notion, while defects in the molecular machinery for apoptotic cell death impair organismal development and promote oncogenesis, the unwarranted activation of apoptosis promotes cell loss and tissue damage in the context of various neurological, cardiovascular, renal, hepatic, infectious, neoplastic and inflammatory conditions. Here, the Nomenclature Committee on Cell Death (NCCD) gathered to critically summarize an abundant pre-clinical literature mechanistically linking the core apoptotic apparatus to organismal homeostasis in the context of disease.

Published
2023

6. Oxaliplatin disrupts nucleolar function through biophysical disintegration

Author

Schmidt, H Broder, Jaafar, Zane A, Wulff, B Erik, Rodencal, Jason J, Hong, Kibeom, Aziz-Zanjani, Mohammad O, Jackson, Peter K, Leonetti, Manuel D, Dixon, Scott J, Rohatgi, Rajat, and Brandman, Onn

Subjects
Biochemistry and Cell Biology, Biological Sciences, Genetics, Digestive Diseases, Women's Health, Cancer, Colo-Rectal Cancer, 5.1 Pharmaceuticals, Oxaliplatin, Platinum, Cell Nucleolus, Antineoplastic Agents, RNA Polymerase I, CP: Cancer, colorectal cancer, drug mechanism, nucleolus, phase separation, transcription/ translation inhibitors, Medical Physiology, Biological sciences
Abstract

Platinum (Pt) compounds such as oxaliplatin are among the most commonly prescribed anti-cancer drugs. Despite their considerable clinical impact, the molecular basis of platinum cytotoxicity and cancer specificity remain unclear. Here we show that oxaliplatin, a backbone for the treatment of colorectal cancer, causes liquid-liquid demixing of nucleoli at clinically relevant concentrations. Our data suggest that this biophysical defect leads to cell-cycle arrest, shutdown of Pol I-mediated transcription, and ultimately cell death. We propose that instead of targeting a single molecule, oxaliplatin preferentially partitions into nucleoli, where it modifies nucleolar RNA and proteins. This mechanism provides a general approach for drugging the increasing number of cellular processes linked to biomolecular condensates.

Published
2022

8. Ferroptosis in health and disease

Author

Berndt, Carsten, Alborzinia, Hamed, Amen, Vera Skafar, Ayton, Scott, Barayeu, Uladzimir, Bartelt, Alexander, Bayir, Hülya, Bebber, Christina M., Birsoy, Kivanc, Böttcher, Jan P., Brabletz, Simone, Brabletz, Thomas, Brown, Ashley R., Brüne, Bernhard, Bulli, Giorgia, Bruneau, Alix, Chen, Quan, DeNicola, Gina M., Dick, Tobias P., Distéfano, Ayelén, Dixon, Scott J., Engler, Jan B., Esser-von Bieren, Julia, Fedorova, Maria, Friedmann Angeli, José Pedro, Friese, Manuel A., Fuhrmann, Dominic C., García-Sáez, Ana J., Garbowicz, Karolina, Götz, Magdalena, Gu, Wei, Hammerich, Linda, Hassannia, Behrouz, Jiang, Xuejun, Jeridi, Aicha, Kang, Yun Pyo, Kagan, Valerian E., Konrad, David B., Kotschi, Stefan, Lei, Peng, Le Tertre, Marlène, Lev, Sima, Liang, Deguang, Linkermann, Andreas, Lohr, Carolin, Lorenz, Svenja, Luedde, Tom, Methner, Axel, Michalke, Bernhard, Milton, Anna V., Min, Junxia, Mishima, Eikan, Müller, Sebastian, Motohashi, Hozumi, Muckenthaler, Martina U., Murakami, Shohei, Olzmann, James A., Pagnussat, Gabriela, Pan, Zijan, Papagiannakopoulos, Thales, Pedrera Puentes, Lohans, Pratt, Derek A., Proneth, Bettina, Ramsauer, Lukas, Rodriguez, Raphael, Saito, Yoshiro, Schmidt, Felix, Schmitt, Carina, Schulze, Almut, Schwab, Annemarie, Schwantes, Anna, Soula, Mariluz, Spitzlberger, Benedikt, Stockwell, Brent R., Thewes, Leonie, Thorn-Seshold, Oliver, Toyokuni, Shinya, Tonnus, Wulf, Trumpp, Andreas, Vandenabeele, Peter, Vanden Berghe, Tom, Venkataramani, Vivek, Vogel, Felix C.E., von Karstedt, Silvia, Wang, Fudi, Westermann, Frank, Wientjens, Chantal, Wilhelm, Christoph, Wölk, Michele, Wu, Katherine, Yang, Xin, Yu, Fan, Zou, Yilong, and Conrad, Marcus

Published
2024
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10. Ribosome stalling during selenoprotein translation exposes a ferroptosis vulnerability

Author

Li, Zhipeng, Ferguson, Lucas, Deol, Kirandeep K, Roberts, Melissa A, Magtanong, Leslie, Hendricks, Joseph M, Mousa, Gergey Alzaem, Kilinc, Seda, Schaefer, Kaitlin, Wells, James A, Bassik, Michael C, Goga, Andrei, Dixon, Scott J, Ingolia, Nicholas T, and Olzmann, James A

Subjects
Biochemistry and Cell Biology, Biological Sciences, Genetics, Cancer, 2.1 Biological and endogenous factors, Ferroptosis, Phospholipid Hydroperoxide Glutathione Peroxidase, Ribosomes, Selenium, Selenoproteins, Medicinal and Biomolecular Chemistry, Biochemistry & Molecular Biology, Biochemistry and cell biology, Medicinal and biomolecular chemistry
Abstract

The selenoprotein glutathione peroxidase 4 (GPX4) prevents ferroptosis by converting lipid peroxides into nontoxic lipid alcohols. GPX4 has emerged as a promising therapeutic target for cancer treatment, but some cancer cells are resistant to ferroptosis triggered by GPX4 inhibition. Using a chemical-genetic screen, we identify LRP8 (also known as ApoER2) as a ferroptosis resistance factor that is upregulated in cancer. Loss of LRP8 decreases cellular selenium levels and the expression of a subset of selenoproteins. Counter to the canonical hierarchical selenoprotein regulatory program, GPX4 levels are strongly reduced due to impaired translation. Mechanistically, low selenium levels result in ribosome stalling at the inefficiently decoded GPX4 selenocysteine UGA codon, leading to ribosome collisions, early translation termination and proteasomal clearance of the N-terminal GPX4 fragment. These findings reveal rewiring of the selenoprotein hierarchy in cancer cells and identify ribosome stalling and collisions during GPX4 translation as ferroptosis vulnerabilities in cancer.

Published
2022

11. SU086, an inhibitor of HSP90, impairs glycolysis and represents a treatment strategy for advanced prostate cancer

Author

Rice, Meghan A, Kumar, Vineet, Tailor, Dhanir, Garcia-Marques, Fernando Jose, Hsu, En-Chi, Liu, Shiqin, Bermudez, Abel, Kanchustambham, Vijayalakshmi, Shankar, Vishnu, Inde, Zintis, Alabi, Busola Ruth, Muruganantham, Arvind, Shen, Michelle, Pandrala, Mallesh, Nolley, Rosalie, Aslan, Merve, Ghoochani, Ali, Agarwal, Arushi, Buckup, Mark, Kumar, Manoj, Going, Catherine C, Peehl, Donna M, Dixon, Scott J, Zare, Richard N, Brooks, James D, Pitteri, Sharon J, Malhotra, Sanjay V, and Stoyanova, Tanya

Subjects
Biomedical and Clinical Sciences, Clinical Sciences, Oncology and Carcinogenesis, Cancer, Urologic Diseases, Prostate Cancer, Biotechnology, Aging, 5.1 Pharmaceuticals, 2.1 Biological and endogenous factors, Cell Proliferation, Glycolysis, HSP90 Heat-Shock Proteins, Humans, Male, Prostatic Neoplasms, Proteomics, HSP90, combination therapy, glycolysis, metabolism, prostate cancer, therapeutics, therapy, Biomedical and clinical sciences
Abstract

Among men, prostate cancer is the second leading cause of cancer-associated mortality, with advanced disease remaining a major clinical challenge. We describe a small molecule, SU086, as a therapeutic strategy for advanced prostate cancer. We demonstrate that SU086 inhibits the growth of prostate cancer cells in vitro, cell-line and patient-derived xenografts in vivo, and ex vivo prostate cancer patient specimens. Furthermore, SU086 in combination with standard of care second-generation anti-androgen therapies displays increased impairment of prostate cancer cell and tumor growth in vitro and in vivo. Cellular thermal shift assay reveals that SU086 binds to heat shock protein 90 (HSP90) and leads to a decrease in HSP90 levels. Proteomic profiling demonstrates that SU086 binds to and decreases HSP90. Metabolomic profiling reveals that SU086 leads to perturbation of glycolysis. Our study identifies SU086 as a treatment for advanced prostate cancer as a single agent or when combined with second-generation anti-androgens.

Published
2022

16. Death-seq identifies regulators of cell death and senolytic therapies

Author

Colville, Alex, Liu, Jie-Yu, Rodriguez-Mateo, Cristina, Thomas, Samantha, Ishak, Heather D., Zhou, Ronghao, Klein, Julian D.D., Morgens, David W., Goshayeshi, Armon, Salvi, Jayesh S., Yao, David, Spees, Kaitlyn, Dixon, Scott J., Liu, Chun, Rhee, June-Wha, Lai, Celine, Wu, Joseph C., Bassik, Michael C., and Rando, Thomas A.

Published
2023
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18. Systematic Identification of Regulators of Oxidative Stress Reveals Non-canonical Roles for Peroxisomal Import and the Pentose Phosphate Pathway

Author

Dubreuil, Michael M, Morgens, David W, Okumoto, Kanji, Honsho, Masanori, Contrepois, Kévin, Lee-McMullen, Brittany, Traber, Gavin McAllister, Sood, Ria S, Dixon, Scott J, Snyder, Michael P, Fujiki, Yukio, and Bassik, Michael C

Subjects
Biochemistry and Cell Biology, Biological Sciences, 2.1 Biological and endogenous factors, CRISPR-Cas Systems, Catalase, Cytoprotection, Cytosol, Genome, Human, Glucose, Glycolysis, HeLa Cells, Humans, K562 Cells, Oxidative Stress, Pentose Phosphate Pathway, Peroxisomes, Phosphogluconate Dehydrogenase, Protein Transport, RNA, Small Interfering, Reactive Oxygen Species, Hela Cells, CRISPR, catalase, genome-wide screen, oxidative stress, pentose phosphate pathway, peroxisomal import pathway, phosphogluconate dehydrogenase, reactive oxygen species, shRNA, Medical Physiology, Biological sciences
Abstract

Reactive oxygen species (ROS) play critical roles in metabolism and disease, yet a comprehensive analysis of the cellular response to oxidative stress is lacking. To systematically identify regulators of oxidative stress, we conducted genome-wide Cas9/CRISPR and shRNA screens. This revealed a detailed picture of diverse pathways that control oxidative stress response, ranging from the TCA cycle and DNA repair machineries to iron transport, trafficking, and metabolism. Paradoxically, disrupting the pentose phosphate pathway (PPP) at the level of phosphogluconate dehydrogenase (PGD) protects cells against ROS. This dramatically alters metabolites in the PPP, consistent with rewiring of upper glycolysis to promote antioxidant production. In addition, disruption of peroxisomal import unexpectedly increases resistance to oxidative stress by altering the localization of catalase. Together, these studies provide insights into the roles of peroxisomal matrix import and the PPP in redox biology and represent a rich resource for understanding the cellular response to oxidative stress.

Published
2020

23. The CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis

Author

Bersuker, Kirill, Hendricks, Joseph M, Li, Zhipeng, Magtanong, Leslie, Ford, Breanna, Tang, Peter H, Roberts, Melissa A, Tong, Bingqi, Maimone, Thomas J, Zoncu, Roberto, Bassik, Michael C, Nomura, Daniel K, Dixon, Scott J, and Olzmann, James A

Subjects
Biochemistry and Cell Biology, Biomedical and Clinical Sciences, Oncology and Carcinogenesis, Biological Sciences, Cancer, Nutrition, 2.1 Biological and endogenous factors, 5.1 Pharmaceuticals, Generic health relevance, Good Health and Well Being, Animals, Apoptosis Regulatory Proteins, Cell Line, Tumor, Cell Membrane, Ferroptosis, Gene Expression Regulation, Enzymologic, Heterografts, Humans, Lipid Peroxides, Male, Mice, Mice, SCID, Mitochondrial Proteins, Phospholipid Hydroperoxide Glutathione Peroxidase, Ubiquinone, General Science & Technology
Abstract

Ferroptosis is a form of regulated cell death that is caused by the iron-dependent peroxidation of lipids1,2. The glutathione-dependent lipid hydroperoxidase glutathione peroxidase 4 (GPX4) prevents ferroptosis by converting lipid hydroperoxides into non-toxic lipid alcohols3,4. Ferroptosis has previously been implicated in the cell death that underlies several degenerative conditions2, and induction of ferroptosis by the inhibition of GPX4 has emerged as a therapeutic strategy to trigger cancer cell death5. However, sensitivity to GPX4 inhibitors varies greatly across cancer cell lines6, which suggests that additional factors govern resistance to ferroptosis. Here, using a synthetic lethal CRISPR-Cas9 screen, we identify ferroptosis suppressor protein 1 (FSP1) (previously known as apoptosis-inducing factor mitochondrial 2 (AIFM2)) as a potent ferroptosis-resistance factor. Our data indicate that myristoylation recruits FSP1 to the plasma membrane where it functions as an oxidoreductase that reduces coenzyme Q10 (CoQ) (also known as ubiquinone-10), which acts as a lipophilic radical-trapping antioxidant that halts the propagation of lipid peroxides. We further find that FSP1 expression positively correlates with ferroptosis resistance across hundreds of cancer cell lines, and that FSP1 mediates resistance to ferroptosis in lung cancer cells in culture and in mouse tumour xenografts. Thus, our data identify FSP1 as a key component of a non-mitochondrial CoQ antioxidant system that acts in parallel to the canonical glutathione-based GPX4 pathway. These findings define a ferroptosis suppression pathway and indicate that pharmacological inhibition of FSP1 may provide an effective strategy to sensitize cancer cells to ferroptosis-inducing chemotherapeutic agents.

Published
2019

24. Exogenous Monounsaturated Fatty Acids Promote a Ferroptosis-Resistant Cell State

Author

Magtanong, Leslie, Ko, Pin-Joe, To, Milton, Cao, Jennifer Yinuo, Forcina, Giovanni C, Tarangelo, Amy, Ward, Carl C, Cho, Kevin, Patti, Gary J, Nomura, Daniel K, Olzmann, James A, and Dixon, Scott J

Subjects
1.1 Normal biological development and functioning, Underpinning research, Animals, Arachidonic Acid, Cell Line, Cell Membrane, Coenzyme A Ligases, Fatty Acids, Monounsaturated, Ferroptosis, Lipid Droplets, Lipids, Mice, Oxidation-Reduction, Phospholipid Hydroperoxide Glutathione Peroxidase, Reactive Oxygen Species, GPX4, MUFAs, cell death, ferroptosis, iron, lipid ROS, lipid droplet, lipotoxicity, oleate
Abstract

The initiation and execution of cell death can be regulated by various lipids. How the levels of environmental (exogenous) lipids impact cell death sensitivity is not well understood. We find that exogenous monounsaturated fatty acids (MUFAs) potently inhibit the non-apoptotic, iron-dependent, oxidative cell death process of ferroptosis. This protective effect is associated with the suppression of lipid reactive oxygen species (ROS) accumulation at the plasma membrane and decreased levels of phospholipids containing oxidizable polyunsaturated fatty acids. Treatment with exogenous MUFAs reduces the sensitivity of plasma membrane lipids to oxidation over several hours. This effect requires MUFA activation by acyl-coenzyme A synthetase long-chain family member 3 (ACSL3) and is independent of lipid droplet formation. Exogenous MUFAs also protect cells from apoptotic lipotoxicity caused by the accumulation of saturated fatty acids, but in an ACSL3-independent manner. Our work demonstrates that ACSL3-dependent MUFA activation promotes a ferroptosis-resistant cell state.

Published
2019

27. Characterization of a small molecule inhibitor of disulfide reductases that induces oxidative stress and lethality in lung cancer cells

Author

Johnson, Fraser D., Ferrarone, John, Liu, Alvin, Brandstädter, Christina, Munuganti, Ravi, Farnsworth, Dylan A., Lu, Daniel, Luu, Jennifer, Sihota, Tianna, Jansen, Sophie, Nagelberg, Amy, Shi, Rocky, Forcina, Giovanni C., Zhang, Xu, Cheng, Grace S.W., Spencer Miko, Sandra E., de Rappard-Yuswack, Georgia, Sorensen, Poul H., Dixon, Scott J., Guha, Udayan, Becker, Katja, Djaballah, Hakim, Somwar, Romel, Varmus, Harold, Morin, Gregg B., and Lockwood, William W.

Published
2022
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28. Author Correction: Lipid droplets and peroxisomes are co-regulated to drive lifespan extension in response to mono-unsaturated fatty acids

Author

Papsdorf, Katharina, Miklas, Jason W., Hosseini, Amir, Cabruja, Matias, Morrow, Christopher S., Savini, Marzia, Yu, Yong, Silva-García, Carlos G., Haseley, Nicole R., Murphy, Luke Meraz, Yao, Pallas, de Launoit, Elisa, Dixon, Scott J., Snyder, Michael P., Wang, Meng C., Mair, William B., and Brunet, Anne

Published
2023
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29. Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018

Author

Galluzzi, Lorenzo, Vitale, Ilio, Aaronson, Stuart A, Abrams, John M, Adam, Dieter, Agostinis, Patrizia, Alnemri, Emad S, Altucci, Lucia, Amelio, Ivano, Andrews, David W, Annicchiarico-Petruzzelli, Margherita, Antonov, Alexey V, Arama, Eli, Baehrecke, Eric H, Barlev, Nickolai A, Bazan, Nicolas G, Bernassola, Francesca, Bertrand, Mathieu JM, Bianchi, Katiuscia, Blagosklonny, Mikhail V, Blomgren, Klas, Borner, Christoph, Boya, Patricia, Brenner, Catherine, Campanella, Michelangelo, Candi, Eleonora, Carmona-Gutierrez, Didac, Cecconi, Francesco, Chan, Francis K-M, Chandel, Navdeep S, Cheng, Emily H, Chipuk, Jerry E, Cidlowski, John A, Ciechanover, Aaron, Cohen, Gerald M, Conrad, Marcus, Cubillos-Ruiz, Juan R, Czabotar, Peter E, D’Angiolella, Vincenzo, Dawson, Ted M, Dawson, Valina L, De Laurenzi, Vincenzo, De Maria, Ruggero, Debatin, Klaus-Michael, DeBerardinis, Ralph J, Deshmukh, Mohanish, Di Daniele, Nicola, Di Virgilio, Francesco, Dixit, Vishva M, Dixon, Scott J, Duckett, Colin S, Dynlacht, Brian D, El-Deiry, Wafik S, Elrod, John W, Fimia, Gian Maria, Fulda, Simone, García-Sáez, Ana J, Garg, Abhishek D, Garrido, Carmen, Gavathiotis, Evripidis, Golstein, Pierre, Gottlieb, Eyal, Green, Douglas R, Greene, Lloyd A, Gronemeyer, Hinrich, Gross, Atan, Hajnoczky, Gyorgy, Hardwick, J Marie, Harris, Isaac S, Hengartner, Michael O, Hetz, Claudio, Ichijo, Hidenori, Jäättelä, Marja, Joseph, Bertrand, Jost, Philipp J, Juin, Philippe P, Kaiser, William J, Karin, Michael, Kaufmann, Thomas, Kepp, Oliver, Kimchi, Adi, Kitsis, Richard N, Klionsky, Daniel J, Knight, Richard A, Kumar, Sharad, Lee, Sam W, Lemasters, John J, Levine, Beth, Linkermann, Andreas, Lipton, Stuart A, Lockshin, Richard A, López-Otín, Carlos, Lowe, Scott W, Luedde, Tom, Lugli, Enrico, MacFarlane, Marion, Madeo, Frank, Malewicz, Michal, Malorni, Walter, and Manic, Gwenola

Subjects
Biochemistry and Cell Biology, Biological Sciences, Animals, Cell Death, Humans, Lysosomes, Mitochondrial Membrane Transport Proteins, Mitochondrial Permeability Transition Pore, Necrosis, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Health sciences
Abstract

Over the past decade, the Nomenclature Committee on Cell Death (NCCD) has formulated guidelines for the definition and interpretation of cell death from morphological, biochemical, and functional perspectives. Since the field continues to expand and novel mechanisms that orchestrate multiple cell death pathways are unveiled, we propose an updated classification of cell death subroutines focusing on mechanistic and essential (as opposed to correlative and dispensable) aspects of the process. As we provide molecularly oriented definitions of terms including intrinsic apoptosis, extrinsic apoptosis, mitochondrial permeability transition (MPT)-driven necrosis, necroptosis, ferroptosis, pyroptosis, parthanatos, entotic cell death, NETotic cell death, lysosome-dependent cell death, autophagy-dependent cell death, immunogenic cell death, cellular senescence, and mitotic catastrophe, we discuss the utility of neologisms that refer to highly specialized instances of these processes. The mission of the NCCD is to provide a widely accepted nomenclature on cell death in support of the continued development of the field.

Published
2018

31. Lipid Quality Control and Ferroptosis: From Concept to Mechanism.

Author

Li, Zhipeng, Lange, Mike, Dixon, Scott J., and Olzmann, James A.

Abstract

Cellular quality control systems sense and mediate homeostatic responses to prevent the buildup of aberrant macromolecules, which arise from errors during biosynthesis, damage by environmental insults, or imbalances in enzymatic and metabolic activity. Lipids are structurally diverse macromolecules that have many important cellular functions, ranging from structural roles in membranes to functions as signaling and energy-storage molecules. As with other macromolecules, lipids can be damaged (e.g., oxidized), and cells require quality control systems to ensure that nonfunctional and potentially toxic lipids do not accumulate. Ferroptosis is a form of cell death that results from the failure of lipid quality control and the consequent accumulation of oxidatively damaged phospholipids. In this review, we describe a framework for lipid quality control, using ferroptosis as an illustrative example to highlight concepts related to lipid damage, membrane remodeling, and suppression or detoxification of lipid damage via preemptive and damage-repair lipid quality control pathways. [ABSTRACT FROM AUTHOR]

Published
2024
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37. MLKL Requires the Inositol Phosphate Code to Execute Necroptosis

Author

Dovey, Cole M., Diep, Jonathan, Clarke, Bradley P., Hale, Andrew T., McNamara, Dan E., Guo, Hongyan, Brown, Nathaniel W., Jr., Cao, Jennifer Yinuo, Grace, Christy R., Gough, Peter J., Bertin, John, Dixon, Scott J., Fiedler, Dorothea, Mocarski, Edward S., Kaiser, William J., Moldoveanu, Tudor, York, John D., and Carette, Jan E.

Published
2018
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38. Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease

Author

Stockwell, Brent R., Friedmann Angeli, José Pedro, Bayir, Hülya, Bush, Ashley I., Conrad, Marcus, Dixon, Scott J., Fulda, Simone, Gascón, Sergio, Hatzios, Stavroula K., Kagan, Valerian E., Noel, Kay, Jiang, Xuejun, Linkermann, Andreas, Murphy, Maureen E., Overholtzer, Michael, Oyagi, Atsushi, Pagnussat, Gabriela C., Park, Jason, Ran, Qitao, Rosenfeld, Craig S., Salnikow, Konstantin, Tang, Daolin, Torti, Frank M., Torti, Suzy V., Toyokuni, Shinya, Woerpel, K.A., and Zhang, Donna D.

Published
2017
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50. Systematic Mapping of Genetic Interaction Networks

Author

Dixon, Scott J., Costanzo, Michael, Baryshnikova, Anastasia, Andrews, Brenda, and Boone, Charles

Subjects
Biological sciences
Abstract

Byline: Scott J. Dixon, Banting and Best Department of Medical Research, Terrence Donnelly Center for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 1A7, Canada; email: charlie.boone@utoronto.ca, Department of Biological Sciences, Columbia University, New York, New York 10027; Michael Costanzo, Banting and Best Department of Medical Research, Terrence Donnelly Center for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 1A7, Canada; email: charlie.boone@utoronto.ca; Anastasia Baryshnikova, Banting and Best Department of Medical Research, Terrence Donnelly Center for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 1A7, Canada; email: charlie.boone@utoronto.ca; Brenda Andrews, Banting and Best Department of Medical Research, Terrence Donnelly Center for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 1A7, Canada; email: charlie.boone@utoronto.ca; Charles Boone, Banting and Best Department of Medical Research, Terrence Donnelly Center for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 1A7, Canada; email: charlie.boone@utoronto.ca Keywords: genetic interaction, network, synthetic lethal, Saccharomyces cerevisiae, epistasis Author Notes: *These authors contributed equally to this work. Abstract Genetic interactions influencing a phenotype of interest can be identified systematically using libraries of genetic tools that perturb biological systems in a defined manner. Systematic screens conducted in the yeast Saccharomyces cerevisiae have identified thousands of genetic interactions and provided insight into the global structure of biological networks. Techniques enabling systematic genetic interaction mapping have been extended to other single-celled organisms, the bacteria Escherichia coli and the yeast Schizosaccharomyces pombe, opening the way to comparative investigations of interaction networks. Genetic interaction screens in Caenorhabditis elegans, Drosophila melanogaster, and mammalian models are helping to improve our understanding of metazoan-specific signaling pathways. Together, our emerging knowledge of the genetic wiring diagrams of eukaryotic and prokaryotic cells is providing a new understanding of the relationship between genotype and phenotype.

Published
2009

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