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250 results on '"McMahon, Steven B."'

1. ARID1A-BAF coordinates ZIC2 genomic occupancy for epithelial-to-mesenchymal transition in cranial neural crest specification

Author

Barnada, Samantha M., Giner de Gracia, Aida, Morenilla-Palao, Cruz, López-Cascales, Maria Teresa, Scopa, Chiara, Waltrich, Francis J., Jr., Mikkers, Harald M.M., Cicardi, Maria Elena, Karlin, Jonathan, Trotti, Davide, Peterson, Kevin A., Brugmann, Samantha A., Santen, Gijs W.E., McMahon, Steven B., Herrera, Eloísa, and Trizzino, Marco

Published
2024
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9. Supplementary Data from USP22 Functions as an Oncogenic Driver in Prostate Cancer by Regulating Cell Proliferation and DNA Repair

Author

McCann, Jennifer J., primary, Vasilevskaya, Irina A., primary, Poudel Neupane, Neermala, primary, Shafi, Ayesha A., primary, McNair, Christopher, primary, Dylgjeri, Emanuela, primary, Mandigo, Amy C., primary, Schiewer, Matthew J., primary, Schrecengost, Randy S., primary, Gallagher, Peter, primary, Stanek, Timothy J., primary, McMahon, Steven B., primary, Berman-Booty, Lisa D., primary, Ostrander, William F., primary, and Knudsen, Karen E., primary

Published
2023
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10. Data from USP22 Functions as an Oncogenic Driver in Prostate Cancer by Regulating Cell Proliferation and DNA Repair

Author

McCann, Jennifer J., primary, Vasilevskaya, Irina A., primary, Poudel Neupane, Neermala, primary, Shafi, Ayesha A., primary, McNair, Christopher, primary, Dylgjeri, Emanuela, primary, Mandigo, Amy C., primary, Schiewer, Matthew J., primary, Schrecengost, Randy S., primary, Gallagher, Peter, primary, Stanek, Timothy J., primary, McMahon, Steven B., primary, Berman-Booty, Lisa D., primary, Ostrander, William F., primary, and Knudsen, Karen E., primary

Published
2023
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11. Supplementary Table 1 from Dachshund Binds p53 to Block the Growth of Lung Adenocarcinoma Cells

Author

Chen, Ke, primary, Wu, Kongming, primary, Cai, Shaoxin, primary, Zhang, Wei, primary, Zhou, Jie, primary, Wang, Jing, primary, Ertel, Adam, primary, Li, Zhiping, primary, Rui, Hallgeir, primary, Quong, Andrew, primary, Lisanti, Michael P., primary, Tozeren, Aydin, primary, Tanes, Ceylan, primary, Addya, Sankar, primary, Gormley, Michael, primary, Wang, Chenguang, primary, McMahon, Steven B., primary, and Pestell, Richard G., primary

Published
2023
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12. Supplementary Figures 1 - 3 from USP22 Regulates Oncogenic Signaling Pathways to Drive Lethal Cancer Progression

Author

Schrecengost, Randy S., primary, Dean, Jeffry L., primary, Goodwin, Jonathan F., primary, Schiewer, Matthew J., primary, Urban, Mark W., primary, Stanek, Timothy J., primary, Sussman, Robyn T., primary, Hicks, Jessica L., primary, Birbe, Ruth C., primary, Draganova-Tacheva, Rossitza A., primary, Visakorpi, Tapio, primary, DeMarzo, Angelo M., primary, McMahon, Steven B., primary, and Knudsen, Karen E., primary

Published
2023
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13. Supplementary Table 1 from USP22 Regulates Oncogenic Signaling Pathways to Drive Lethal Cancer Progression

Author

Schrecengost, Randy S., primary, Dean, Jeffry L., primary, Goodwin, Jonathan F., primary, Schiewer, Matthew J., primary, Urban, Mark W., primary, Stanek, Timothy J., primary, Sussman, Robyn T., primary, Hicks, Jessica L., primary, Birbe, Ruth C., primary, Draganova-Tacheva, Rossitza A., primary, Visakorpi, Tapio, primary, DeMarzo, Angelo M., primary, McMahon, Steven B., primary, and Knudsen, Karen E., primary

Published
2023
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14. Supplementary Figures 1 - 4 from Dachshund Binds p53 to Block the Growth of Lung Adenocarcinoma Cells

Author

Chen, Ke, primary, Wu, Kongming, primary, Cai, Shaoxin, primary, Zhang, Wei, primary, Zhou, Jie, primary, Wang, Jing, primary, Ertel, Adam, primary, Li, Zhiping, primary, Rui, Hallgeir, primary, Quong, Andrew, primary, Lisanti, Michael P., primary, Tozeren, Aydin, primary, Tanes, Ceylan, primary, Addya, Sankar, primary, Gormley, Michael, primary, Wang, Chenguang, primary, McMahon, Steven B., primary, and Pestell, Richard G., primary

Published
2023
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15. Data from USP22 Regulates Oncogenic Signaling Pathways to Drive Lethal Cancer Progression

Author

Schrecengost, Randy S., primary, Dean, Jeffry L., primary, Goodwin, Jonathan F., primary, Schiewer, Matthew J., primary, Urban, Mark W., primary, Stanek, Timothy J., primary, Sussman, Robyn T., primary, Hicks, Jessica L., primary, Birbe, Ruth C., primary, Draganova-Tacheva, Rossitza A., primary, Visakorpi, Tapio, primary, DeMarzo, Angelo M., primary, McMahon, Steven B., primary, and Knudsen, Karen E., primary

Published
2023
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16. Supplementary Figure Legend from Dachshund Binds p53 to Block the Growth of Lung Adenocarcinoma Cells

Author

Chen, Ke, primary, Wu, Kongming, primary, Cai, Shaoxin, primary, Zhang, Wei, primary, Zhou, Jie, primary, Wang, Jing, primary, Ertel, Adam, primary, Li, Zhiping, primary, Rui, Hallgeir, primary, Quong, Andrew, primary, Lisanti, Michael P., primary, Tozeren, Aydin, primary, Tanes, Ceylan, primary, Addya, Sankar, primary, Gormley, Michael, primary, Wang, Chenguang, primary, McMahon, Steven B., primary, and Pestell, Richard G., primary

Published
2023
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17. Data from Dachshund Binds p53 to Block the Growth of Lung Adenocarcinoma Cells

Author

Chen, Ke, primary, Wu, Kongming, primary, Cai, Shaoxin, primary, Zhang, Wei, primary, Zhou, Jie, primary, Wang, Jing, primary, Ertel, Adam, primary, Li, Zhiping, primary, Rui, Hallgeir, primary, Quong, Andrew, primary, Lisanti, Michael P., primary, Tozeren, Aydin, primary, Tanes, Ceylan, primary, Addya, Sankar, primary, Gormley, Michael, primary, Wang, Chenguang, primary, McMahon, Steven B., primary, and Pestell, Richard G., primary

Published
2023
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23. MYST protein acetyltransferase activity requires active site lysine autoacetylation

Author

Yuan, Hua, Rossetto, Dorine, Mellert, Hestia, Dang, Weiwei, Srinivasan, Madhusudan, Johnson, Jamel, Hodawadekar, Santosh, Ding, Emily C, Speicher, Kaye, Abshiru, Nebiyu, Perry, Rocco, Wu, Jiang, Yang, Chao, Zheng, Y George, Speicher, David W, Thibault, Pierre, Verreault, Alain, Johnson, F Bradley, Berger, Shelley L, Sternglanz, Rolf, McMahon, Steven B, Côté, Jacques, and Marmorstein, Ronen

Published
2012
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27. The ATM-related domain of TRRAP is required for histone acetyltransferase recruitment and Myc-dependent oncogenesis

Author

Park, Jeonghyeon, Kunjibettu, Sudeesha, McMahon, Steven B., and Cole, Michael D.

Subjects
Cytochemistry -- Research, Transferases -- Physiological aspects, Carcinogenesis -- Physiological aspects, Histones -- Physiological aspects, Biological sciences
Abstract

The ATM-related domain of TRRAP has been found to be necessary for Myc-dependent oncogenesis and histone acetyltransferase (HAT) recruitment. To look at the function of the ATM-related region of TRRAP, a progressive series of C-terminal deletions has been made from a FLAG epitope-tagged full-length TRRAP cDNA expression vector.

Published
2001

29. USP22 Functions as an Oncogenic Driver in Prostate Cancer by Regulating Cell Proliferation and DNA Repair

Author

McCann, Jennifer J., primary, Vasilevskaya, Irina A., additional, Poudel Neupane, Neermala, additional, Shafi, Ayesha A., additional, McNair, Christopher, additional, Dylgjeri, Emanuela, additional, Mandigo, Amy C., additional, Schiewer, Matthew J., additional, Schrecengost, Randy S., additional, Gallagher, Peter, additional, Stanek, Timothy J., additional, McMahon, Steven B., additional, Berman-Booty, Lisa D., additional, Ostrander, William F., additional, and Knudsen, Karen E., additional

Published
2020
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30. The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins

Author

Mcmahon, Steven B., Van Buskirk, Heather A., Dugan, Kerri A., Copeland, Terry D., and Cole, Michael D.

Subjects
Oncogenes -- Research, Carcinogenesis -- Research, Biological sciences
Abstract

Transformation/transcription domain-associated protein (TRRAP) is a protein related to the ataxia-telangiectasia mutated kinase family. TRRAP has been shown to interact with the oncogene product c-Myc via the amino terminus and with E2F-1 transactivation domain. Mutation and antisense studies of the TRRAP protein resulted in the inhibition of c-Myc- and E2F-1- dependent oncogenesis. TRRAP is a 434-kiloDalton highly conserved protein postulated to be an essential cofactor in carcinogenesis.

Published
1998

31. Interaction between the BAG1S isoform and HSP70 mediates the stability of anti-apoptotic proteins and the survival of osteosarcoma cells expressing oncogenic MYC.

Author

Gennaro, Victoria J., Wedegaertner, Helen, McMahon, Steven B., Gennaro, Victoria J., Wedegaertner, Helen, and McMahon, Steven B.

Abstract

BACKGROUND: The oncoprotein MYC has the dual capacity to drive cell cycle progression or induce apoptosis, depending on the cellular context. BAG1 was previously identified as a transcriptional target of MYC that functions as a critical determinant of this cell fate decision. The BAG1 protein is expressed as multiple isoforms, each having an array of distinct biochemical functions; however, the specific effector function of BAG1 that directs MYC-dependent cell survival has not been defined. METHODS: In our studies the human osteosarcoma line U2OS expressing a conditional MYC-ER allele was used to induce oncogenic levels of MYC. We interrogated MYC-driven survival processes by modifying BAG1 protein expression. The function of the separate BAG1 isoforms was investigated by depleting cells of endogenous BAG1 and reintroducing the distinct isoforms. Flow cytometry and immunoblot assays were performed to analyze the effect of specific BAG1 isoforms on MYC-dependent apoptosis. These experiments were repeated to determine the role of the HSP70 chaperone complex in BAG1 survival processes. Finally, a proteomic approach was used to identify a set of specific pro-survival proteins controlled by the HSP70/BAG1 complex. RESULTS: Loss of BAG1 resulted in robust MYC-induced apoptosis. Expression of the larger isoforms of BAG1, BAG1L and BAG1M, were insufficient to rescue survival in cells with oncogenic levels of MYC. Alternatively, reintroduction of BAG1S significantly reduced the level of apoptosis. Manipulation of the BAG1S interaction with HSP70 revealed that BAG1S provides its pro-survival function by serving as a cofactor for the HSP70 chaperone complex. Via a proteomic approach we identified and classified a set of pro-survival proteins controlled by this HSP70/BAG1 chaperone complex that contribute to the BAG1 anti-apoptotic phenotype. CONCLUSIONS: The small isoform of BAG1, BAG1S, in cooperation with the HSP70 chaperone complex, selectively mediates cell survival in MYC

Published
2019

37. A PERK–miR-211 axis suppresses circadian regulators and protein synthesis to promote cancer cell survival

Author

Bu, Yiwen, primary, Yoshida, Akihiro, additional, Chitnis, Nilesh, additional, Altman, Brian J., additional, Tameire, Feven, additional, Oran, Amanda, additional, Gennaro, Victoria, additional, Armeson, Kent E., additional, McMahon, Steven B., additional, Wertheim, Gerald B., additional, Dang, Chi V., additional, Ruggero, Davide, additional, Koumenis, Constantinos, additional, Fuchs, Serge Y., additional, and Diehl, J. Alan, additional

Published
2017
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38. Delayed Accumulation of H3K27me3 on Nascent DNA Is Essential for Recruitment of Transcription Factors at Early Stages of Stem Cell Differentiation

Author

Petruk, Svetlana, primary, Cai, Jingli, additional, Sussman, Robyn, additional, Sun, Guizhi, additional, Kovermann, Sina K., additional, Mariani, Samanta A., additional, Calabretta, Bruno, additional, McMahon, Steven B., additional, Brock, Hugh W., additional, Iacovitti, Lorraine, additional, and Mazo, Alexander, additional

Published
2017
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40. Multi-focal control of mitochondrial gene expression by oncogenic MYC provides potential therapeutic targets in cancer.

Author

Oran, Amanda R., Adams, Clare M., Zhang, Xiao-Yong, Gennaro, Victoria J., Pfeiffer, Harla K., Mellert, Hestia S., Seidel, Hans E., Mascioli, Kirsten, Kaplan, Jordan, Gaballa, Mahmoud R., Shen, Chen, Rigoutsos, Isidore, King, Michael P., Cotney, Justin L, Arnold, Jamie J., Sharma, Suresh D., Martinez-Outshoorn, Ubaldo E., Vakoc, Christopher R., Chodosh, Lewis A., Thompson, James E., Bradner, James E., Cameron, Craig E., Shadel, Gerald S., Eischen, Christine M., McMahon, Steven B., Oran, Amanda R., Adams, Clare M., Zhang, Xiao-Yong, Gennaro, Victoria J., Pfeiffer, Harla K., Mellert, Hestia S., Seidel, Hans E., Mascioli, Kirsten, Kaplan, Jordan, Gaballa, Mahmoud R., Shen, Chen, Rigoutsos, Isidore, King, Michael P., Cotney, Justin L, Arnold, Jamie J., Sharma, Suresh D., Martinez-Outshoorn, Ubaldo E., Vakoc, Christopher R., Chodosh, Lewis A., Thompson, James E., Bradner, James E., Cameron, Craig E., Shadel, Gerald S., Eischen, Christine M., and McMahon, Steven B.

Abstract

Despite ubiquitous activation in human cancer, essential downstream effector pathways of the MYC transcription factor have been difficult to define and target. Using a structure/function-based approach, we identified the mitochondrial RNA polymerase (POLRMT) locus as a critical downstream target of MYC. The multifunctional POLRMT enzyme controls mitochondrial gene expression, a process required both for mitochondrial function and mitochondrial biogenesis. We further demonstrate that inhibition of this newly defined MYC effector pathway causes robust and selective tumor cell apoptosis, via an acute, checkpoint-like mechanism linked to aberrant electron transport chain complex assembly and mitochondrial reactive oxygen species (ROS) production. Fortuitously, MYC-dependent tumor cell death can be induced by inhibiting the mitochondrial gene expression pathway using a variety of strategies, including treatment with FDA-approved antibiotics. In vivo studies using a mouse model of Burkitt's Lymphoma provide pre-clinical evidence that these antibiotics can successfully block progression of MYC-dependent tumors.

Published
2016

41. Multi-focal control of mitochondrial gene expression by oncogenic MYC provides potential therapeutic targets in cancer

Author

Oran, Amanda R., primary, Adams, Clare M., additional, Zhang, Xiao-yong, additional, Gennaro, Victoria J., additional, Pfeiffer, Harla K., additional, Mellert, Hestia S., additional, Seidel, Hans E., additional, Mascioli, Kirsten, additional, Kaplan, Jordan, additional, Gaballa, Mahmoud R., additional, Shen, Chen, additional, Rigoutsos, Isidore, additional, King, Michael P., additional, Cotney, Justin L., additional, Arnold, Jamie J., additional, Sharma, Suresh D., additional, Martinez-Outschoorn, Ubaldo E., additional, Vakoc, Christopher R., additional, Chodosh, Lewis A., additional, Thompson, James E., additional, Bradner, James E., additional, Cameron, Craig E., additional, Shadel, Gerald S., additional, Eischen, Christine M., additional, and McMahon, Steven B., additional

Published
2016
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44. Subtelomeric p53 binding prevents accumulation of DNA damage at human telomeres

Author

Tutton, Stephen, primary, Azzam, Greggory A, additional, Stong, Nicholas, additional, Vladimirova, Olga, additional, Wiedmer, Andreas, additional, Monteith, Jessica A, additional, Beishline, Kate, additional, Wang, Zhuo, additional, Deng, Zhong, additional, Riethman, Harold, additional, McMahon, Steven B, additional, Murphy, Maureen, additional, and Lieberman, Paul M, additional

Published
2015
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45. MYST protein acetyltransferase activity requires active site lysine autoacetylation

Author

Yuan, Hua, Rossetto, Dorine, Mellert, Hestia, Dang, Weiwei, Srinivasan, Madhusudan, Johnson, Jamel, Hodawadekar, Santosh, Ding, Emily C, Speicher, Kaye, Abshiru, Nebiyu, Perry, Rocco, Wu, Jiang, Yang, Chao, Zheng, Y George, Speicher, David W, Thibault, Pierre, Verreault, Alain, Johnson, F Bradley, Berger, Shelley L, Sternglanz, Rolf, McMahon, Steven B, Côté, Jacques, and Marmorstein, Ronen

Subjects
Histones, Binding Sites, Saccharomyces cerevisiae Proteins, Catalytic Domain, Lysine, Humans, Acetylation, Crystallography, X-Ray, Article, Histone Acetyltransferases
Abstract

The MYST protein lysine acetyltransferases are evolutionarily conserved throughout eukaryotes and acetylate proteins to regulate diverse biological processes including gene regulation, DNA repair, cell-cycle regulation, stem cell homeostasis and development. Here, we demonstrate that MYST protein acetyltransferase activity requires active site lysine autoacetylation. The X-ray crystal structures of yeast Esa1 (yEsa1/KAT5) bound to a bisubstrate H4K16CoA inhibitor and human MOF (hMOF/KAT8/MYST1) reveal that they are autoacetylated at a strictly conserved lysine residue in MYST proteins (yEsa1-K262 and hMOF-K274) in the enzyme active site. The structure of hMOF also shows partial occupancy of K274 in the unacetylated form, revealing that the side chain reorients to a position that engages the catalytic glutamate residue and would block cognate protein substrate binding. Consistent with the structural findings, we present mass spectrometry data and biochemical experiments to demonstrate that this lysine autoacetylation on yEsa1, hMOF and its yeast orthologue, ySas2 (KAT8) occurs in solution and is required for acetylation and protein substrate binding in vitro. We also show that this autoacetylation occurs in vivo and is required for the cellular functions of these MYST proteins. These findings provide an avenue for the autoposttranslational regulation of MYST proteins that is distinct from other acetyltransferases but draws similarities to the phosphoregulation of protein kinases.

Published
2011

48. Retraction Notice to: Nuclear Receptor Function Requires a TFTC-Type Histone Acetyl Transferase Complex

Author

Yanagisawa, Junn, primary, Kitagawa, Hirochika, additional, Yanagida, Mitsuaki, additional, Wada, Osamu, additional, Ogawa, Satoko, additional, Nakagomi, Madoka, additional, Oishi, Hajime, additional, Yamamoto, Yasuji, additional, Nagasawa, Hiromich, additional, McMahon, Steven B., additional, Cole, Michael D., additional, Tora, Laszlo, additional, Takahashi, Nobuhiro, additional, and Kato, Shigeaki, additional

Published
2014
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49. USP22 Regulates Oncogenic Signaling Pathways to Drive Lethal Cancer Progression

Author

Schrecengost, Randy S., primary, Dean, Jeffry L., additional, Goodwin, Jonathan F., additional, Schiewer, Matthew J., additional, Urban, Mark W., additional, Stanek, Timothy J., additional, Sussman, Robyn T., additional, Hicks, Jessica L., additional, Birbe, Ruth C., additional, Draganova-Tacheva, Rossitza A., additional, Visakorpi, Tapio, additional, DeMarzo, Angelo M., additional, McMahon, Steven B., additional, and Knudsen, Karen E., additional

Published
2014
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50. Acetylation of the cell-fate factor dachshund determines p53 binding and signaling modules in breast cancer.

Author

Chen, Ke, Wu, Kongming, Gormley, Michael, Ertel, Adam, Wang, Jing, Zhang, Wei, Zhou, Jie, Disante, Gabriele, Li, Zhiping, Rui, Hallgeir, Quong, Andrew A, McMahon, Steven B, Deng, Haiteng, Lisanti, Michael P, Wang, Chenguang, Pestell, Richard G, Chen, Ke, Wu, Kongming, Gormley, Michael, Ertel, Adam, Wang, Jing, Zhang, Wei, Zhou, Jie, Disante, Gabriele, Li, Zhiping, Rui, Hallgeir, Quong, Andrew A, McMahon, Steven B, Deng, Haiteng, Lisanti, Michael P, Wang, Chenguang, and Pestell, Richard G

Abstract

Breast cancer is a leading form of cancer in the world. The Drosophila Dac gene was cloned as an inhibitor of the hyperactive epidermal growth factor (EGFR), ellipse. Herein, endogenous DACH1 co-localized with p53 in a nuclear, extranucleolar compartment and bound to p53 in human breast cancer cell lines, p53 and DACH1 bound common genes in Chip-Seq. Full inhibition of breast cancer contact-independent growth by DACH1 required p53. The p53 breast cancer mutants R248Q and R273H, evaded DACH1 binding. DACH1 phosphorylation at serine residue (S439) inhibited p53 binding and phosphorylation at p53 amino-terminal sites (S15, S20) enhanced DACH1 binding. DACH1 binding to p53 was inhibited by NAD-dependent deacetylation via DACH1 K628. DACH1 repressed p21CIP1 and induced RAD51, an association found in basal breast cancer. DACH1 inhibits breast cancer cellular growth in an NAD and p53-dependent manner through direct protein-protein association.

Published
2013

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