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Volumn 23, Issue 5, 2012, Pages 499-508

The ubiquitin/proteasome system-dependent control of mitochondrial steps in apoptosis

Author keywords

Apoptosis; Bcl 2; E3 ubiquitin ligase; Mitochondria; Proteasome; Ubiquitin

Indexed keywords

BCL2 RELATED PROTEIN A1; BIM PROTEIN; CASPASE; ENZYME; PROTEASOME; PROTEIN; PROTEIN ARTS; PROTEIN BAD; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL W; PROTEIN BCL XL; PROTEIN BLK; PROTEIN BMF; PROTEIN MCL 1; PROTEIN MOAP 1; PROTEIN NOXA; PUMA PROTEIN; UBIQUITIN; UBIQUITIN ACTIVATING ENZYME E1; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84863880821     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2012.03.019     Document Type: Review
Times cited : (26)

References (108)
  • 1
    • 0019225640 scopus 로고
    • Characterization of the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes
    • Ciechanover A., Elias S., Heller H., Ferber S., Hershko A. Characterization of the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes. Journal of Biological Chemistry 1980, 255:7525-7528.
    • (1980) Journal of Biological Chemistry , vol.255 , pp. 7525-7528
    • Ciechanover, A.1    Elias, S.2    Heller, H.3    Ferber, S.4    Hershko, A.5
  • 4
    • 33646795597 scopus 로고    scopus 로고
    • Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes
    • Millard S.M., Wood S.A. Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes. Journal of Cell Biology 2006, 173:463-468.
    • (2006) Journal of Cell Biology , vol.173 , pp. 463-468
    • Millard, S.M.1    Wood, S.A.2
  • 5
  • 8
    • 33645854348 scopus 로고    scopus 로고
    • Role of ubiquitylation in cellular membrane transport
    • Staub O., Rotin D. Role of ubiquitylation in cellular membrane transport. Physiological Reviews 2006, 86:669-707.
    • (2006) Physiological Reviews , vol.86 , pp. 669-707
    • Staub, O.1    Rotin, D.2
  • 9
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • Sun L., Chen Z.J. The novel functions of ubiquitination in signaling. Current Opinion in Cell Biology 2004, 16:119-126.
    • (2004) Current Opinion in Cell Biology , vol.16 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 11
    • 23144439184 scopus 로고    scopus 로고
    • Proteolysis: anytime, any place, anywhere?
    • Pines J., Lindon C. Proteolysis: anytime, any place, anywhere?. Nature Cell Biology 2005, 7:731-735.
    • (2005) Nature Cell Biology , vol.7 , pp. 731-735
    • Pines, J.1    Lindon, C.2
  • 12
    • 79953142340 scopus 로고    scopus 로고
    • A systematic search for ER membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis
    • Neutzner A., Neutzner M., Benischke A.S., Ryu S.W., Frank S., Youle R.J., et al. A systematic search for ER membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis. Journal of Biological Chemistry 2011.
    • (2011) Journal of Biological Chemistry
    • Neutzner, A.1    Neutzner, M.2    Benischke, A.S.3    Ryu, S.W.4    Frank, S.5    Youle, R.J.6
  • 13
    • 79960716413 scopus 로고    scopus 로고
    • Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation
    • Karbowski M., Youle R.J. Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation. Current Opinion in Cell Biology 2011, 23:476-482.
    • (2011) Current Opinion in Cell Biology , vol.23 , pp. 476-482
    • Karbowski, M.1    Youle, R.J.2
  • 16
    • 61449134122 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of apoptosis
    • Broemer M., Meier P. Ubiquitin-mediated regulation of apoptosis. Trends in Cell Biology 2009, 19:130-140.
    • (2009) Trends in Cell Biology , vol.19 , pp. 130-140
    • Broemer, M.1    Meier, P.2
  • 17
    • 1942534018 scopus 로고    scopus 로고
    • Regulation of apoptosis proteins in cancer cells by ubiquitin
    • Zhang H.G., Wang J., Yang X., Hsu H.C., Mountz J.D. Regulation of apoptosis proteins in cancer cells by ubiquitin. Oncogene 2004, 23:2009-2015.
    • (2004) Oncogene , vol.23 , pp. 2009-2015
    • Zhang, H.G.1    Wang, J.2    Yang, X.3    Hsu, H.C.4    Mountz, J.D.5
  • 18
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk J.E., Green D.R. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?. Trends in Cell Biology 2008, 18:157-164.
    • (2008) Trends in Cell Biology , vol.18 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 19
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle R.J., Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nature Reviews Molecular Cell Biology 2008, 9:47-59.
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 20
    • 84860389354 scopus 로고    scopus 로고
    • Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases
    • Strasser A., Cory S., Adams J.M. Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases. EMBO Journal 2011, 30:3667-3683.
    • (2011) EMBO Journal , vol.30 , pp. 3667-3683
    • Strasser, A.1    Cory, S.2    Adams, J.M.3
  • 22
    • 17044368875 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac/DIABLO
    • Morizane Y., Honda R., Fukami K., Yasuda H. X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac/DIABLO. Journal of Biochemistry 2005, 137:125-132.
    • (2005) Journal of Biochemistry , vol.137 , pp. 125-132
    • Morizane, Y.1    Honda, R.2    Fukami, K.3    Yasuda, H.4
  • 23
    • 0036300214 scopus 로고    scopus 로고
    • The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis
    • Wilson R., Goyal L., Ditzel M., Zachariou A., Baker D.A., Agapite J., et al. The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis. Nature Cell Biology 2002, 4:445-450.
    • (2002) Nature Cell Biology , vol.4 , pp. 445-450
    • Wilson, R.1    Goyal, L.2    Ditzel, M.3    Zachariou, A.4    Baker, D.A.5    Agapite, J.6
  • 25
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • Adams J.M., Cory S. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 2007, 26:1324-1337.
    • (2007) Oncogene , vol.26 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 26
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • Zhong Q., Gao W., Du F., Wang X. Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 2005, 121:1085-1095.
    • (2005) Cell , vol.121 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4
  • 27
    • 79952261405 scopus 로고    scopus 로고
    • SCF(FBW7) regulates cellular apoptosis by targeting MCL1 for ubiquitylation and destruction
    • Inuzuka H., Shaik S., Onoyama I., Gao D., Tseng A., Maser R.S., et al. SCF(FBW7) regulates cellular apoptosis by targeting MCL1 for ubiquitylation and destruction. Nature 2011, 471:104-109.
    • (2011) Nature , vol.471 , pp. 104-109
    • Inuzuka, H.1    Shaik, S.2    Onoyama, I.3    Gao, D.4    Tseng, A.5    Maser, R.S.6
  • 28
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • Schwickart M., Huang X., Lill J.R., Liu J., Ferrando R., French D.M., et al. Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 2010, 463:103-107.
    • (2010) Nature , vol.463 , pp. 103-107
    • Schwickart, M.1    Huang, X.2    Lill, J.R.3    Liu, J.4    Ferrando, R.5    French, D.M.6
  • 29
    • 0348014686 scopus 로고    scopus 로고
    • DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells
    • Cuconati A., Mukherjee C., Perez D., White E. DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells. Genes and Development 2003, 17:2922-2932.
    • (2003) Genes and Development , vol.17 , pp. 2922-2932
    • Cuconati, A.1    Mukherjee, C.2    Perez, D.3    White, E.4
  • 30
    • 0038046166 scopus 로고    scopus 로고
    • Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation
    • Nijhawan D., Fang M., Traer E., Zhong Q., Gao W., Du F., et al. Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. Genes and Development 2003, 17:1475-1486.
    • (2003) Genes and Development , vol.17 , pp. 1475-1486
    • Nijhawan, D.1    Fang, M.2    Traer, E.3    Zhong, Q.4    Gao, W.5    Du, F.6
  • 31
    • 79551663809 scopus 로고    scopus 로고
    • The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover
    • Xu S., Peng G., Wang Y., Fang S., Karbowski M. The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover. Molecular Biology of the Cell 2011, 22:291-300.
    • (2011) Molecular Biology of the Cell , vol.22 , pp. 291-300
    • Xu, S.1    Peng, G.2    Wang, Y.3    Fang, S.4    Karbowski, M.5
  • 33
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y., Meyer H., Rapoport T. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 2001, 414:652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.2    Rapoport, T.3
  • 34
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 2004, 429:841-847.
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 35
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway?
    • Jentsch S., Rumpf S. Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway?. Trends in Biochemical Sciences 2007, 32:6-11.
    • (2007) Trends in Biochemical Sciences , vol.32 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 36
    • 33745224935 scopus 로고    scopus 로고
    • P97: The cell's molecular purgatory?
    • Halawani D., Latterich M. p97: The cell's molecular purgatory?. Molecular Cell 2006, 22:713-717.
    • (2006) Molecular Cell , vol.22 , pp. 713-717
    • Halawani, D.1    Latterich, M.2
  • 37
    • 33845932083 scopus 로고    scopus 로고
    • S-nitrosylation of Bcl-2 inhibits its ubiquitin-proteasomal degradation. A novel antiapoptotic mechanism that suppresses apoptosis
    • Azad N., Vallyathan V., Wang L., Tantishaiyakul V., Stehlik C., Leonard S.S., et al. S-nitrosylation of Bcl-2 inhibits its ubiquitin-proteasomal degradation. A novel antiapoptotic mechanism that suppresses apoptosis. Journal of Biological Chemistry 2006, 281:34124-34134.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 34124-34134
    • Azad, N.1    Vallyathan, V.2    Wang, L.3    Tantishaiyakul, V.4    Stehlik, C.5    Leonard, S.S.6
  • 38
    • 0033974063 scopus 로고    scopus 로고
    • Posttranslational modification of Bcl-2 facilitates its proteasome-dependent degradation: molecular characterization of the involved signaling pathway
    • Breitschopf K., Haendeler J., Malchow P., Zeiher A.M., Dimmeler S. Posttranslational modification of Bcl-2 facilitates its proteasome-dependent degradation: molecular characterization of the involved signaling pathway. Molecular and Cellular Biology 2000, 20:1886-1896.
    • (2000) Molecular and Cellular Biology , vol.20 , pp. 1886-1896
    • Breitschopf, K.1    Haendeler, J.2    Malchow, P.3    Zeiher, A.M.4    Dimmeler, S.5
  • 39
    • 79951670106 scopus 로고    scopus 로고
    • INrf2 (Keap1) targets Bcl-2 degradation and controls cellular apoptosis
    • Niture S.K., Jaiswal A.K. INrf2 (Keap1) targets Bcl-2 degradation and controls cellular apoptosis. Cell Death and Differentiation 2011, 18:439-451.
    • (2011) Cell Death and Differentiation , vol.18 , pp. 439-451
    • Niture, S.K.1    Jaiswal, A.K.2
  • 40
    • 79953170575 scopus 로고    scopus 로고
    • Activation of GluR6-containing kainate receptors induces ubiquitin-dependent Bcl-2 degradation via denitrosylation in the rat hippocampus after kainate treatment
    • Zhang J., Yan H., Wu Y.P., Li C., Zhang G.Y. Activation of GluR6-containing kainate receptors induces ubiquitin-dependent Bcl-2 degradation via denitrosylation in the rat hippocampus after kainate treatment. Journal of Biological Chemistry 2011, 286:7669-7680.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 7669-7680
    • Zhang, J.1    Yan, H.2    Wu, Y.P.3    Li, C.4    Zhang, G.Y.5
  • 41
    • 3843059163 scopus 로고    scopus 로고
    • Mitochondrial pro-apoptotic ARTS protein is lost in the majority of acute lymphoblastic leukemia patients
    • Elhasid R., Sahar D., Merling A., Zivony Y., Rotem A., Ben-Arush M., et al. Mitochondrial pro-apoptotic ARTS protein is lost in the majority of acute lymphoblastic leukemia patients. Oncogene 2004, 23:5468-5475.
    • (2004) Oncogene , vol.23 , pp. 5468-5475
    • Elhasid, R.1    Sahar, D.2    Merling, A.3    Zivony, Y.4    Rotem, A.5    Ben-Arush, M.6
  • 42
    • 8844275871 scopus 로고    scopus 로고
    • Expression of the pro-apoptotic protein ARTS in astrocytic tumors: correlation with malignancy grade and survival rate
    • Gottfried Y., Voldavsky E., Yodko L., Sabo E., Ben-Itzhak O., Larisch S. Expression of the pro-apoptotic protein ARTS in astrocytic tumors: correlation with malignancy grade and survival rate. Cancer 2004, 101:2614-2621.
    • (2004) Cancer , vol.101 , pp. 2614-2621
    • Gottfried, Y.1    Voldavsky, E.2    Yodko, L.3    Sabo, E.4    Ben-Itzhak, O.5    Larisch, S.6
  • 44
    • 2342561882 scopus 로고    scopus 로고
    • The mitochondrial ARTS protein promotes apoptosis through targeting XIAP
    • Gottfried Y., Rotem A., Lotan R., Steller H., Larisch S. The mitochondrial ARTS protein promotes apoptosis through targeting XIAP. EMBO Journal 2004, 23:1627-1635.
    • (2004) EMBO Journal , vol.23 , pp. 1627-1635
    • Gottfried, Y.1    Rotem, A.2    Lotan, R.3    Steller, H.4    Larisch, S.5
  • 45
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D., Tanaka A., Suen D.F., Youle R.J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. Journal of Cell Biology 2008, 183:795-803.
    • (2008) Journal of Cell Biology , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 46
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
    • Darios F., Corti O., Lucking C.B., Hampe C., Muriel M.P., Abbas N., et al. Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Human Molecular Genetics 2003, 12:517-526.
    • (2003) Human Molecular Genetics , vol.12 , pp. 517-526
    • Darios, F.1    Corti, O.2    Lucking, C.B.3    Hampe, C.4    Muriel, M.P.5    Abbas, N.6
  • 49
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998, 94:491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 50
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: how BH3-only proteins induce apoptosis
    • Willis S.N., Adams J.M. Life in the balance: how BH3-only proteins induce apoptosis. Current Opinion in Cell Biology 2005, 17:617-625.
    • (2005) Current Opinion in Cell Biology , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 52
    • 57149135309 scopus 로고    scopus 로고
    • Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax
    • Lovell J.F., Billen L.P., Bindner S., Shamas-Din A., Fradin C., Leber B., et al. Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. Cell 2008, 135:1074-1084.
    • (2008) Cell , vol.135 , pp. 1074-1084
    • Lovell, J.F.1    Billen, L.P.2    Bindner, S.3    Shamas-Din, A.4    Fradin, C.5    Leber, B.6
  • 54
    • 0034647563 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction
    • Breitschopf K., Zeiher A.M., Dimmeler S. Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction. Journal of Biological Chemistry 2000, 275:21648-21652.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 21648-21652
    • Breitschopf, K.1    Zeiher, A.M.2    Dimmeler, S.3
  • 55
    • 38049059937 scopus 로고    scopus 로고
    • Apoptosis induction by Bid requires unconventional ubiquitination and degradation of its N-terminal fragment
    • Tait S.W., de Vries E., Maas C., Keller A.M., D'Santos C.S., Borst J. Apoptosis induction by Bid requires unconventional ubiquitination and degradation of its N-terminal fragment. Journal of Cell Biology 2007, 179:1453-1466.
    • (2007) Journal of Cell Biology , vol.179 , pp. 1453-1466
    • Tait, S.W.1    de Vries, E.2    Maas, C.3    Keller, A.M.4    D'Santos, C.S.5    Borst, J.6
  • 56
    • 76349086181 scopus 로고    scopus 로고
    • The ubiquitin ligase Itch mediates the antiapoptotic activity of epidermal growth factor by promoting the ubiquitylation and degradation of the truncated C-terminal portion of Bid
    • Azakir B.A., Desrochers G., Angers A. The ubiquitin ligase Itch mediates the antiapoptotic activity of epidermal growth factor by promoting the ubiquitylation and degradation of the truncated C-terminal portion of Bid. FEBS Journal 2010, 277:1319-1330.
    • (2010) FEBS Journal , vol.277 , pp. 1319-1330
    • Azakir, B.A.1    Desrochers, G.2    Angers, A.3
  • 58
    • 7444233268 scopus 로고    scopus 로고
    • BimEL is an important determinant for induction of anoikis sensitivity by mitogen-activated protein/extracellular signal-regulated kinase kinase inhibitors
    • Fukazawa H., Noguchi K., Masumi A., Murakami Y., Uehara Y. BimEL is an important determinant for induction of anoikis sensitivity by mitogen-activated protein/extracellular signal-regulated kinase kinase inhibitors. Molecular Cancer Therapeutics 2004, 3:1281-1288.
    • (2004) Molecular Cancer Therapeutics , vol.3 , pp. 1281-1288
    • Fukazawa, H.1    Noguchi, K.2    Masumi, A.3    Murakami, Y.4    Uehara, Y.5
  • 59
    • 79957598477 scopus 로고    scopus 로고
    • Identification of a novel Bcl-2-interacting mediator of cell death (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in rapid ischemic tolerance-induced neuroprotection
    • Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P., et al. Identification of a novel Bcl-2-interacting mediator of cell death (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in rapid ischemic tolerance-induced neuroprotection. Journal of Biological Chemistry 2011, 286:19331-19339.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 19331-19339
    • Thompson, S.1    Pearson, A.N.2    Ashley, M.D.3    Jessick, V.4    Murphy, B.M.5    Gafken, P.6
  • 60
    • 68149116041 scopus 로고    scopus 로고
    • BIK, the founding member of the BH3-only family proteins: mechanisms of cell death and role in cancer and pathogenic processes
    • Chinnadurai G., Vijayalingam S., Rashmi R. BIK, the founding member of the BH3-only family proteins: mechanisms of cell death and role in cancer and pathogenic processes. Oncogene 2008, 27(Suppl. 1):S20-S29.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Chinnadurai, G.1    Vijayalingam, S.2    Rashmi, R.3
  • 61
    • 10744232926 scopus 로고    scopus 로고
    • Regulation of osteoclast apoptosis by ubiquitylation of proapoptotic BH3-only Bcl-2 family member Bim
    • Akiyama T., Bouillet P., Miyazaki T., Kadono Y., Chikuda H., Chung U.I., et al. Regulation of osteoclast apoptosis by ubiquitylation of proapoptotic BH3-only Bcl-2 family member Bim. EMBO Journal 2003, 22:6653-6664.
    • (2003) EMBO Journal , vol.22 , pp. 6653-6664
    • Akiyama, T.1    Bouillet, P.2    Miyazaki, T.3    Kadono, Y.4    Chikuda, H.5    Chung, U.I.6
  • 62
    • 79959334667 scopus 로고    scopus 로고
    • Bim protein degradation contributes to cisplatin resistance
    • Wang J., Zhou J.Y., Wu G.S. Bim protein degradation contributes to cisplatin resistance. Journal of Biological Chemistry 2011, 286:22384-22392.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 22384-22392
    • Wang, J.1    Zhou, J.Y.2    Wu, G.S.3
  • 63
    • 79952776227 scopus 로고    scopus 로고
    • BIM(EL), an intrinsically disordered protein, is degraded by 20S proteasomes in the absence of poly-ubiquitylation
    • Wiggins C.M., Tsvetkov P., Johnson M., Joyce C.L., Lamb C.A., Bryant N.J., et al. BIM(EL), an intrinsically disordered protein, is degraded by 20S proteasomes in the absence of poly-ubiquitylation. Journal of Cell Science 2011, 124:969-977.
    • (2011) Journal of Cell Science , vol.124 , pp. 969-977
    • Wiggins, C.M.1    Tsvetkov, P.2    Johnson, M.3    Joyce, C.L.4    Lamb, C.A.5    Bryant, N.J.6
  • 64
    • 33845486323 scopus 로고    scopus 로고
    • Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets
    • Hinds M.G., Smits C., Fredericks-Short R., Risk J.M., Bailey M., Huang D.C., et al. Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. Cell Death and Differentiation 2007, 14:128-136.
    • (2007) Cell Death and Differentiation , vol.14 , pp. 128-136
    • Hinds, M.G.1    Smits, C.2    Fredericks-Short, R.3    Risk, J.M.4    Bailey, M.5    Huang, D.C.6
  • 65
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. Journal of Molecular Biology 1999, 293:321-331.
    • (1999) Journal of Molecular Biology , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 67
    • 0001003612 scopus 로고    scopus 로고
    • Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members
    • Hsu S.Y., Kaipia A., McGee E., Lomeli M., Hsueh A.J. Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members. Proceedings of the National Academy of Sciences of the United States of America 1997, 94:12401-12406.
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , pp. 12401-12406
    • Hsu, S.Y.1    Kaipia, A.2    McGee, E.3    Lomeli, M.4    Hsueh, A.J.5
  • 68
    • 41949136647 scopus 로고    scopus 로고
    • Bortezomib blocks Bax degradation in malignant B cells during treatment with TRAIL
    • Liu F.T., Agrawal S.G., Gribben J.G., Ye H., Du M.Q., Newland A.C., et al. Bortezomib blocks Bax degradation in malignant B cells during treatment with TRAIL. Blood 2008, 111:2797-2805.
    • (2008) Blood , vol.111 , pp. 2797-2805
    • Liu, F.T.1    Agrawal, S.G.2    Gribben, J.G.3    Ye, H.4    Du, M.Q.5    Newland, A.C.6
  • 69
    • 41949096727 scopus 로고    scopus 로고
    • Increased proteasomal degradation of Bax is a common feature of poor prognosis chronic lymphocytic leukemia
    • Agrawal S.G., Liu F.T., Wiseman C., Shirali S., Liu H., Lillington D., et al. Increased proteasomal degradation of Bax is a common feature of poor prognosis chronic lymphocytic leukemia. Blood 2008, 111:2790-2796.
    • (2008) Blood , vol.111 , pp. 2790-2796
    • Agrawal, S.G.1    Liu, F.T.2    Wiseman, C.3    Shirali, S.4    Liu, H.5    Lillington, D.6
  • 70
  • 71
    • 58149299435 scopus 로고    scopus 로고
    • Baxbeta: a constitutively active human Bax isoform that is under tight regulatory control by the proteasomal degradation mechanism
    • Fu N.Y., Sukumaran S.K., Kerk S.Y., Yu V.C. Baxbeta: a constitutively active human Bax isoform that is under tight regulatory control by the proteasomal degradation mechanism. Molecular Cell 2009, 33:15-29.
    • (2009) Molecular Cell , vol.33 , pp. 15-29
    • Fu, N.Y.1    Sukumaran, S.K.2    Kerk, S.Y.3    Yu, V.C.4
  • 72
    • 77951464624 scopus 로고    scopus 로고
    • IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation
    • Benard G., Neutzner A., Peng G., Wang C., Livak F., Youle R.J., et al. IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation. EMBO Journal 2010, 29:1458-1471.
    • (2010) EMBO Journal , vol.29 , pp. 1458-1471
    • Benard, G.1    Neutzner, A.2    Peng, G.3    Wang, C.4    Livak, F.5    Youle, R.J.6
  • 74
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu Y.T., Youle R.J. Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. Journal of Biological Chemistry 1998, 273:10777-10783.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 75
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki M., Youle R.J., Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 2000, 103:645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 76
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson B., Montessuit S., Sanchez B., Martinou J.C. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. Journal of Biological Chemistry 2001, 276:11615-11623.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 77
    • 0042090307 scopus 로고    scopus 로고
    • BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization
    • Ruffolo S.C., Shore G.C. BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization. Journal of Biological Chemistry 2003, 278:25039-25045.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 25039-25045
    • Ruffolo, S.C.1    Shore, G.C.2
  • 78
    • 33744953583 scopus 로고    scopus 로고
    • Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2
    • Tan C., Dlugosz P.J., Peng J., Zhang Z., Lapolla S.M., Plafker S.M., et al. Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2. Journal of Biological Chemistry 2006, 281:14764-14775.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 14764-14775
    • Tan, C.1    Dlugosz, P.J.2    Peng, J.3    Zhang, Z.4    Lapolla, S.M.5    Plafker, S.M.6
  • 79
    • 34547118616 scopus 로고    scopus 로고
    • BARD1 translocation to mitochondria correlates with Bax oligomerization, loss of mitochondrial membrane potential, and apoptosis
    • Tembe V., Henderson B.R. BARD1 translocation to mitochondria correlates with Bax oligomerization, loss of mitochondrial membrane potential, and apoptosis. Journal of Biological Chemistry 2007, 282:20513-20522.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 20513-20522
    • Tembe, V.1    Henderson, B.R.2
  • 80
    • 70450224250 scopus 로고    scopus 로고
    • Differential modulation of BRCA1 and BARD1 nuclear localisation and foci assembly by DNA damage
    • Brodie K.M., Henderson B.R. Differential modulation of BRCA1 and BARD1 nuclear localisation and foci assembly by DNA damage. Cellular Signalling 2010, 22:291-302.
    • (2010) Cellular Signalling , vol.22 , pp. 291-302
    • Brodie, K.M.1    Henderson, B.R.2
  • 82
    • 0035951847 scopus 로고    scopus 로고
    • MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains
    • Tan K.O., Tan K.M., Chan S.L., Yee K.S., Bevort M., Ang K.C., et al. MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains. Journal of Biological Chemistry 2001, 276:2802-2807.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 2802-2807
    • Tan, K.O.1    Tan, K.M.2    Chan, S.L.3    Yee, K.S.4    Bevort, M.5    Ang, K.C.6
  • 83
    • 63049102690 scopus 로고    scopus 로고
    • TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process
    • Lee S.S., Fu N.Y., Sukumaran S.K., Wan K.F., Wan Q., Yu V.C. TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. Experimental Cell Research 2009, 315:1313-1325.
    • (2009) Experimental Cell Research , vol.315 , pp. 1313-1325
    • Lee, S.S.1    Fu, N.Y.2    Sukumaran, S.K.3    Wan, K.F.4    Wan, Q.5    Yu, V.C.6
  • 84
    • 55249122277 scopus 로고    scopus 로고
    • E6 proteins from multiple human betapapillomavirus types degrade Bak and protect keratinocytes from apoptosis after UVB irradiation
    • Underbrink M.P., Howie H.L., Bedard K.M., Koop J.I., Galloway D.A. E6 proteins from multiple human betapapillomavirus types degrade Bak and protect keratinocytes from apoptosis after UVB irradiation. Journal of Virology 2008, 82:10408-10417.
    • (2008) Journal of Virology , vol.82 , pp. 10408-10417
    • Underbrink, M.P.1    Howie, H.L.2    Bedard, K.M.3    Koop, J.I.4    Galloway, D.A.5
  • 85
    • 53449091865 scopus 로고    scopus 로고
    • Identification of the regions of the HPV 5 E6 protein involved in Bak degradation and inhibition of apoptosis
    • Simmonds M., Storey A. Identification of the regions of the HPV 5 E6 protein involved in Bak degradation and inhibition of apoptosis. International Journal of Cancer 2008, 123:2260-2266.
    • (2008) International Journal of Cancer , vol.123 , pp. 2260-2266
    • Simmonds, M.1    Storey, A.2
  • 86
    • 68949194550 scopus 로고    scopus 로고
    • Oncogenic activities of human papillomaviruses
    • McLaughlin-Drubin M.E., Munger K. Oncogenic activities of human papillomaviruses. Virus Research 2009, 143:195-208.
    • (2009) Virus Research , vol.143 , pp. 195-208
    • McLaughlin-Drubin, M.E.1    Munger, K.2
  • 87
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • Scheffner M., Werness B.A., Huibregtse J.M., Levine A.J., Howley P.M. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 1990, 63:1129-1136.
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 88
    • 77958140445 scopus 로고    scopus 로고
    • Mitochondria on guard: role of mitochondrial fusion and fission in the regulation of apoptosis
    • Karbowski M. Mitochondria on guard: role of mitochondrial fusion and fission in the regulation of apoptosis. Advances in Experimental Medicine and Biology 2010, 687:131-142.
    • (2010) Advances in Experimental Medicine and Biology , vol.687 , pp. 131-142
    • Karbowski, M.1
  • 89
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: dynamic organelles in disease, aging, and development
    • Chan D.C. Mitochondria: dynamic organelles in disease, aging, and development. Cell 2006, 125:1241-1252.
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 91
    • 0043166392 scopus 로고    scopus 로고
    • Dynamics of mitochondrial morphology in healthy cells and during apoptosis
    • Karbowski M., Youle R.J. Dynamics of mitochondrial morphology in healthy cells and during apoptosis. Cell Death and Differentiation 2003, 10:870-880.
    • (2003) Cell Death and Differentiation , vol.10 , pp. 870-880
    • Karbowski, M.1    Youle, R.J.2
  • 93
    • 34347398050 scopus 로고    scopus 로고
    • The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
    • Karbowski M., Neutzner A., Youle R.J. The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division. Journal of Cell Biology 2007, 178:71-84.
    • (2007) Journal of Cell Biology , vol.178 , pp. 71-84
    • Karbowski, M.1    Neutzner, A.2    Youle, R.J.3
  • 94
    • 33749253910 scopus 로고    scopus 로고
    • MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology
    • Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S. MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Reports 2006, 7:1019-1022.
    • (2006) EMBO Reports , vol.7 , pp. 1019-1022
    • Nakamura, N.1    Kimura, Y.2    Tokuda, M.3    Honda, S.4    Hirose, S.5
  • 95
    • 33747613595 scopus 로고    scopus 로고
    • A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics
    • Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., et al. A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics. EMBO Journal 2006, 25:3618-3626.
    • (2006) EMBO Journal , vol.25 , pp. 3618-3626
    • Yonashiro, R.1    Ishido, S.2    Kyo, S.3    Fukuda, T.4    Goto, E.5    Matsuki, Y.6
  • 96
    • 51049095678 scopus 로고    scopus 로고
    • GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis and slows growth
    • Zhang B., Huang J., Li H.L., Liu T., Wang Y.Y., Waterman P., et al. GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis and slows growth. Cell Research 2008, 18:900-910.
    • (2008) Cell Research , vol.18 , pp. 900-910
    • Zhang, B.1    Huang, J.2    Li, H.L.3    Liu, T.4    Wang, Y.Y.5    Waterman, P.6
  • 97
    • 34248182897 scopus 로고    scopus 로고
    • Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death
    • Wasiak S., Zunino R., McBride H.M. Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. Journal of Cell Biology 2007, 177:439-450.
    • (2007) Journal of Cell Biology , vol.177 , pp. 439-450
    • Wasiak, S.1    Zunino, R.2    McBride, H.M.3
  • 98
    • 0141960411 scopus 로고    scopus 로고
    • Effects of the proteasome inhibitor, bortezomib, on apoptosis in isolated lymphocytes obtained from patients with chronic lymphocytic leukemia
    • Pahler J.C., Ruiz S., Niemer I., Calvert L.R., Andreeff M., Keating M., et al. Effects of the proteasome inhibitor, bortezomib, on apoptosis in isolated lymphocytes obtained from patients with chronic lymphocytic leukemia. Clinical Cancer Research 2003, 9:4570-4577.
    • (2003) Clinical Cancer Research , vol.9 , pp. 4570-4577
    • Pahler, J.C.1    Ruiz, S.2    Niemer, I.3    Calvert, L.R.4    Andreeff, M.5    Keating, M.6
  • 99
    • 84872601365 scopus 로고    scopus 로고
    • Bortezomib-induced sensitization of malignant human glioma cells to vorinostat-induced apoptosis depends on reactive oxygen species production, mitochondrial dysfunction, Noxa upregulation, Mcl-1 cleavage, and DNA damage
    • [Epub ahead of print]
    • Premkumar D.R., Jane E.P., Agostino N.R., Didomenico J.D., Pollack I.F. Bortezomib-induced sensitization of malignant human glioma cells to vorinostat-induced apoptosis depends on reactive oxygen species production, mitochondrial dysfunction, Noxa upregulation, Mcl-1 cleavage, and DNA damage. Molecular Carcinogenesis 2011, http://dx.doi.org/10.1002/mc.21835. [Epub ahead of print].
    • (2011) Molecular Carcinogenesis
    • Premkumar, D.R.1    Jane, E.P.2    Agostino, N.R.3    Didomenico, J.D.4    Pollack, I.F.5
  • 100
    • 1642564603 scopus 로고    scopus 로고
    • Inhibition of proteasomal function by curcumin induces apoptosis through mitochondrial pathway
    • Jana N.R., Dikshit P., Goswami A., Nukina N. Inhibition of proteasomal function by curcumin induces apoptosis through mitochondrial pathway. Journal of Biological Chemistry 2004, 279:11680-11685.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 11680-11685
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Nukina, N.4
  • 102
    • 67649443814 scopus 로고    scopus 로고
    • Curcumin inhibits proliferation and migration by increasing the Bax to Bcl-2 ratio and decreasing NF-kappaBp65 expression in breast cancer MDA-MB-231 cells
    • Chiu T.L., Su C.C. Curcumin inhibits proliferation and migration by increasing the Bax to Bcl-2 ratio and decreasing NF-kappaBp65 expression in breast cancer MDA-MB-231 cells. International Journal of Molecular Medicine 2009, 23:469-475.
    • (2009) International Journal of Molecular Medicine , vol.23 , pp. 469-475
    • Chiu, T.L.1    Su, C.C.2
  • 103
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signaling
    • Chou J.J., Li H., Salvesen G.S., Yuan J., Wagner G. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell 1999, 96(5):615-624.
    • (1999) Cell , vol.96 , Issue.5 , pp. 615-624
    • Chou, J.J.1    Li, H.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 104
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • Zha J., Weiler S., Oh K.J., Wei M.C., Korsmeyer S.J. Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 2000, 290(5497):1761-1765.
    • (2000) Science , vol.290 , Issue.5497 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 105
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana T., Mackey M.R., Perkins G., Ellisman M.H., Latterich M., Schneiter R., et al. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 2002, 111(3):331-342.
    • (2002) Cell , vol.111 , Issue.3 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Perkins, G.3    Ellisman, M.H.4    Latterich, M.5    Schneiter, R.6
  • 106
    • 0038832563 scopus 로고    scopus 로고
    • A novel BH3-like domain in BID is required for intramolecular interaction and autoinhibition of pro-apoptotic activity
    • Tan K.O., Tan K.M., Yu V.C. A novel BH3-like domain in BID is required for intramolecular interaction and autoinhibition of pro-apoptotic activity. Journal of Biological Chemistry 1999, 274(34):23687-23690.
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.34 , pp. 23687-23690
    • Tan, K.O.1    Tan, K.M.2    Yu, V.C.3
  • 107
    • 0034725630 scopus 로고    scopus 로고
    • The destabilization of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved bid is inhibited by the N-terminal fragment
    • Kudla G., Montessuit S., Eskes R., Berrier C., Martinou J.C., Ghazi A. The destabilization of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved bid is inhibited by the N-terminal fragment. Journal of Biological Chemistry 2000, 275(30):22713-22718.
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.30 , pp. 22713-22718
    • Kudla, G.1    Montessuit, S.2    Eskes, R.3    Berrier, C.4    Martinou, J.C.5    Ghazi, A.6


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