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828 results on '"Dixit, Vishva M"'

4. Inhibiting membrane rupture with NINJ1 antibodies limits tissue injury

Author

Kayagaki, Nobuhiko, Stowe, Irma B., Alegre, Kamela, Deshpande, Ishan, Wu, Shuang, Lin, Zhonghua, Kornfeld, Opher S., Lee, Bettina L., Zhang, Juan, Liu, John, Suto, Eric, Lee, Wyne P., Schneider, Kellen, Lin, WeiYu, Seshasayee, Dhaya, Bhangale, Tushar, Chalouni, Cecile, Johnson, Matthew C., Joshi, Prajakta, Mossemann, Jan, Zhao, Sarah, Ali, Danish, Goldenberg, Neil M., Sayed, Blayne A., Steinberg, Benjamin E., Newton, Kim, Webster, Joshua D., Kelly, Ryan L., and Dixit, Vishva M.

Published
2023
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5. Cell death

Author

Newton, Kim, Strasser, Andreas, Kayagaki, Nobuhiko, and Dixit, Vishva M.

Published
2024
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6. Targeted alveolar regeneration with Frizzled-specific agonists

Author

Nabhan, Ahmad N., Webster, Joshua D., Adams, Jarret J., Blazer, Levi, Everrett, Christine, Eidenschenk, Celine, Arlantico, Alexander, Fleming, Isabel, Brightbill, Hans D., Wolters, Paul J., Modrusan, Zora, Seshagiri, Somasekar, Angers, Stephane, Sidhu, Sachdev S., Newton, Kim, Arron, Joseph R., and Dixit, Vishva M.

Published
2023
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7. 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

8. Assembly and Function of Heterotypic Ubiquitin Chains in Cell-Cycle and Protein Quality Control

Author

Yau, Richard G, Doerner, Kerstin, Castellanos, Erick R, Haakonsen, Diane L, Werner, Achim, Wang, Nan, Yang, X William, Martinez-Martin, Nadia, Matsumoto, Marissa L, Dixit, Vishva M, and Rape, Michael

Subjects
Biochemistry and Cell Biology, Biological Sciences, 1.1 Normal biological development and functioning, Underpinning research, Generic health relevance, Anaphase-Promoting Complex-Cyclosome, Antibodies, Bispecific, Cell Cycle, Humans, Mitosis, Protein Biosynthesis, Signal Transduction, Ubiquitin, Ubiquitination, Huntingtin, Huntington’s disease, anaphase-promoting complex, branched ubiquitin chain, proteasome, protein quality control, ubiquitin, ubiquitin chain, Medical and Health Sciences, Developmental Biology, Biological sciences, Biomedical and clinical sciences
Abstract

Posttranslational modification with ubiquitin chains controls cell fate in all eukaryotes. Depending on the connectivity between subunits, different ubiquitin chain types trigger distinct outputs, as seen with K48- and K63-linked conjugates that drive protein degradation or complex assembly, respectively. Recent biochemical analyses also suggested roles for mixed or branched ubiquitin chains, yet without a method to monitor endogenous conjugates, the physiological significance of heterotypic polymers remained poorly understood. Here, we engineered a bispecific antibody to detect K11/K48-linked chains and identified mitotic regulators, misfolded nascent polypeptides, and pathological Huntingtin variants as their endogenous substrates. We show that K11/K48-linked chains are synthesized and processed by essential ubiquitin ligases and effectors that are mutated across neurodegenerative diseases; accordingly, these conjugates promote rapid proteasomal clearance of aggregation-prone proteins. By revealing key roles of K11/K48-linked chains in cell-cycle and quality control, we establish heterotypic ubiquitin conjugates as important carriers of biological information.

Published
2017

9. NINJ1 mediates plasma membrane rupture during lytic cell death

Author

Kayagaki, Nobuhiko, Kornfeld, Opher S., Lee, Bettina L., Stowe, Irma B., O’Rourke, Karen, Li, Qingling, Sandoval, Wendy, Yan, Donghong, Kang, Jing, Xu, Min, Zhang, Juan, Lee, Wyne P., McKenzie, Brent S., Ulas, Gözde, Payandeh, Jian, Roose-Girma, Merone, Modrusan, Zora, Reja, Rohit, Sagolla, Meredith, Webster, Joshua D., Cho, Vicky, Andrews, T. Daniel, Morris, Lucy X., Miosge, Lisa A., Goodnow, Christopher C., Bertram, Edward M., and Dixit, Vishva M.

Published
2021
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10. Integration of innate immune signalling by caspase-8 cleavage of N4BP1

Author

Gitlin, Alexander D., Heger, Klaus, Schubert, Alexander F., Reja, Rohit, Yan, Donghong, Pham, Victoria C., Suto, Eric, Zhang, Juan, Kwon, Youngsu C., Freund, Emily C., Kang, Jing, Pham, Anna, Caothien, Roger, Bacarro, Natasha, Hinkle, Trent, Xu, Min, McKenzie, Brent S., Haley, Benjamin, Lee, Wyne P., Lill, Jennie R., Roose-Girma, Merone, Dohse, Monika, Webster, Joshua D., Newton, Kim, and Dixit, Vishva M.

Published
2020
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12. Ubiquitin ligase COP1 coordinates transcriptional programs that control cell type specification in the developing mouse brain

Author

Newton, Kim, Dugger, Debra L., Sengupta-Ghosh, Arundhati, Ferrando, Ronald E., Chu, Felix, Tao, Janet, Lam, Wendy, Haller, Susan, Chan, Sara, Sa, Susan, Dunlap, Debra, Eastham-Anderson, Jeffrey, Ngu, Hai, Hung, Jeffrey, French, Dorothy M., Webster, Joshua D., Bolon, Brad, Liu, Jinfeng, Reja, Rohit, Kummerfeld, Sarah, Chen, Ying-Jiun, Modrusan, Zora, Lewcock, Joseph W., and Dixit, Vishva M.

Published
2018

25. OTULIN limits cell death and inflammation by deubiquitinating LUBAC

Author

Heger, Klaus, Wickliffe, Katherine E., Ndoja, Ada, Zhang, Juan, Murthy, Aditya, Dugger, Debra L., Maltzman, Allie, de Sousa e Melo, Felipe, Hung, Jeffrey, Zeng, Yi, Verschueren, Erik, Kirkpatrick, Donald S., Vucic, Domagoj, Lee, Wyne P., Roose-Girma, Merone, Newman, Robert J., Warming, Søren, Hsiao, Yi-Chun, Kőműves, László G., Webster, Joshua D., Newton, Kim, and Dixit, Vishva M.

Published
2018
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30. Src-like Adaptor Protein (Slap) Is a Negative Regulator of T Cell Receptor Signaling

Author

Sosinowski, Tomasz, Pandey, Akhilesh, Dixit, Vishva M, and Weiss, Arthur

Subjects
Biomedical and Clinical Sciences, Health Sciences, 2.1 Biological and endogenous factors, Aetiology, 3T3 Cells, Adaptor Proteins, Signal Transducing, Animals, Calcium, Cell Line, Detergents, Down-Regulation, HeLa Cells, Humans, Jurkat Cells, Mice, Phosphoproteins, Protein-Tyrosine Kinases, Proto-Oncogene Proteins pp60(c-src), RNA, Messenger, Receptors, Antigen, T-Cell, Signal Transduction, Subcellular Fractions, Transcription, Genetic, Transfection, src Homology Domains, Lck, Src homology 2, T cell activation, calcium flux, endosomes, Hela Cells, Medical and Health Sciences, Immunology, Biomedical and clinical sciences, Health sciences
Abstract

Initiation of T cell antigen receptor (TCR) signaling is dependent on Lck, a Src family kinase. The Src-like adaptor protein (SLAP) contains Src homology (SH)3 and SH2 domains, which are highly homologous to those of Lck and other Src family members. Because of the structural similarity between Lck and SLAP, we studied its potential role in TCR signaling. Here, we show that SLAP is expressed in T cells, and that when expressed in Jurkat T cells it can specifically inhibit TCR signaling leading to nuclear factor of activated T cells (NFAT)-, activator protein 1 (AP-1)-, and interleukin 2-dependent transcription. The SH3 and SH2 domains of SLAP are required for maximal attenuation of TCR signaling. This inhibitory activity can be bypassed by the combination of phorbol myristate acetate (PMA) and ionomycin, suggesting that SLAP acts proximally in the TCR signaling pathway. SLAP colocalizes with endosomes in Jurkat and in HeLa cells, and is insoluble in mild detergents. In stimulated Jurkat cells, SLAP associates with a molecular signaling complex containing CD3zeta, ZAP-70, SH2 domain-containing leukocyte protein of 76 kD (SLP-76), Vav, and possibly linker for activation of T cells (LAT). These results suggest that SLAP is a negative regulator of TCR signaling.

Published
2000

33. Caspase cleavage of RIPK3 after Asp333is dispensable for mouse embryogenesis

Author

Newton, Kim, Wickliffe, Katherine E., Maltzman, Allie, Dugger, Debra L., Webster, Joshua D., Guo, Hongyan, and Dixit, Vishva M.

Abstract

The proteolytic activity of caspase-8 suppresses lethal RIPK1-, RIPK3- and MLKL-dependent necroptosis during mouse embryogenesis. Caspase-8 is reported to cleave RIPK3 in addition to the RIPK3-interacting kinase RIPK1, but whether cleavage of RIPK3 is crucial for necroptosis suppression is unclear. Here we show that caspase-8-driven cleavage of endogenous mouse RIPK3 after Asp333is dependent on downstream caspase-3. Consistent with RIPK3 cleavage being a consequence of apoptosis rather than a critical brake on necroptosis, Ripk3D333A/D333Aknock-in mice lacking the Asp333cleavage site are viable and develop normally. Moreover, in contrast to mice lacking caspase-8 in their intestinal epithelial cells, Ripk3D333A/D333Amice do not exhibit increased sensitivity to high dose tumor necrosis factor (TNF). Ripk3D333A/D333Amacrophages died at the same rate as wild-type (WT) macrophages in response to TNF plus cycloheximide, TNF plus emricasan, or infection with murine cytomegalovirus (MCMV) lacking M36 and M45 to inhibit caspase-8 and RIPK3 activation, respectively. We conclude that caspase cleavage of RIPK3 is dispensable for mouse development, and that cleavage of caspase-8 substrates, including RIPK1, is sufficient to prevent necroptosis.

Published
2024
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34. RIPK1 inhibits ZBP1-driven necroptosis during development

Author

Newton, Kim, Wickliffe, Katherine E., Maltzman, Allie, Dugger, Debra L., Strasser, Andreas, Pham, Victoria C., Lill, Jennie R., Roose-Girma, Merone, Warming, Sren, Solon, Margaret, Ngu, Hai, Webster, Joshua D., and Dixit, Vishva M.

Subjects
Apoptosis, Necrosis -- Causes of -- Prevention, Protein kinases -- Health aspects, Binding proteins -- Health aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Kim Newton (corresponding author) [1]; Katherine E. Wickliffe [1]; Allie Maltzman [1]; Debra L. Dugger [1]; Andreas Strasser [2, 3]; Victoria C. Pham [4]; Jennie R. Lill [4]; Merone [...]

Published
2016
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35. Synchronized renal tubular cell death involves ferroptosis

Author

Linkermann, Andreas, Skouta, Rachid, Himmerkus, Nina, Mulay, Shrikant R., Dewitz, Christin, De Zen, Federica, Prokai, Agnes, Zuchtriegel, Gabriele, Krombach, Fritz, Welz, Patrick-Simon, Weinlich, Ricardo, Berghe, Tom Vanden, Vandenabeele, Peter, Pasparakis, Manolis, Bleich, Markus, Weinberg, Joel M., Reichel, Christoph A., Bräsen, Jan Hinrich, Kunzendorf, Ulrich, Anders, Hans-Joachim, Stockwell, Brent R., Green, Douglas R., Krautwald, Stefan, and Dixit, Vishva M.

Published
2014

39. Phosphorylation and linear ubiquitin direct A20 inhibition of inflammation

Author

Wertz, Ingrid E., Newton, Kim, Seshasayee, Dhaya, Kusam, Saritha, Lam, Cynthia, Zhang, Juan, Popovych, Nataliya, Helgason, Elizabeth, Schoeffler, Allyn, Jeet, Surinder, Ramamoorthi, Nandhini, Kategaya, Lorna, Newman, Robert J., Horikawa, Keisuke, Dugger, Debra, Sandoval, Wendy, Mukund, Susmith, Zindal, Anuradha, Martin, Flavius, Quan, Clifford, Tom, Jeffrey, Fairbrother, Wayne J., Townsend, Michael, Warming, Soren, DeVoss, Jason, Liu, Jinfeng, Dueber, Erin, Caplazi, Patrick, Lee, Wyne P., Goodnow, Christopher C., Balazs, Mercedesz, Yu, Kebing, Kolumam, Ganesh, and Dixit, Vishva M.

Subjects
Inflammation -- Research -- Development and progression -- Care and treatment, Ubiquitin -- Research, Phosphorylation -- Research -- Genetic aspects, Genetically modified organisms -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Inactivation of the TNFAIP3 gene, encoding the A20 protein, is associated with critical inflammatory diseases including multiple sclerosis, rheumatoid arthritis and Crohn's disease. However, the role of A20 in attenuating inflammatory signalling is unclear owing to paradoxical in vitro and in vivo findings. Here we utilize genetically engineered mice bearing mutations in the A20 ovarian tumour (OTU)-type deubiquitinase domain or in the zinc finger-4 (ZnF4) ubiquitinbinding motif to investigate these discrepancies. We find that phosphorylation of A2 0 promotes cleavage of Lys63- linked polyubiquitin chains by the OTU domain and enhances ZnF4-mediated substrate ubiquitination. Additionally, levels of linear ubiquitination dictate whether A20-deficient cells die in response to tumour necrosis factor. Mechanistically, linear ubiquitin chains preserve the architecture of the TNFR1 signalling complex by blocking A20-mediated disassembly of Lys63-linked polyubiquitin scaffolds. Collectively, our studies reveal molecular mechanisms whereby A20 deubiquitinase activity and ubiquitin binding, linear ubiquitination, and cellular kinases cooperate to regulate inflammation and cell death., Debilitating autoimmune syndromes and inflammatory diseases are associated with inactivation of the TNFAIP3 gene, which encodes the A20 protein (1). Despite the well-validated role of A20 in attenuating inflammation, fundamental [...]

Published
2015
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42. Polyclonal hyper-IgE mouse model reveals mechanistic insights into antibody class switch recombination

Author

Misaghi, Shahram, Senger, Kate, Sai, Tao, Qu, Yan, Sun, Yonglian, Hamidzadeh, Kajal, Nguyen, Allen, Jin, Zhaoyu, Zhou, Meijuan, Yan, Donghong, Lin, Wei Yu, Lin, Zhonghua, Lorenzo, Maria N., Sebrell, Andrew, Ding, Jiabing, Xu, Min, Caplazi, Patrick, Austin, Cary D., Balazs, Mercedesz, Roose-Girma, Merone, DeForge, Laura, Warming, Søren, Lee, Wyne P., Dixit, Vishva M., and Zarrin, Ali A.

Published
2013

45. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling

Author

Kayagaki, Nobuhiko, Stowe, Irma B., Lee, Bettina L., O'Rourke, Karen, Anderson, Keith, Warming, Soren, Cuellar, Trinna, Haley, Benjamin, Roose-Girma, Merone, Phung, Qui T., Liu, Peter S., Lill, Jennie R., Li, Hong, Wu, Jiansheng, Kummerfeld, Sarah, Zhang, Juan, Lee, Wyne P., Snipas, Scott J., Salvesen, Guy S., Morris, Lucy X., Fitzgerald, Linda, Zhang, Yafei, Bertram, Edward M., Goodnow, Christopher C., and Dixit, Vishva M.

Subjects
Inflammation -- Physiological aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Intracellular lipopolysaccharide from Gram-negative bacteria including Escherichia coli, Salmonella typhimurium, Shigella flexneri, and Burkholderia thailandensis activates mouse caspase-11, causing pyroptotic cell death, interleukin-1β processing, and lethal septic shock. How caspase-11 executes these downstream signalling events is largely unknown. Here we show that gasdermin D is essential for caspase-11-dependent pyroptosis and interleukm-1β maturation. A forward genetic screen with ethyl-N-nitrosourea-mutagenized mice links Gsdmd to the intracellular lipopolysaccharide response. Macrophages from [Gsdmd.sup.-/-] mice generated by gene targeting also exhibit defective pyroptosis and interleukin-1β secretion induced by cytoplasmic lipopolysaccharide or Gram-negative bacteria. In addition, [Gsdmd.sup.-/-] mice are protected from a lethal dose of lipopolysaccharide. Mechanistically, caspase-11 cleaves gasdermin D, and the resulting amino-terminal fragment promotes both pyroptosis and NLRP3-dependent activation of caspase-1 in a cell-intrinsic manner. Our data identify gasdermin D as a critical target of caspase-11 and a key mediatorof the host response against Gram-negative bacteria., Cytoplasmic caspase-11 (also known as caspase-4) defines the non-canonical inflammasome that is activated by various Gram-negative bacterial infections and causes infected cells to die by pyroptosis (1-4). Caspase-11 also triggers [...]

Published
2015
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46. Deubiquitinase DUBA is a post-translational brake on interleukin-17 production in T cells

Author

Rutz, Sascha, Kayagaki, Nobuhiko, Phung, Qui T., Eidenschenk, Celine, Noubade, Rajkumar, Wang, Xiaoting, Lesch, Justin, Lu, Rongze, Newton, Kim, Huang, Oscar W., Cochran, Andrea G., Vasser, Mark, Fauber, Benjamin P., DeVoss, Jason, Webster, Joshua, Diehl, Lauri, Modrusan, Zora, Kirkpatrick, Donald S., Lill, Jennie R., Ouyang, Wenjun, and Dixit, Vishva M.

Subjects
Post-translational modification -- Research, T cells -- Genetic aspects, Cell research, Protein research, Interleukins -- Physiological aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

T-helpertype 17 ([T.sub.H]17) cells that produce the cytokines interleukin-17A (IL-17A) and IL-17F are implicated in the pathogenesis of several autoimmune diseases (1,2). The differentiation of [T.sub.H]17 cells is regulated by [...]

Published
2015

47. Loss of the Tumor Suppressor BAP1 Causes Myeloid Transformation

Author

Dey, Anwesha, Seshasayee, Dhaya, Noubade, Rajkumar, French, Dorothy M., Liu, Jinfeng, Chaurushiya, Mira S., Kirkpatrick, Donald S., Pham, Victoria C., Lill, Jennie R., Bakalarski, Corey E., Wu, Jiansheng, Phu, Lilian, Katavolos, Paula, LaFave, Lindsay M., Abdel-Wahab, Omar, Modrusan, Zora, Seshagiri, Somasekar, Dong, Ken, Lin, Zhonghua, Balazs, Mercedesz, Suriben, Rowena, Newton, Kim, Hymowitz, Sarah, Garcia-Manero, Guillermo, Martin, Flavius, Levine, Ross L., and Dixit, Vishva M.

Published
2012
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