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2. Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis.

Author

Yoshida, Soichiro, Tsutsumi, Shinji, Muhlebach, Guillaume, Sourbier, Carole, Lee, Min-Jung, Lee, Sunmin, Vartholomaiou, Evangelia, Tatokoro, Manabu, Beebe, Kristin, Miyajima, Naoto, Mohney, Robert, Chen, Yang, Hasumi, Hisashi, Xu, Wanping, Fukushima, Hiroshi, Koga, Fumitaka, Kihara, Kazunori, Trepel, Jane, Picard, Didier, Neckers, Leonard, and Nakamura, Ken

Subjects
Animals, COS Cells, CSK Tyrosine-Protein Kinase, Chlorocebus aethiops, Glycolysis, HSP90 Heat-Shock Proteins, HeLa Cells, Humans, Intracellular Signaling Peptides and Proteins, Mice, Mice, Knockout, Mitochondria, Mitochondrial Proteins, Molecular Chaperones, NIH 3T3 Cells, Neoplasm Invasiveness, Oxidative Phosphorylation, RNA Interference, Transfection, src-Family Kinases
Abstract

TRAP1 (TNF receptor-associated protein), a member of the HSP90 chaperone family, is found predominantly in mitochondria. TRAP1 is broadly considered to be an anticancer molecular target. However, current inhibitors cannot distinguish between HSP90 and TRAP1, making their utility as probes of TRAP1-specific function questionable. Some cancers express less TRAP1 than do their normal tissue counterparts, suggesting that TRAP1 function in mitochondria of normal and transformed cells is more complex than previously appreciated. We have used TRAP1-null cells and transient TRAP1 silencing/overexpression to show that TRAP1 regulates a metabolic switch between oxidative phosphorylation and aerobic glycolysis in immortalized mouse fibroblasts and in human tumor cells. TRAP1-deficiency promotes an increase in mitochondrial respiration and fatty acid oxidation, and in cellular accumulation of tricarboxylic acid cycle intermediates, ATP and reactive oxygen species. At the same time, glucose metabolism is suppressed. TRAP1-deficient cells also display strikingly enhanced invasiveness. TRAP1 interaction with and regulation of mitochondrial c-Src provide a mechanistic basis for these phenotypes. Taken together with the observation that TRAP1 expression is inversely correlated with tumor grade in several cancers, these data suggest that, in some settings, this mitochondrial molecular chaperone may act as a tumor suppressor.

Published
2013

5. Supplementary Figure 4 from The HSP90 Inhibitor Ganetespib Synergizes with the MET Kinase Inhibitor Crizotinib in both Crizotinib-Sensitive and -Resistant MET-Driven Tumor Models

Author

Miyajima, Naoto, primary, Tsutsumi, Shinji, primary, Sourbier, Carole, primary, Beebe, Kristin, primary, Mollapour, Mehdi, primary, Rivas, Candy, primary, Yoshida, Soichiro, primary, Trepel, Jane B., primary, Huang, Ying, primary, Tatokoro, Manabu, primary, Shinohara, Nobuo, primary, Nonomura, Katsuya, primary, and Neckers, Len, primary

Published
2023
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6. Supplementary Figure 1 from The HSP90 Inhibitor Ganetespib Synergizes with the MET Kinase Inhibitor Crizotinib in both Crizotinib-Sensitive and -Resistant MET-Driven Tumor Models

Author

Miyajima, Naoto, primary, Tsutsumi, Shinji, primary, Sourbier, Carole, primary, Beebe, Kristin, primary, Mollapour, Mehdi, primary, Rivas, Candy, primary, Yoshida, Soichiro, primary, Trepel, Jane B., primary, Huang, Ying, primary, Tatokoro, Manabu, primary, Shinohara, Nobuo, primary, Nonomura, Katsuya, primary, and Neckers, Len, primary

Published
2023
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7. Supplementary Figure Legend from The HSP90 Inhibitor Ganetespib Synergizes with the MET Kinase Inhibitor Crizotinib in both Crizotinib-Sensitive and -Resistant MET-Driven Tumor Models

Author

Miyajima, Naoto, primary, Tsutsumi, Shinji, primary, Sourbier, Carole, primary, Beebe, Kristin, primary, Mollapour, Mehdi, primary, Rivas, Candy, primary, Yoshida, Soichiro, primary, Trepel, Jane B., primary, Huang, Ying, primary, Tatokoro, Manabu, primary, Shinohara, Nobuo, primary, Nonomura, Katsuya, primary, and Neckers, Len, primary

Published
2023
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8. Supplementary Table 1 from The HSP90 Inhibitor Ganetespib Synergizes with the MET Kinase Inhibitor Crizotinib in both Crizotinib-Sensitive and -Resistant MET-Driven Tumor Models

Author

Miyajima, Naoto, primary, Tsutsumi, Shinji, primary, Sourbier, Carole, primary, Beebe, Kristin, primary, Mollapour, Mehdi, primary, Rivas, Candy, primary, Yoshida, Soichiro, primary, Trepel, Jane B., primary, Huang, Ying, primary, Tatokoro, Manabu, primary, Shinohara, Nobuo, primary, Nonomura, Katsuya, primary, and Neckers, Len, primary

Published
2023
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9. Supplementary Figure 3 from The HSP90 Inhibitor Ganetespib Synergizes with the MET Kinase Inhibitor Crizotinib in both Crizotinib-Sensitive and -Resistant MET-Driven Tumor Models

Author

Miyajima, Naoto, primary, Tsutsumi, Shinji, primary, Sourbier, Carole, primary, Beebe, Kristin, primary, Mollapour, Mehdi, primary, Rivas, Candy, primary, Yoshida, Soichiro, primary, Trepel, Jane B., primary, Huang, Ying, primary, Tatokoro, Manabu, primary, Shinohara, Nobuo, primary, Nonomura, Katsuya, primary, and Neckers, Len, primary

Published
2023
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10. Data from The HSP90 Inhibitor Ganetespib Synergizes with the MET Kinase Inhibitor Crizotinib in both Crizotinib-Sensitive and -Resistant MET-Driven Tumor Models

Author

Miyajima, Naoto, primary, Tsutsumi, Shinji, primary, Sourbier, Carole, primary, Beebe, Kristin, primary, Mollapour, Mehdi, primary, Rivas, Candy, primary, Yoshida, Soichiro, primary, Trepel, Jane B., primary, Huang, Ying, primary, Tatokoro, Manabu, primary, Shinohara, Nobuo, primary, Nonomura, Katsuya, primary, and Neckers, Len, primary

Published
2023
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11. Supplementary Figure 5 from The HSP90 Inhibitor Ganetespib Synergizes with the MET Kinase Inhibitor Crizotinib in both Crizotinib-Sensitive and -Resistant MET-Driven Tumor Models

Author

Miyajima, Naoto, primary, Tsutsumi, Shinji, primary, Sourbier, Carole, primary, Beebe, Kristin, primary, Mollapour, Mehdi, primary, Rivas, Candy, primary, Yoshida, Soichiro, primary, Trepel, Jane B., primary, Huang, Ying, primary, Tatokoro, Manabu, primary, Shinohara, Nobuo, primary, Nonomura, Katsuya, primary, and Neckers, Len, primary

Published
2023
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12. Supplementary Table 2 from The HSP90 Inhibitor Ganetespib Synergizes with the MET Kinase Inhibitor Crizotinib in both Crizotinib-Sensitive and -Resistant MET-Driven Tumor Models

Author

Miyajima, Naoto, primary, Tsutsumi, Shinji, primary, Sourbier, Carole, primary, Beebe, Kristin, primary, Mollapour, Mehdi, primary, Rivas, Candy, primary, Yoshida, Soichiro, primary, Trepel, Jane B., primary, Huang, Ying, primary, Tatokoro, Manabu, primary, Shinohara, Nobuo, primary, Nonomura, Katsuya, primary, and Neckers, Len, primary

Published
2023
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13. Supplementary Figure 2 from The HSP90 Inhibitor Ganetespib Synergizes with the MET Kinase Inhibitor Crizotinib in both Crizotinib-Sensitive and -Resistant MET-Driven Tumor Models

Author

Miyajima, Naoto, primary, Tsutsumi, Shinji, primary, Sourbier, Carole, primary, Beebe, Kristin, primary, Mollapour, Mehdi, primary, Rivas, Candy, primary, Yoshida, Soichiro, primary, Trepel, Jane B., primary, Huang, Ying, primary, Tatokoro, Manabu, primary, Shinohara, Nobuo, primary, Nonomura, Katsuya, primary, and Neckers, Len, primary

Published
2023
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45. Heat shock protein 90 targeting therapy

Author

Tatokoro, Manabu, Koga, Fumitaka, Yoshida, Soichiro, and Kihara, Kazunori

Subjects
polycyclic compounds, cancer, bladder cancer, clinical trial, Hsp90 inhibitor
Abstract

Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that plays a role in stabilizing and activating more than 200 client proteins. It is required for the stability and function of numerous oncogenic signaling proteins that determine the hallmarks of cancer. Since the initial discovery of the first Hsp90 inhibitor in the 1970s, multiple phase II and III clinical trials of several Hsp90 inhibitors have been undertaken. This review provides an overview of the current status on clinical trials of Hsp90 inhibitors and future perspectives on novel anticancer strategies using Hsp90 inhibitors., EXCLI Journal ; Vol. 14, 2015

Published
2015

46. Heat shock protein 90 targeting therapy: state of the art and future perspective

Author

Tatokoro, Manabu, Koga, Fumitaka, Yoshida, Soichiro, and Kihara, Kazunori

Subjects
polycyclic compounds, cancer, bladder cancer, clinical trial, Hsp90 inhibitor
Abstract

Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that plays a role in stabilizing and activating more than 200 client proteins. It is required for the stability and function of numerous oncogenic signaling proteins that determine the hallmarks of cancer. Since the initial discovery of the first Hsp90 inhibitor in the 1970s, multiple phase II and III clinical trials of several Hsp90 inhibitors have been undertaken. This review provides an overview of the current status on clinical trials of Hsp90 inhibitors and future perspectives on novel anticancer strategies using Hsp90 inhibitors., EXCLI Journal; 14:Doc48; ISSN 1611-2156

Published
2015
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47. Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants

Author

Prince, Thomas L., primary, Kijima, Toshiki, additional, Tatokoro, Manabu, additional, Lee, Sunmin, additional, Tsutsumi, Shinji, additional, Yim, Kendrick, additional, Rivas, Candy, additional, Alarcon, Sylvia, additional, Schwartz, Harvey, additional, Khamit-Kush, Kofi, additional, Scroggins, Bradley T., additional, Beebe, Kristin, additional, Trepel, Jane B., additional, and Neckers, Len, additional

Published
2015
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50. Diagnostic performance and safety of a three‐dimensional 14‐core systematic biopsy method

Author

Takeshita, Hideki, primary, Kawakami, Satoru, additional, Numao, Noboru, additional, Sakura, Mizuaki, additional, Tatokoro, Manabu, additional, Yamamoto, Shinya, additional, Kijima, Toshiki, additional, Komai, Yoshinobu, additional, Saito, Kazutaka, additional, Koga, Fumitaka, additional, Fujii, Yasuhisa, additional, Fukui, Iwao, additional, and Kihara, Kazunori, additional

Published
2014
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