메뉴 건너뛰기




Volumn 45, Issue 3, 2014, Pages 969-977

TRAP1 revisited: Novel localizations and functions of a 'next-generation' biomarker (Review)

Author keywords

Anticancer agents; Apoptosis; Heat shock proteins; Protein quality control; TRAP1; Tumor biomarker

Indexed keywords

ALPHA SYNUCLEIN; ANTINEOPLASTIC AGENT; BIOLOGICAL MARKER; HEAT SHOCK PROTEIN; MITOCHONDRIAL PROTEIN; OXIDIZING AGENT; PARKIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REGULATOR PROTEIN; SUCCINATE DEHYDROGENASE; SUCCINATE DEHYDROGENASE (UBIQUINONE); TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 1; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG; HEAT SHOCK PROTEIN 90; TRAP1 PROTEIN, HUMAN;

EID: 84904396628     PISSN: 10196439     EISSN: 17912423     Source Type: Journal    
DOI: 10.3892/ijo.2014.2530     Document Type: Review
Times cited : (47)

References (47)
  • 1
    • 0028954475 scopus 로고
    • Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
    • Song HY, Dunbar JD, Zhang YX, Guo D and Donner DB: Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J Biol Chem 270: 3574-3581, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 3574-3581
    • Song, H.Y.1    Dunbar, J.D.2    Zhang, Y.X.3    Guo, D.4    Donner, D.B.5
  • 2
    • 0029760873 scopus 로고    scopus 로고
    • A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock
    • Chen CF, Chen Y, Dai K, Chen PL, Riley DJ and Lee WH: 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, 1996. (Pubitemid 26272122)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.9 , pp. 4691-4699
    • Chen, C.-F.1    Chen, Y.2    Dai, K.3    Chen, P.-L.4    Riley, D.J.5    Lee, W.-H.6
  • 4
    • 28644443855 scopus 로고    scopus 로고
    • The HSP90 family of genes in the human genome: Insights into their divergence and evolution
    • DOI 10.1016/j.ygeno.2005.08.012, PII S0888754305002430
    • Chen B, Piel WH, Gui L, Bruford E and Monteiro A: The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics 86: 627-637, 2005. (Pubitemid 41752943)
    • (2005) Genomics , vol.86 , Issue.6 , pp. 627-637
    • Chen, B.1    Piel, W.H.2    Gui, L.3    Bruford, E.4    Monteiro, A.5
  • 5
    • 0034603178 scopus 로고    scopus 로고
    • The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties
    • DOI 10.1074/jbc.275.5.3305
    • Felts SJ, Owen BA, Nguyen P, Trepel J, Donner DB and Toft DO: The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J Biol Chem 275: 3305-3312, 2000. (Pubitemid 30083032)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.5 , pp. 3305-3312
    • Felts, S.J.1    Owen, B.A.L.2    Nguyen, P.3    Trepel, J.4    Donner, D.B.5    Toft, D.O.6
  • 6
    • 0034633963 scopus 로고    scopus 로고
    • Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites
    • Cechetto JD and Gupta RS: Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites. Exp Cell Res 260: 30-39, 2000.
    • (2000) Exp Cell Res , vol.260 , pp. 30-39
    • Cechetto, J.D.1    Gupta, R.S.2
  • 7
    • 35348887850 scopus 로고    scopus 로고
    • Regulation of Tumor Cell Mitochondrial Homeostasis by an Organelle-Specific Hsp90 Chaperone Network
    • DOI 10.1016/j.cell.2007.08.028, PII S0092867407010914
    • Kang BH, Plescia J, Dohi T, Rosa J, Doxsey SJ and Altieri DC: Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network. Cell 131: 257-270, 2007. (Pubitemid 47576138)
    • (2007) Cell , vol.131 , Issue.2 , pp. 257-270
    • Kang, B.H.1    Plescia, J.2    Dohi, T.3    Rosa, J.4    Doxsey, S.J.5    Altieri, D.C.6
  • 9
    • 36248980938 scopus 로고    scopus 로고
    • Tumor necrosis factor-associated protein 1 (TRAP-1) protects cells from oxidative stress and apoptosis
    • DOI 10.1080/10253890701314863, PII 779717076
    • Montesano Gesualdi N, Chirico G, Pirozzi G, Costantino E, Landriscina M and Esposito F: Tumor necrosis factor-associated protein 1 (TRAP-1) protects cells from oxidative stress and apoptosis. Stress 10: 342-350, 2007. (Pubitemid 350125789)
    • (2007) Stress , vol.10 , Issue.4 , pp. 342-350
    • Gesualdi, N.M.1    Chirico, G.2    Pirozzi, G.3    Costantino, E.4    Landriscina, M.5    Esposito, F.6
  • 11
    • 78549293327 scopus 로고    scopus 로고
    • Heat shock protein 60 regulation of the mitochondrial permeability transition pore in tumor cells
    • Ghosh JC, Siegelin MD, Dohi T and Altieri DC: Heat shock protein 60 regulation of the mitochondrial permeability transition pore in tumor cells. Cancer Res 70: 8988-8993, 2010.
    • (2010) Cancer Res , vol.70 , pp. 8988-8993
    • Ghosh, J.C.1    Siegelin, M.D.2    Dohi, T.3    Altieri, D.C.4
  • 12
    • 77952671613 scopus 로고    scopus 로고
    • Signal transduction to the permeability transition pore
    • Rasola A, Sciacovelli M, Pantic B and Bernardi P: Signal transduction to the permeability transition pore. FEBS Lett 584: 1989-1996, 2010.
    • (2010) FEBS Lett , vol.584 , pp. 1989-1996
    • Rasola, A.1    Sciacovelli, M.2    Pantic, B.3    Bernardi, P.4
  • 13
    • 84879605590 scopus 로고    scopus 로고
    • Hsp90 regulation of mitochondrial protein folding: From organelle integrity to cellular homeostasis
    • Altieri DC: Hsp90 regulation of mitochondrial protein folding: from organelle integrity to cellular homeostasis. Cell Mol Life Sci 70: 2463-2472, 2013.
    • (2013) Cell Mol Life Sci , vol.70 , pp. 2463-2472
    • Altieri, D.C.1
  • 14
    • 82955161663 scopus 로고    scopus 로고
    • Concomitant inhibition of HSP90, its mitochondrial localized homologue TRAP1 and HSP27 by green tea in pancreatic cancer HPAF-II cells
    • Zhang L, Pang E, Loo RR, Rao J, Go VL, Loo JA and Lu QY: Concomitant inhibition of HSP90, its mitochondrial localized homologue TRAP1 and HSP27 by green tea in pancreatic cancer HPAF-II cells. Proteomics 11: 4638-4647, 2011.
    • (2011) Proteomics , vol.11 , pp. 4638-4647
    • Zhang, L.1    Pang, E.2    Loo, R.R.3    Rao, J.4    Go, V.L.5    Loo, J.A.6    Lu, Q.Y.7
  • 15
    • 84873736763 scopus 로고    scopus 로고
    • Correlation between mitochondrial TRAP-1 expression and lymph node metastasis in colorectal cancer
    • Gao JY, Song BR, Peng JJ and Lu YM: Correlation between mitochondrial TRAP-1 expression and lymph node metastasis in colorectal cancer. World J Gastroenterol 18: 5965-5971, 2012.
    • (2012) World J Gastroenterol , vol.18 , pp. 5965-5971
    • Gao, J.Y.1    Song, B.R.2    Peng, J.J.3    Lu, Y.M.4
  • 16
    • 84893921265 scopus 로고    scopus 로고
    • Combination of TRAP1 and ERCC1 expression predicts clinical outcomes in metastatic colorectal cancer treated with oxaliplatin/5-fluorouracil
    • Han JJ, Baek SK, Lee JJ, Kim GY, Kim SY and Lee SH: Combination of TRAP1 and ERCC1 expression predicts clinical outcomes in metastatic colorectal cancer treated with oxaliplatin/5-fluorouracil. Cancer Res Treat 46: 55-64, 2014.
    • (2014) Cancer Res Treat , vol.46 , pp. 55-64
    • Han, J.J.1    Baek, S.K.2    Lee, J.J.3    Kim, G.Y.4    Kim, S.Y.5    Lee, S.H.6
  • 17
    • 84882667367 scopus 로고    scopus 로고
    • RuvBL2 is involved in histone deacetylase inhibitor PCI-24781-induced cell death in SK-N-DZ neuroblastoma cells
    • Zhan Q, Tsai S, Lu Y, Wang C, Kwan Y and Ngai S: RuvBL2 is involved in histone deacetylase inhibitor PCI-24781-induced cell death in SK-N-DZ neuroblastoma cells. PLoS One 8: e71663, 2013.
    • (2013) PLoS One , vol.8
    • Zhan, Q.1    Tsai, S.2    Lu, Y.3    Wang, C.4    Kwan, Y.5    Ngai, S.6
  • 19
    • 84904382013 scopus 로고    scopus 로고
    • Overexpression of tumor necrosis factor receptor-associated protein 1 (TRAP1), leads to mitochondrial aberrations in mouse fibroblast NIH/3T3 cells
    • Dec 1, Epub ahead of print. pii: 2469
    • Im CN and Seo JS: Overexpression of tumor necrosis factor receptor-associated protein 1 (TRAP1), leads to mitochondrial aberrations in mouse fibroblast NIH/3T3 cells. BMB Rep: Dec 1, 2013 (Epub ahead of print). pii: 2469.
    • (2013) BMB Rep
    • Im, C.N.1    Seo, J.S.2
  • 25
    • 34548118366 scopus 로고    scopus 로고
    • Estrogen-regulated gene expression predicts response to endocrine therapy in patients with ovarian cancer
    • DOI 10.1016/j.ygyno.2007.05.009, PII S0090825807003411
    • Walker G, MacLeod K, Williams AR, Cameron DA, Smyth JF and Langdon SP: Estrogen-regulated gene expression predicts response to endocrine therapy in patients with ovarian cancer. Gynecol Oncol 106: 461-468, 2007 (Pubitemid 47302473)
    • (2007) Gynecologic Oncology , vol.106 , Issue.3 , pp. 461-468
    • Walker, G.1    MacLeod, K.2    Williams, A.R.W.3    Cameron, D.A.4    Smyth, J.F.5    Langdon, S.P.6
  • 26
    • 29144512841 scopus 로고    scopus 로고
    • Estrogen receptor-alpha mediates gene expression changes and growth response in ovarian cancer cells exposed to estrogen
    • DOI 10.1677/erc.1.01039
    • O'Donnell AJ, Macleod KG, Burns DJ, Smyth JF and Langdon SP: Estrogen receptor-alpha mediates gene expression changes and growth response in ovarian cancer cells exposed to estrogen. Endocr Relat Cancer 12: 851-866, 2005. (Pubitemid 41815780)
    • (2005) Endocrine-Related Cancer , vol.12 , Issue.4 , pp. 851-866
    • O'Donnell, A.J.M.1    Macleod, K.G.2    Burns, D.J.3    Smyth, J.F.4    Langdon, S.P.5
  • 29
    • 84883229070 scopus 로고    scopus 로고
    • A cotranslational ubiquitination pathway for quality control of misfolded proteins
    • Wang F, Durfee LA and Huibregtse JM: A cotranslational ubiquitination pathway for quality control of misfolded proteins. Mol Cell 50: 368-378, 2013.
    • (2013) Mol Cell , vol.50 , pp. 368-378
    • Wang, F.1    Durfee, L.A.2    Huibregtse, J.M.3
  • 31
    • 84866425291 scopus 로고    scopus 로고
    • Translational control in cancer etiology
    • pii a012336
    • Ruggero D: Translational control in cancer etiology. Cold Spring Harb Perspect Biol 5: pii a012336, 2013.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Ruggero, D.1
  • 33
    • 84873467908 scopus 로고    scopus 로고
    • Cotranslational response to proteotoxic stress by elongation pausing of ribosomes
    • Liu B, Han Y and Qian SB: Cotranslational response to proteotoxic stress by elongation pausing of ribosomes. Mol Cell 49: 453-463, 2013.
    • (2013) Mol Cell , vol.49 , pp. 453-463
    • Liu, B.1    Han, Y.2    Qian, S.B.3
  • 35
    • 84894453220 scopus 로고    scopus 로고
    • TRAP1 role in endoplasmic reticulum stress protection favors resistance to anthracyclins in breast carcinoma cells
    • Sisinni L, Maddalena F, Lettini G, Condelli V, Matassa DS, Esposito F and Landriscina M: TRAP1 role in endoplasmic reticulum stress protection favors resistance to anthracyclins in breast carcinoma cells. Int J Oncol 44: 573-582, 2014.
    • (2014) Int J Oncol , vol.44 , pp. 573-582
    • Sisinni, L.1    Maddalena, F.2    Lettini, G.3    Condelli, V.4    Matassa, D.S.5    Esposito, F.6    Landriscina, M.7
  • 36
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1
    • Pridgeon JW, Olzmann JA, Chin LS and Li L: PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol 5: e172, 2007.
    • (2007) PLoS Biol , vol.5
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 39
    • 84878533362 scopus 로고    scopus 로고
    • Drosophila Trap1 protects against mitochondrial dysfunction in a PINK1/parkin model of Parkinson's disease
    • Costa AC, Loh SH and Martins LM: Drosophila Trap1 protects against mitochondrial dysfunction in a PINK1/parkin model of Parkinson's disease. Cell Death Dis 4: e467, 2013.
    • (2013) Cell Death Dis , vol.4
    • Costa, A.C.1    Loh, S.H.2    Martins, L.M.3
  • 43
    • 84874035053 scopus 로고    scopus 로고
    • Mitochondrial factors and VACTERL association-related congenital malformations
    • Siebel S and Solomon BD: Mitochondrial factors and VACTERL association-related congenital malformations. Mol Syndromol 4: 63-73, 2013.
    • (2013) Mol Syndromol , vol.4 , pp. 63-73
    • Siebel, S.1    Solomon, B.D.2
  • 44
    • 84866361655 scopus 로고    scopus 로고
    • Gene expression of Hsp70, Hsp90, and Hsp110 families in normal and abnormal embryonic development of mouse forelimbs
    • Zhu Y, Zhou H, Zhu Y, Wan X, Zhu J and Zhang T: Gene expression of Hsp70, Hsp90, and Hsp110 families in normal and abnormal embryonic development of mouse forelimbs. Drug Chem Toxicol 35: 432-444, 2012.
    • (2012) Drug Chem Toxicol , vol.35 , pp. 432-444
    • Zhu, Y.1    Zhou, H.2    Zhu, Y.3    Wan, X.4    Zhu, J.5    Zhang, T.6
  • 45
    • 84870427712 scopus 로고    scopus 로고
    • Gene expression of Hsp70, Hsp90 and Hsp110 families in normal palate and cleft palate during mouse embryogenesis
    • Zhu Y, Ren C, Wan X, Zhu Y, Zhu J, Zhou H and Zhang T: Gene expression of Hsp70, Hsp90 and Hsp110 families in normal palate and cleft palate during mouse embryogenesis. Toxicol Ind Health 29: 915-930, 2013.
    • (2013) Toxicol Ind Health , vol.29 , pp. 915-930
    • Zhu, Y.1    Ren, C.2    Wan, X.3    Zhu, Y.4    Zhu, J.5    Zhou, H.6    Zhang, T.7
  • 46
    • 84892857095 scopus 로고    scopus 로고
    • Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism
    • Lavery LA, Partridge JR, Ramelot TA, Elnatan D, Kennedy MA and Agard DA: Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Mol Cell 53: 330-343, 2014.
    • (2014) Mol Cell , vol.53 , pp. 330-343
    • Lavery, L.A.1    Partridge, J.R.2    Ramelot, T.A.3    Elnatan, D.4    Kennedy, M.A.5    Agard, D.A.6
  • 47
    • 84895836004 scopus 로고    scopus 로고
    • Targeting tumour-supportive cellular machineries in anticancer drug development
    • Dobbelstein M and Moll U: Targeting tumour-supportive cellular machineries in anticancer drug development. Nat Rev Drug Discov 13: 179-196, 2014.
    • (2014) Nat Rev Drug Discov , vol.13 , pp. 179-196
    • Dobbelstein, M.1    Moll, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.