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Volumn 18, Issue 6, 2005, Pages 637-650

The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to bax conformational change and cell death

Author keywords

[No Author keywords available]

Indexed keywords

BH3 PROTEIN; CYTOCHROME C; DEATH RECEPTOR; MICROTUBULE ASSOCIATED PROTEIN 1; PROTEIN BAX; RAS ASSOCIATION DOMAIN FAMILY PROTEIN 1A; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND;

EID: 20444414891     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.05.010     Document Type: Article
Times cited : (150)

References (39)
  • 1
    • 0036899079 scopus 로고    scopus 로고
    • Apoptosomes: Engines for caspase activation
    • J.M. Adams, and S. Cory Apoptosomes: engines for caspase activation Curr. Opin. Cell Biol. 14 2002 715 720
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 715-720
    • Adams, J.M.1    Cory, S.2
  • 3
    • 0037089068 scopus 로고    scopus 로고
    • BH3-only proteins - Evolutionarily conserved proapoptotic Bcl-2 family members essential for initiating programmed cell death
    • P. Bouillet, and A. Strasser BH3-only proteins - evolutionarily conserved proapoptotic Bcl-2 family members essential for initiating programmed cell death J. Cell Sci. 115 2002 1567 1574
    • (2002) J. Cell Sci. , vol.115 , pp. 1567-1574
    • Bouillet, P.1    Strasser, A.2
  • 4
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • T.R. Brummelkamp, R. Bernards, and R. Agami A system for stable expression of short interfering RNAs in mammalian cells Science 296 2002 550 553
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 5
    • 0036478928 scopus 로고    scopus 로고
    • The Apaf-1 apoptosome: A large caspase-activating complex
    • K. Cain, S.B. Bratton, and G.M. Cohen The Apaf-1 apoptosome: a large caspase-activating complex Biochimie 84 2002 203 214
    • (2002) Biochimie , vol.84 , pp. 203-214
    • Cain, K.1    Bratton, S.B.2    Cohen, G.M.3
  • 6
    • 0031918223 scopus 로고    scopus 로고
    • BCL-2 family: Regulators of cell death
    • D.T. Chao, and S.J. Korsmeyer BCL-2 family: regulators of cell death Annu. Rev. Immunol. 16 1998 395 419
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 395-419
    • Chao, D.T.1    Korsmeyer, S.J.2
  • 7
    • 1642553461 scopus 로고    scopus 로고
    • The dark side of Ras: Regulation of apoptosis
    • A.D. Cox, and C.J. Der The dark side of Ras: regulation of apoptosis Oncogene 22 2003 8999 9006
    • (2003) Oncogene , vol.22 , pp. 8999-9006
    • Cox, A.D.1    Der, C.J.2
  • 8
    • 0033918563 scopus 로고    scopus 로고
    • Epigenetic inactivation of a RAS association domain family protein from the lung tumour suppressor locus 3p21.3
    • R. Dammann, C. Li, J.H. Yoon, P.L. Chin, S. Bates, and G.P. Pfeifer Epigenetic inactivation of a RAS association domain family protein from the lung tumour suppressor locus 3p21.3 Nat. Genet. 25 2000 315 319
    • (2000) Nat. Genet. , vol.25 , pp. 315-319
    • Dammann, R.1    Li, C.2    Yoon, J.H.3    Chin, P.L.4    Bates, S.5    Pfeifer, G.P.6
  • 11
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • N.N. Danial, and S.J. Korsmeyer Cell death: critical control points Cell 116 2004 205 219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 13
  • 15
    • 0037427443 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilisation by Bax/Bak
    • M.D. Esposti, and C. Dive Mitochondrial membrane permeabilisation by Bax/Bak Biochem. Biophys. Res. Commun. 304 2003 455 461
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 455-461
    • Esposti, M.D.1    Dive, C.2
  • 17
    • 0035378345 scopus 로고    scopus 로고
    • Cytochrome c release occurs via Ca2+-dependent and Ca2+-independent mechanisms that are regulated by Bax
    • V. Gogvadze, J.D. Robertson, B. Zhivotovsky, and S. Orrenius Cytochrome c release occurs via Ca2+-dependent and Ca2+-independent mechanisms that are regulated by Bax J. Biol. Chem. 276 2001 19066 19071
    • (2001) J. Biol. Chem. , vol.276 , pp. 19066-19071
    • Gogvadze, V.1    Robertson, J.D.2    Zhivotovsky, B.3    Orrenius, S.4
  • 18
    • 0037815277 scopus 로고    scopus 로고
    • Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis
    • N. Harper, M. Hughes, M. MacFarlane, and G.M. Cohen Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis J. Biol. Chem. 278 2003 25534 25541
    • (2003) J. Biol. Chem. , vol.278 , pp. 25534-25541
    • Harper, N.1    Hughes, M.2    MacFarlane, M.3    Cohen, G.M.4
  • 19
    • 4644345260 scopus 로고    scopus 로고
    • Splitting the apoptosome
    • A.T. Ho, and E. Zacksenhaus Splitting the apoptosome Cell Cycle 3 2004 446 448
    • (2004) Cell Cycle , vol.3 , pp. 446-448
    • Ho, A.T.1    Zacksenhaus, E.2
  • 20
    • 0038456210 scopus 로고    scopus 로고
    • Death receptors and melanoma resistance to apoptosis
    • V.N. Ivanov, A. Bhoumik, and Z. Ronai Death receptors and melanoma resistance to apoptosis Oncogene 22 2003 3152 3161
    • (2003) Oncogene , vol.22 , pp. 3152-3161
    • Ivanov, V.N.1    Bhoumik, A.2    Ronai, Z.3
  • 21
    • 0037379739 scopus 로고    scopus 로고
    • Involvement of proapoptotic molecules Bax and Bak in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced mitochondrial disruption and apoptosis: Differential regulation of cytochrome c and Smac/DIABLO release
    • K. Kandasamy, S.M. Srinivasula, E.S. Alnemri, C.B. Thompson, S.J. Korsmeyer, J.L. Bryant, and R.K. Srivastava Involvement of proapoptotic molecules Bax and Bak in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced mitochondrial disruption and apoptosis: differential regulation of cytochrome c and Smac/DIABLO release Cancer Res. 63 2003 1712 1721
    • (2003) Cancer Res. , vol.63 , pp. 1712-1721
    • Kandasamy, K.1    Srinivasula, S.M.2    Alnemri, E.S.3    Thompson, C.B.4    Korsmeyer, S.J.5    Bryant, J.L.6    Srivastava, R.K.7
  • 22
    • 0037427479 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: An introduction
    • G. Kroemer Mitochondrial control of apoptosis: an introduction Biochem. Biophys. Res. Commun. 304 2003 433 435
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 433-435
    • Kroemer, G.1
  • 24
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • A. Letai, M.C. Bassik, L.D. Walensky, M.D. Sorcinelli, S. Weiler, and S.J. Korsmeyer Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics Cancer Cell 2 2002 183 192
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 25
    • 0344825077 scopus 로고    scopus 로고
    • Control of microtubule stability by the RASSF1A tumor suppressor
    • L. Liu, S. Tommasi, D.H. Lee, R. Dammann, and G.P. Pfeifer Control of microtubule stability by the RASSF1A tumor suppressor Oncogene 22 2003 8125 8136
    • (2003) Oncogene , vol.22 , pp. 8125-8136
    • Liu, L.1    Tommasi, S.2    Lee, D.H.3    Dammann, R.4    Pfeifer, G.P.5
  • 26
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • O. Micheau, and J. Tschopp Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes Cell 114 2003 181 190
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 27
    • 0038025230 scopus 로고    scopus 로고
    • Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release
    • V. Mikhailov, M. Mikhailova, K. Degenhardt, M.A. Venkatachalam, E. White, and P. Saikumar Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release J. Biol. Chem. 278 2003 5367 5376
    • (2003) J. Biol. Chem. , vol.278 , pp. 5367-5376
    • Mikhailov, V.1    Mikhailova, M.2    Degenhardt, K.3    Venkatachalam, M.A.4    White, E.5    Saikumar, P.6
  • 28
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • S.J. Riedl, and Y. Shi Molecular mechanisms of caspase regulation during apoptosis Nat. Rev. Mol. Cell Biol. 5 2004 897 907
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 30
    • 0037427412 scopus 로고    scopus 로고
    • Mechanisms of cytochrome c release by proapoptotic BCL-2 family members
    • L. Scorrano, and S.J. Korsmeyer Mechanisms of cytochrome c release by proapoptotic BCL-2 family members Biochem. Biophys. Res. Commun. 304 2003 437 444
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 437-444
    • Scorrano, L.1    Korsmeyer, S.J.2
  • 31
    • 0036264815 scopus 로고    scopus 로고
    • The RASSF1A tumor suppressor blocks cell cycle progression and inhibits cyclin D1 accumulation
    • L. Shivakumar, J. Minna, T. Sakamaki, R. Pestell, and M.A. White The RASSF1A tumor suppressor blocks cell cycle progression and inhibits cyclin D1 accumulation Mol. Cell. Biol. 22 2002 4309 4318
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4309-4318
    • Shivakumar, L.1    Minna, J.2    Sakamaki, T.3    Pestell, R.4    White, M.A.5
  • 32
    • 4644232764 scopus 로고    scopus 로고
    • Control of APC-Cdc20 by the tumor suppressor RASSF1A
    • M.S. Song, and D.S. Lim Control of APC-Cdc20 by the tumor suppressor RASSF1A Cell Cycle 3 2004 574 576
    • (2004) Cell Cycle , vol.3 , pp. 574-576
    • Song, M.S.1    Lim, D.S.2
  • 33
    • 0035976902 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K
    • R. Sundararajan, A. Cuconati, D. Nelson, and E. White Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K J. Biol. Chem. 276 2001 45120 45127
    • (2001) J. Biol. Chem. , vol.276 , pp. 45120-45127
    • Sundararajan, R.1    Cuconati, A.2    Nelson, D.3    White, E.4
  • 34
    • 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
    • K.O. Tan, K.M. Tan, S.L. Chan, K.S. Yee, M. Bevort, K.C. Ang, and V.C. Yu MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains J. Biol. Chem. 276 2001 2802 2807
    • (2001) J. Biol. Chem. , 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    Yu, V.C.7
  • 35
    • 0242656497 scopus 로고    scopus 로고
    • Death receptor-induced cell killing
    • A. Thorburn Death receptor-induced cell killing Cell. Signal. 16 2004 139 144
    • (2004) Cell. Signal. , vol.16 , pp. 139-144
    • Thorburn, A.1
  • 37
    • 0037075898 scopus 로고    scopus 로고
    • Activation of the p53 tumor suppressor protein
    • K.H. Vousden Activation of the p53 tumor suppressor protein Biochim. Biophys. Acta 1602 2002 47 59
    • (2002) Biochim. Biophys. Acta , vol.1602 , pp. 47-59
    • Vousden, K.H.1
  • 39
    • 0032799633 scopus 로고    scopus 로고
    • Caspases: Their intracellular localization and translocation during apoptosis
    • B. Zhivotovsky, A. Samali, A. Gahm, and S. Orrenius Caspases: their intracellular localization and translocation during apoptosis Cell Death Differ. 6 1999 644 651
    • (1999) Cell Death Differ. , vol.6 , pp. 644-651
    • Zhivotovsky, B.1    Samali, A.2    Gahm, A.3    Orrenius, S.4


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