References
- Welch, W. J. (1991) The role of heat-shock proteins as molecular chaperones. Curr. Opin. Cell. Biol. 3, 1033-1038. https://doi.org/10.1016/0955-0674(91)90125-I
- Hightower, L. E. (1991) Heat shock, stress proteins, chaperones, and proteotoxicity. Cell 66, 191-197. https://doi.org/10.1016/0092-8674(91)90611-2
- Whitesell, L. and Lindquist, S. L. (2005) HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 5, 761-772. https://doi.org/10.1038/nrc1716
- Pearl, L. H. and Prodromou, C. (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271-294. https://doi.org/10.1146/annurev.biochem.75.103004.142738
- Feder, M. E. and Hofmann, G. E. (1999) Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol. 61, 243-282. https://doi.org/10.1146/annurev.physiol.61.1.243
- Taipale, M., Jarosz, D. F. and Lindquist, S. (2010) HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell. Biol. 11, 515-528. https://doi.org/10.1038/nrm2918
- Bagatell, R. and Whitesell, L. (2004) Altered Hsp90 function in cancer: a unique therapeutic opportunity. Mol. Cancer Ther. 3, 1021-1030. https://doi.org/10.4161/cbt.3.10.1142
- Blagg, B. S. and Kerr, T. D. (2006) Hsp90 inhibitors: small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation. Med. Res. Rev. 26, 310-338. https://doi.org/10.1002/med.20052
- Solit, D. B. and Chiosis, G. (2008) Development and application of Hsp90 inhibitors. Drug Discov. Today 13, 38-43. https://doi.org/10.1016/j.drudis.2007.10.007
- Biamonte, M. A., Van de Water, R., Arndt, J. W., Scannevin, R. H., Perret, D. and Lee, W. C. (2010) Heat shock protein 90: inhibitors in clinical trials. J. Med. Chem. 53, 3-17. https://doi.org/10.1021/jm9004708
- Chen, B., Piel, W. H., Gui, L., Bruford, E. and Monteiro, A. (2005) The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics. 86, 627-637. https://doi.org/10.1016/j.ygeno.2005.08.012
- Song, H. Y., Dunbar, J. D., Zhang, Y. X., Guo, D. and Donner, D. B. (1995) Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 270, 3574-3581. https://doi.org/10.1074/jbc.270.8.3574
- Chen, C. F., Chen, Y., Dai, K., Chen, P. L., Riley, D. J. and Lee, W. H. (1996) A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock. Mol. Cell. Biol. 16, 4691-4699. https://doi.org/10.1128/MCB.16.9.4691
- Felts, S. J., Owen, B. A., Nguyen, P., Trepel, J., Donner, D. B. and Toft, D. O. (2000) The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J. Biol. Chem. 275, 3305-3312. https://doi.org/10.1074/jbc.275.5.3305
- Leskovar, A., Wegele, H., Werbeck, N. D., Buchner, J. and Reinstein, J. (2008) The ATPase cycle of the mitochondrial Hsp90 analog Trap1. J. Biol. Chem. 283, 11677-11688. https://doi.org/10.1074/jbc.M709516200
- Kang, B. H., Plescia, J., Dohi, T., Rosa, J., Doxsey, S. J. and Altieri, D. C. (2007) Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network. Cell 131, 257-270. https://doi.org/10.1016/j.cell.2007.08.028
- Kang, B. H., Plescia, J., Song, H. Y., Meli, M., Colombo, G., Beebe, K., Scroggins, B., Neckers, L. and Altieri, D. C. (2009) Combinatorial drug design targeting multiple cancer signaling networks controlled by mitochondrial Hsp90. J. Clin. Invest. 119, 454-464. https://doi.org/10.1172/JCI37613
- Schleiff, E. and Becker, T. (2011) Common ground for protein translocation: access control for mitochondria and chloroplasts. Nat. Rev. Mol. Cell. Biol. 12, 48-59. https://doi.org/10.1038/nrm3027
- Simmons, A. D., Musy, M. M., Lopes, C. S., Hwang, L. Y., Yang, Y. P. and Lovett, M. (1999) A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses. Hum. Mol. Genet. 8, 2155-2164. https://doi.org/10.1093/hmg/8.12.2155
- Deocaris, C. C., Kaul, S. C. and Wadhwa, R. (2006) On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60. Cell Stress Chaperones 11, 116-128. https://doi.org/10.1379/CSC-144R.1
- Patten, D. A., Germain, M., Kelly, M. A. and Slack, R. S. (2010) Reactive oxygen species: stuck in the middle of neurodegeneration. J. Alzheimers Dis. 20(Suppl 2), S357-367. https://doi.org/10.3233/JAD-2010-100498
- Sotgia, F., Martinez-Outschoorn, U. E. and Lisanti, M. P. (2011) Mitochondrial oxidative stress drives tumor progression and metastasis: should we use antioxidants as a key component of cancer treatment and prevention? BMC Med. 9, 62. https://doi.org/10.1186/1741-7015-9-62
- Masuda, Y., Shima, G., Aiuchi, T., Horie, M., Hori, K., Nakajo, S., Kajimoto, S., Shibayama-Imazu, T. and Nakaya, K. (2004) Involvement of tumor necrosis factor receptor- associated protein 1 (TRAP1) in apoptosis induced by beta-hydroxyisovalerylshikonin. J. Biol. Chem. 279, 42503-42515. https://doi.org/10.1074/jbc.M404256200
- Montesano Gesualdi, N., Chirico, G., Pirozzi, G., Costantino, E., Landriscina, M. and Esposito, F. (2007) Tumor necrosis factor-associated protein 1 (TRAP-1) protects cells from oxidative stress and apoptosis. Stress 10, 342-350. https://doi.org/10.1080/10253890701314863
- Hua, G., Zhang, Q. and Fan, Z. (2007) Heat shock protein 75 (TRAP1) antagonizes reactive oxygen species generation and protects cells from granzyme M-mediated apoptosis. J. Biol. Chem. 282, 20553-20560. https://doi.org/10.1074/jbc.M703196200
- Im, C. N., Lee, J. S., Zheng, Y. and Seo, J. S. (2007) Iron chelation study in a normal human hepatocyte cell line suggests that tumor necrosis factor receptor-associated protein 1 (TRAP1) regulates production of reactive oxygen species. J. Cell. Biochem. 100, 474-486. https://doi.org/10.1002/jcb.21064
- Siegelin, M. D., Dohi, T., Raskett, C. M., Orlowski, G. M., Powers, C. M., Gilbert, C. A., Ross, A. H., Plescia, J. and Altieri, D. C. (2011) Exploiting the mitochondrial unfolded protein response for cancer therapy in mice and human cells. J. Clin. Invest. 121, 1349-1360. https://doi.org/10.1172/JCI44855
- Mattson, M. P. and Kroemer, G. (2003) Mitochondria in cell death: novel targets for neuroprotection and cardioprotection. Trends Mol. Med. 9, 196-205. https://doi.org/10.1016/S1471-4914(03)00046-7
- Kroemer, G., Galluzzi, L. and Brenner, C. (2007) Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 87, 99-163. https://doi.org/10.1152/physrev.00013.2006
- Tsujimoto, Y., Nakagawa, T. and Shimizu, S. (2006) Mitochondrial membrane permeability transition and cell death. Biochim. Biophys. Acta. 1757, 1297-1300. https://doi.org/10.1016/j.bbabio.2006.03.017
- Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J. and Molkentin, J. D. (2007) Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nat. Cell. Biol. 9, 550-555. https://doi.org/10.1038/ncb1575
- Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R. and Wallace, D. C. (2004) The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature 427, 461-465. https://doi.org/10.1038/nature02229
- Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A. and Bernardi, P. (2005) Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D. J. Biol. Chem. 280, 18558-18561. https://doi.org/10.1074/jbc.C500089200
- Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., Robbins, J. and Molkentin, J. D. (2005) Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434, 658-662. https://doi.org/10.1038/nature03434
- Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T. and Tsujimoto, Y. (2005) Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434, 652-658. https://doi.org/10.1038/nature03317
- Johnson, N., Khan, A., Virji, S., Ward, J. M. and Crompton, M. (1999) Import and processing of heart mitochondrial cyclophilin D. Eur. J. Biochem. 263, 353-359. https://doi.org/10.1046/j.1432-1327.1999.00490.x
- Kang, B. H. and Altieri, D. C. (2009) Compartmentalized cancer drug discovery targeting mitochondrial Hsp90 chaperones. Oncogene 28, 3681-3688. https://doi.org/10.1038/onc.2009.227
- Coller, H. A., Grandori, C., Tamayo, P., Colbert, T., Lander, E. S., Eisenman, R. N. and Golub, T. R. (2000) Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion. Proc. Natl. Acad. Sci. U.S.A. 97, 3260-3265. https://doi.org/10.1073/pnas.97.7.3260
- Putz, S. M., Vogiatzi, F., Stiewe, T. and Sickmann, A. (2010) Malignant transformation in a defined genetic background: proteome changes displayed by 2D-PAGE. Mol. Cancer 9, 254. https://doi.org/10.1186/1476-4598-9-254
- Leav, I., Plescia, J., Goel, H. L., Li, J., Jiang, Z., Cohen, R. J., Languino, L. R. and Altieri, D. C. (2010) Cytoprotective mitochondrial chaperone TRAP-1 as a novel molecular target in localized and metastatic prostate cancer. Am. J. Pathol. 176, 393-401. https://doi.org/10.2353/ajpath.2010.090521
- Kang, B. H., Xia, F., Pop, R., Dohi, T., Socolovsky, M. and Altieri, D. C. (2011) Developmental control of apoptosis by the immunophilin aryl hydrocarbon receptor-interacting protein (AIP) involves mitochondrial import of the survivin protein. J. Biol. Chem. 286, 16758-16767. https://doi.org/10.1074/jbc.M110.210120
- Pridgeon, J. W., Olzmann, J. A., Chin, L. S. and Li, L. (2007) PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol. 5, e172. https://doi.org/10.1371/journal.pbio.0050172
- Trepel, J., Mollapour, M., Giaccone, G. and Neckers, L. (2010) Targeting the dynamic HSP90 complex in cancer. Nat. Rev. Cancer 10, 537-549. https://doi.org/10.1038/nrc2887
- Gatenby, R. A. and Gillies, R. J. (2004) Why do cancers have high aerobic glycolysis? Nat. Rev. Cancer 4, 891-899. https://doi.org/10.1038/nrc1478
- Costantino, E., Maddalena, F., Calise, S., Piscazzi, A., Tirino, V., Fersini, A., Ambrosi, A., Neri, V., Esposito, F. and Landriscina, M. (2009) TRAP1, a novel mitochondrial chaperone responsible for multi-drug resistance and protection from apoptosis in human colorectal carcinoma cells. Cancer Lett. 279, 39-46. https://doi.org/10.1016/j.canlet.2009.01.018
- Liu, D., Hu, J., Agorreta, J., Cesario, A., Zhang, Y., Harris, A. L., Gatter, K. and Pezzella, F. (2010) Tumor necrosis factor receptor-associated protein 1(TRAP1) regulates genes involved in cell cycle and metastases. Cancer Lett. 296, 194-205. https://doi.org/10.1016/j.canlet.2010.04.017
- Takemoto, K., Miyata, S., Takamura, H., Katayama, T. and Tohyama, M. (2011) Mitochondrial TRAP1 regulates the unfolded protein response in the endoplasmic reticulum. Neurochem. Int. 58, 880-887. https://doi.org/10.1016/j.neuint.2011.02.015
- Kang, B. H., Siegelin, M. D., Plescia, J., Raskett, C. M., Garlick, D. S., Dohi, T., Lian, J. B., Stein, G. S., Languino, L. R. and Altieri, D. C. (2010) Preclinical characterization of mitochondria-targeted small molecule hsp90 inhibitors, gamitrinibs, in advanced prostate cancer. Clin. Cancer Res. 16, 4779-4788. https://doi.org/10.1158/1078-0432.CCR-10-1818
- Kang, B. H., Tavecchio, M., Goel, H. L., Hsieh, C. C., Garlick, D. S., Raskett, C. M., Lian, J. B., Stein, G. S., Languino, L. R. and Altieri, D. C. (2011) Targeted inhibition of mitochondrial Hsp90 suppresses localised and metastatic prostate cancer growth in a genetic mouse model of disease. Br. J. Cancer 104, 629-634. https://doi.org/10.1038/bjc.2011.9
- Plescia, J., Salz, W., Xia, F., Pennati, M., Zaffaroni, N., Daidone, M. G., Meli, M., Dohi, T., Fortugno, P., Nefedova, Y., Gabrilovich, D. I., Colombo, G. and Altieri, D. C. (2005) Rational design of shepherdin, a novel anticancer agent. Cancer Cell 7, 457-468. https://doi.org/10.1016/j.ccr.2005.03.035
- Fulda, S., Galluzzi, L. and Kroemer, G. (2010) Targeting mitochondria for cancer therapy. Nat. Rev. Drug Discov. 9, 447-464. https://doi.org/10.1038/nrd3137
Cited by
- TRAP1 role in endoplasmic reticulum stress protection favors resistance to anthracyclins in breast carcinoma cells vol.44, pp.2, 2014, https://doi.org/10.3892/ijo.2013.2199
- Tumor Necrosis Factor Receptor-associated Protein 1 (TRAP1) Mutation and TRAP1 Inhibitor Gamitrinib-triphenylphosphonium (G-TPP) Induce a Forkhead Box O (FOXO)-dependent Cell Protective Signal from Mitochondria vol.291, pp.4, 2016, https://doi.org/10.1074/jbc.M115.656934
- Past, present, and emerging roles of mitochondrial heat shock protein TRAP1 in the metabolism and regulation of cancer stem cells vol.21, pp.4, 2016, https://doi.org/10.1007/s12192-016-0687-3
- Mitochondria-Targeted Triphenylphosphonium-Based Compounds: Syntheses, Mechanisms of Action, and Therapeutic and Diagnostic Applications vol.117, pp.15, 2017, https://doi.org/10.1021/acs.chemrev.7b00042
- Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis Mechanism vol.53, pp.2, 2014, https://doi.org/10.1016/j.molcel.2013.12.023
- Acute toxicity of functionalized single wall carbon nanotubes: A biochemical, histopathologic and proteomics approach vol.275, 2017, https://doi.org/10.1016/j.cbi.2017.08.004
- Mitochondrial Hsp90s suppress calcium-mediated stress signals propagating from mitochondria to the ER in cancer cells vol.13, pp.1, 2014, https://doi.org/10.1186/1476-4598-13-148
- The Hsp90 inhibitor SNX-2112, induces apoptosis in multidrug resistant K562/ADR cells through suppression of Akt/NF-κB and disruption of mitochondria-dependent pathways vol.205, pp.1, 2013, https://doi.org/10.1016/j.cbi.2013.06.007
- The Chaperone TRAP1 As a Modulator of the Mitochondrial Adaptations in Cancer Cells vol.7, 2017, https://doi.org/10.3389/fonc.2017.00058
- TRAP1-dependent regulation of p70S6K is involved in the attenuation of protein synthesis and cell migration: Relevance in human colorectal tumors vol.8, pp.8, 2014, https://doi.org/10.1016/j.molonc.2014.06.003
- Chaperoning mitochondrial permeability transition: regulation of transition pore complex by a J-protein, DnaJC15 vol.5, pp.3, 2014, https://doi.org/10.1038/cddis.2014.72
- The Establishment of Tumor Necrosis Factor Receptor-associated Protein1 (TRAP1) Transgenic Mice and Severe Fat Accumulation in the Liver of TRAP1 Mice during Liver Regeneration vol.5, pp.4, 2013, https://doi.org/10.4051/ibc.2013.5.4.0009
- Development of a Mitochondria-Targeted Hsp90 Inhibitor Based on the Crystal Structures of Human TRAP1 vol.137, pp.13, 2015, https://doi.org/10.1021/ja511893n
- Endoplasmic Reticulum-Localized Iridium(III) Complexes as Efficient Photodynamic Therapy Agents via Protein Modifications vol.138, pp.34, 2016, https://doi.org/10.1021/jacs.6b05302
- Cross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and Disease vol.2016, 2016, https://doi.org/10.1155/2016/4587691
- Crystallization and preliminary X-ray diffraction analysis of Trap1 complexed with Hsp90 inhibitors vol.70, pp.12, 2014, https://doi.org/10.1107/S2053230X14024959
- Mitochondrial dynamics: biology and therapy in lung cancer vol.23, pp.5, 2014, https://doi.org/10.1517/13543784.2014.899350
- Paralog Specificity Determines Subcellular Distribution, Action Mechanism, and Anticancer Activity of TRAP1 Inhibitors vol.60, pp.17, 2017, https://doi.org/10.1021/acs.jmedchem.7b00978
- A Novel In Vitro CypD-Mediated p53 Aggregation Assay Suggests a Model for Mitochondrial Permeability Transition by Chaperone Systems vol.428, pp.20, 2016, https://doi.org/10.1016/j.jmb.2016.08.001
- Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis vol.110, pp.17, 2013, https://doi.org/10.1073/pnas.1220659110
- Utilization of the cellular stress response to sensitize cancer cells to TRAIL-mediated apoptosis vol.16, pp.8, 2012, https://doi.org/10.1517/14728222.2012.703655
- Clinicopathologic significance of TRAP1 expression in colorectal cancer: a large scale study of human colorectal adenocarcinoma tissues vol.12, pp.1, 2017, https://doi.org/10.1186/s13000-017-0598-3
- Mitochondria malfunctions as mediators of stem-cells’ related carcinogenesis: A hypothesis that supports the highly conserved profile of carcinogenesis vol.80, pp.1, 2013, https://doi.org/10.1016/j.mehy.2012.10.002
- Mitochondrial Channels: Ion Fluxes and More vol.94, pp.2, 2014, https://doi.org/10.1152/physrev.00021.2013
- The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease vol.19, pp.9, 2018, https://doi.org/10.3390/ijms19092560