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Volumn 290, Issue 19, 2015, Pages 11843-11852

The proapoptotic F-box protein Fbxl7 regulates mitochondrial function by mediating the ubiquitylation and proteasomal degradation of survivin

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; FLUORINE; MITOCHONDRIA; MOBILE SECURITY;

EID: 84929012256     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.629931     Document Type: Article
Times cited : (58)

References (41)
  • 1
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi, A., and Dixit, V. M. (1998) Death receptors: signaling and modulation. Science 281, 1305-1308
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 3
    • 0036088471 scopus 로고    scopus 로고
    • IAP proteins: Blocking the road to death's door
    • Salvesen, G. S., and Duckett, C. S. (2002) IAP proteins: blocking the road to death's door. Nat. Rev. Mol. Cell Biol. 3, 401-410
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 5
    • 0037267333 scopus 로고    scopus 로고
    • Validating survivin as a cancer therapeutic target
    • Altieri, D. C. (2003) Validating survivin as a cancer therapeutic target. Nat. Rev. Cancer 3, 46-54
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 46-54
    • Altieri, D.C.1
  • 6
    • 2542549018 scopus 로고    scopus 로고
    • High expression levels of X-linked inhibitor of apoptosis protein and survivin correlate with poor overall survival in childhood de novo acute myeloid leukemia
    • Tamm, I., Richter, S., Oltersdorf, D., Creutzig, U., Harbott, J., Scholz, F., Karawajew, L., Ludwig, W. D., and Wuchter, C. (2004) High expression levels of X-linked inhibitor of apoptosis protein and survivin correlate with poor overall survival in childhood de novo acute myeloid leukemia. Clin. Cancer Res. 10, 3737-3744
    • (2004) Clin. Cancer Res. , vol.10 , pp. 3737-3744
    • Tamm, I.1    Richter, S.2    Oltersdorf, D.3    Creutzig, U.4    Harbott, J.5    Scholz, F.6    Karawajew, L.7    Ludwig, W.D.8    Wuchter, C.9
  • 7
    • 0037249506 scopus 로고    scopus 로고
    • Expression and prognostic significance of LIVIN, SURVIVIN and other apoptosis-related genes in the progression of superficial bladder cancer
    • Gazzaniga, P., Gradilone, A., Giuliani, L., Gandini, O., Silvestri, I., Nofroni, I., Saccani, G., Frati, L., and Aglianò, A. M. (2003) Expression and prognostic significance of LIVIN, SURVIVIN and other apoptosis-related genes in the progression of superficial bladder cancer. Ann. Oncol. 14, 85-90
    • (2003) Ann. Oncol. , vol.14 , pp. 85-90
    • Gazzaniga, P.1    Gradilone, A.2    Giuliani, L.3    Gandini, O.4    Silvestri, I.5    Nofroni, I.6    Saccani, G.7    Frati, L.8    Aglianò, A.M.9
  • 8
    • 4844231863 scopus 로고    scopus 로고
    • XIAP and survivin as therapeutic targets for radiation sensitization in preclinical models of lung cancer
    • Cao, C., Mu, Y., Hallahan, D. E., and Lu, B. (2004) XIAP and survivin as therapeutic targets for radiation sensitization in preclinical models of lung cancer. Oncogene 23, 7047-7052
    • (2004) Oncogene , vol.23 , pp. 7047-7052
    • Cao, C.1    Mu, Y.2    Hallahan, D.E.3    Lu, B.4
  • 9
    • 84885178346 scopus 로고    scopus 로고
    • BIRC5/Survivin enhances aerobic glycolysis and drug resistance by altered regulation of the mitochondrial fusion/fission machinery
    • Hagenbuchner, J., Kuznetsov, A. V., Obexer, P., and Ausserlechner, M. J. (2013) BIRC5/Survivin enhances aerobic glycolysis and drug resistance by altered regulation of the mitochondrial fusion/fission machinery. Oncogene 32, 4748-4757
    • (2013) Oncogene , vol.32 , pp. 4748-4757
    • Hagenbuchner, J.1    Kuznetsov, A.V.2    Obexer, P.3    Ausserlechner, M.J.4
  • 10
    • 0030746636 scopus 로고    scopus 로고
    • A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma
    • Ambrosini, G., Adida, C., and Altieri, D. C. (1997) A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nat. Med. 3, 917-921
    • (1997) Nat. Med. , vol.3 , pp. 917-921
    • Ambrosini, G.1    Adida, C.2    Altieri, D.C.3
  • 11
    • 84901827031 scopus 로고    scopus 로고
    • CUL9 mediates the functions of the 3M complex and ubiquitylates survivin to maintain genome integrity
    • Li, Z., Pei, X. H., Yan, J., Yan, F., Cappell, K. M., Whitehurst, A. W., and Xiong, Y. (2014) CUL9 mediates the functions of the 3M complex and ubiquitylates survivin to maintain genome integrity. Mol. Cell 54, 805-819
    • (2014) Mol. Cell , vol.54 , pp. 805-819
    • Li, Z.1    Pei, X.H.2    Yan, J.3    Yan, F.4    Cappell, K.M.5    Whitehurst, A.W.6    Xiong, Y.7
  • 12
    • 34548817572 scopus 로고    scopus 로고
    • Degradation of survivin by the X-linked inhibitor of apoptosis (XIAP)-XAF1 complex
    • Arora, V., Cheung, H. H., Plenchette, S., Micali, O. C., Liston, P., and Korneluk, R. G. (2007) Degradation of survivin by the X-linked inhibitor of apoptosis (XIAP)-XAF1 complex. J. Biol. Chem. 282, 26202-26209
    • (2007) J. Biol. Chem. , vol.282 , pp. 26202-26209
    • Arora, V.1    Cheung, H.H.2    Plenchette, S.3    Micali, O.C.4    Liston, P.5    Korneluk, R.G.6
  • 15
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: Insights into a molecular machine
    • Cardozo, T., and Pagano, M. (2004) The SCF ubiquitin ligase: insights into a molecular machine. Nat. Rev. Mol. Cell Biol. 5, 739-751
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 16
    • 84878260314 scopus 로고    scopus 로고
    • Mechanisms and function of substrate recruitment by F-box proteins
    • Skaar, J. R., Pagan, J. K., and Pagano, M. (2013) Mechanisms and function of substrate recruitment by F-box proteins. Nat. Rev. Mol. Cell Biol. 14, 369-381
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 369-381
    • Skaar, J.R.1    Pagan, J.K.2    Pagano, M.3
  • 18
    • 84892948811 scopus 로고    scopus 로고
    • Emerging therapies targeting the ubiquitin proteasome system in cancer
    • Weathington, N. M., and Mallampalli, R. K. (2014) Emerging therapies targeting the ubiquitin proteasome system in cancer. J. Clin. Invest. 124, 6-12
    • (2014) J. Clin. Invest. , vol.124 , pp. 6-12
    • Weathington, N.M.1    Mallampalli, R.K.2
  • 20
    • 84863129775 scopus 로고    scopus 로고
    • Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A, causing mitotic arrest
    • Coon, T. A., Glasser, J. R., Mallampalli, R. K., and Chen, B. B. (2012) Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A, causing mitotic arrest. Cell Cycle 11, 721-729
    • (2012) Cell Cycle , vol.11 , pp. 721-729
    • Coon, T.A.1    Glasser, J.R.2    Mallampalli, R.K.3    Chen, B.B.4
  • 21
    • 84923171541 scopus 로고    scopus 로고
    • F-box protein Fbxl18 mediates polyubiquitylation and proteasomal degradation of the pro-apoptotic SCF subunit Fbxl7
    • Liu, Y., Lear, T., Zhao, Y., Zhao, J., Zou, C., Chen, B. B., and Mallampalli, R. K. (2015) F-box protein Fbxl18 mediates polyubiquitylation and proteasomal degradation of the pro-apoptotic SCF subunit Fbxl7. Cell Death Dis. 6, e1630
    • (2015) Cell Death Dis , vol.6 , pp. e1630
    • Liu, Y.1    Lear, T.2    Zhao, Y.3    Zhao, J.4    Zou, C.5    Chen, B.B.6    Mallampalli, R.K.7
  • 22
    • 84862636380 scopus 로고    scopus 로고
    • F-box protein FBXL19-mediated ubiquitination and degradation of the receptor for IL-33 limits pulmonary inflammation
    • Zhao, J., Wei, J., Mialki, R. K., Mallampalli, D. F., Chen, B. B., Coon, T., Zou, C., Mallampalli, R. K., and Zhao, Y. (2012) F-box protein FBXL19-mediated ubiquitination and degradation of the receptor for IL-33 limits pulmonary inflammation. Nat. Immunol. 13, 651-658
    • (2012) Nat. Immunol. , vol.13 , pp. 651-658
    • Zhao, J.1    Wei, J.2    Mialki, R.K.3    Mallampalli, D.F.4    Chen, B.B.5    Coon, T.6    Zou, C.7    Mallampalli, R.K.8    Zhao, Y.9
  • 24
    • 84871569969 scopus 로고    scopus 로고
    • Specific small molecule inhibitors of Skp2-mediated p27 degradation
    • Wu, L., Grigoryan, A. V., Li, Y., Hao, B., Pagano, M., and Cardozo, T. J. (2012) Specific small molecule inhibitors of Skp2-mediated p27 degradation. Chem. Biol. 19, 1515-1524
    • (2012) Chem. Biol. , vol.19 , pp. 1515-1524
    • Wu, L.1    Grigoryan, A.V.2    Li, Y.3    Hao, B.4    Pagano, M.5    Cardozo, T.J.6
  • 26
    • 78650383624 scopus 로고    scopus 로고
    • Chemical genetics approach to restoring p27Kip1 reveals novel compounds with antiproliferative activity in prostate cancer cells
    • Rico-Bautista, E., Yang, C. C., Lu, L., Roth, G. P., and Wolf, D. A. (2010) Chemical genetics approach to restoring p27Kip1 reveals novel compounds with antiproliferative activity in prostate cancer cells. BMCBiol. 8, 153
    • (2010) BMCBiol , vol.8 , pp. 153
    • Rico-Bautista, E.1    Yang, C.C.2    Lu, L.3    Roth, G.P.4    Wolf, D.A.5
  • 29
    • 0033179212 scopus 로고    scopus 로고
    • An exegesis of IAPs: Salvation and surprises from BIR motifs
    • Miller, L. K. (1999) An exegesis of IAPs: salvation and surprises from BIR motifs. Trends Cell Biol. 9, 323-328
    • (1999) Trends Cell Biol , vol.9 , pp. 323-328
    • Miller, L.K.1
  • 31
    • 0033923368 scopus 로고    scopus 로고
    • Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement
    • Verdecia, M. A., Huang, H., Dutil, E., Kaiser, D. A., Hunter, T., and Noel, J. P. (2000) Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement. Nat. Struct. Biol. 7, 602-608
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 602-608
    • Verdecia, M.A.1    Huang, H.2    Dutil, E.3    Kaiser, D.A.4    Hunter, T.5    Noel, J.P.6
  • 33
    • 84877577024 scopus 로고    scopus 로고
    • FBXL2- and PTPL1-mediated degradation of p110-free p85β regulatory subunit controls the PI(3)K signalling cascade
    • Kuchay, S., Duan, S., Schenkein, E., Peschiaroli, A., Saraf, A., Florens, L., Washburn, M. P., and Pagano, M. (2013) FBXL2- and PTPL1-mediated degradation of p110-free p85β regulatory subunit controls the PI(3)K signalling cascade. Nat. Cell Biol. 15, 472-480
    • (2013) Nat. Cell Biol. , vol.15 , pp. 472-480
    • Kuchay, S.1    Duan, S.2    Schenkein, E.3    Peschiaroli, A.4    Saraf, A.5    Florens, L.6    Washburn, M.P.7    Pagano, M.8
  • 35
    • 0242321836 scopus 로고    scopus 로고
    • Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains
    • Yoshida, Y., Tokunaga, F., Chiba, T., Iwai, K., Tanaka, K., and Tai, T. (2003) Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. J. Biol. Chem. 278, 43877-43884
    • (2003) J. Biol. Chem. , vol.278 , pp. 43877-43884
    • Yoshida, Y.1    Tokunaga, F.2    Chiba, T.3    Iwai, K.4    Tanaka, K.5    Tai, T.6
  • 36
    • 84874774494 scopus 로고    scopus 로고
    • SCF(Fbxw15) mediates histone acetyltransferase binding to origin recognition complex (HBO1) ubiquitin-proteasomal degradation to regulate cell proliferation
    • Zou, C., Chen, Y., Smith, R. M., Snavely, C., Li, J., Coon, T. A., Chen, B. B., Zhao, Y., and Mallampalli, R. K. (2013) SCF(Fbxw15) mediates histone acetyltransferase binding to origin recognition complex (HBO1) ubiquitin-proteasomal degradation to regulate cell proliferation. J. Biol. Chem. 288, 6306-6316
    • (2013) J. Biol. Chem. , vol.288 , pp. 6306-6316
    • Zou, C.1    Chen, Y.2    Smith, R.M.3    Snavely, C.4    Li, J.5    Coon, T.A.6    Chen, B.B.7    Zhao, Y.8    Mallampalli, R.K.9
  • 37
    • 1242339630 scopus 로고    scopus 로고
    • Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo
    • Wheatley, S. P., Henzing, A. J., Dodson, H., Khaled, W., and Earnshaw, W. C. (2004) Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo. J. Biol. Chem. 279, 5655-5660
    • (2004) J. Biol. Chem. , vol.279 , pp. 5655-5660
    • Wheatley, S.P.1    Henzing, A.J.2    Dodson, H.3    Khaled, W.4    Earnshaw, W.C.5
  • 39
    • 84856495152 scopus 로고    scopus 로고
    • Targeting IAP proteins for therapeutic intervention in cancer
    • Fulda, S., and Vucic, D. (2012) Targeting IAP proteins for therapeutic intervention in cancer. Nat. Rev. Drug Discov. 11, 109-124
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 109-124
    • Fulda, S.1    Vucic, D.2
  • 40
    • 84907883684 scopus 로고    scopus 로고
    • Phase I dose-escalation study of LCL161, an oral inhibitor of apoptosis proteins inhibitor, in patients with advanced solid tumors
    • Infante, J. R., Dees, E. C., Olszanski, A. J., Dhuria, S. V., Sen, S., Cameron, S., and Cohen, R. B. (2014) Phase I dose-escalation study of LCL161, an oral inhibitor of apoptosis proteins inhibitor, in patients with advanced solid tumors. J. Clin. Oncol. 32, 3103-3110
    • (2014) J. Clin. Oncol. , vol.32 , pp. 3103-3110
    • Infante, J.R.1    Dees, E.C.2    Olszanski, A.J.3    Dhuria, S.V.4    Sen, S.5    Cameron, S.6    Cohen, R.B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.