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Volumn 258, Issue 1, 1998, Pages 19-28

Under respiratory growth conditions, Bcl-x(L) and Bcl-2 are unable to overcome yeast cell death triggered by a mutant Bax protein lacking the membrane anchor

Author keywords

Apoptosis; Bax; Bcl 2; Bcl x(L); Membrane anchor

Indexed keywords

PROTEIN BAX;

EID: 0032533976     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2580019.x     Document Type: Article
Times cited : (16)

References (36)
  • 1
    • 0028212937 scopus 로고
    • Apoptosis and its role in human disease
    • Barr, P. J. & Tomei, L. D. (1994) Apoptosis and its role in human disease, Biotechnology 12, 487-493.
    • (1994) Biotechnology , vol.12 , pp. 487-493
    • Barr, P.J.1    Tomei, L.D.2
  • 2
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson, C. B. (1995) Apoptosis in the pathogenesis and treatment of disease, Science 267, 1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 3
    • 0030046508 scopus 로고    scopus 로고
    • Life, death, and the pursuit of apoptosis
    • White, E. (1996) Life, death, and the pursuit of apoptosis, Genes and Devel. 10, 1-15.
    • (1996) Genes and Devel. , vol.10 , pp. 1-15
    • White, E.1
  • 5
    • 0028956550 scopus 로고
    • Regulators of cell death
    • Korsmeyer, S. J. (1995) Regulators of cell death. Trends Genet. 11, 101-105.
    • (1995) Trends Genet. , vol.11 , pp. 101-105
    • Korsmeyer, S.J.1
  • 6
    • 0028040019 scopus 로고
    • Bcl-2 and the regulation of programmed cell death
    • Reed, J. C. (1994) Bcl-2 and the regulation of programmed cell death, J. Cell Biol. 124, 1 -6.
    • (1994) J. Cell Biol. , vol.124 , pp. 1-6
    • Reed, J.C.1
  • 7
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog Bax, that accelerates programed cell death
    • Oltvai, Z. N., Milliman, C. L. & Korsmeyer. S. J. (1993) Bcl-2 heterodimerizes in vivo with a conserved homolog Bax, that accelerates programed cell death. Cell 74. 609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 11
    • 0029917541 scopus 로고    scopus 로고
    • Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2
    • Zha, H., Aimé-Sempé. C., Sato, T. & Reed. J. C. (1996) Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J. Biol. Chem. 271. 7440-7444.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7440-7444
    • Zha, H.1    Aimé-Sempé, C.2    Sato, T.3    Reed, J.C.4
  • 12
    • 0030047365 scopus 로고    scopus 로고
    • Functional dissection of the human Bcl-2 protein: Sequence requirements for inhibition of apoptosis
    • Hunter, J. J., Bond. B. L. & Parslow, T. G. ( 1996) Functional dissection of the human Bcl-2 protein: sequence requirements for inhibition of apoptosis, Mol. Cell. Biol. 16. 877-883.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 877-883
    • Hunter, J.J.1    Bond, B.L.2    Parslow, T.G.3
  • 13
    • 0028289951 scopus 로고
    • Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by EIB-defective adenovirus
    • Nguyen, M., Branton. P. E., Walton, P. A., Oltvai, Z. N., Korsmeyer, S. J. & Shore, G. C. ( 1994) Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by EIB-defective adenovirus, J. Biol. Chem. 269, 16521-16524.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16521-16524
    • Nguyen, M.1    Branton, P.E.2    Walton, P.A.3    Oltvai, Z.N.4    Korsmeyer, S.J.5    Shore, G.C.6
  • 14
    • 0027977928 scopus 로고
    • The protein product of the oncogene Bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane
    • Lithgow, T, van-Driel, R., Bertram. J. F. & Strasser, A. (1994) The protein product of the oncogene Bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane. Cell Growth Differ. 5, 411 -417.
    • (1994) Cell Growth Differ. , vol.5 , pp. 411-417
    • Lithgow, T.1    Van-Driel, R.2    Bertram, J.F.3    Strasser, A.4
  • 15
    • 0028170778 scopus 로고
    • Bel-XL is the major Bcl-x mRNAform expressed during murine development and its product localizes to mitochondria
    • González-Garcia, M., Perez-Ballestero. R., Ding, L., Duan, L., Boise, L. H., Thompson, C. B. & Nuñez. G. (1994) Bel-XL is the major Bcl-x mRNAform expressed during murine development and its product localizes to mitochondria. Development 120. 3033-3042.
    • (1994) Development , vol.120 , pp. 3033-3042
    • González-Garcia, M.1    Perez-Ballestero, R.2    Ding, L.3    Duan, L.4    Boise, L.H.5    Thompson, C.B.6    Nuñez, G.7
  • 16
    • 0029024368 scopus 로고
    • Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and isolation of a novel alternatively spliced transcript, BAX delta
    • Apte, S. S., Mattei, M.-G. & Olsen. B. R. (1995) Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and isolation of a novel alternatively spliced transcript, BAX delta. Genomics 26. 592-594.
    • (1995) Genomics , vol.26 , pp. 592-594
    • Apte, S.S.1    Mattei, M.-G.2    Olsen, B.R.3
  • 17
    • 0029848765 scopus 로고    scopus 로고
    • Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells
    • Zha. H., Fisk, H. A., Yaffe, M. P., Mahajan, N., Herman. B. & Reed. J. C. (1996) Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells. Mol. Cell. Biol. 16. 6494-6508.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6494-6508
    • Zha, H.1    Fisk, H.A.2    Yaffe, M.P.3    Mahajan, N.4    Herman, B.5    Reed, J.C.6
  • 18
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-x(L) during apoptosis
    • Hsu. Y.-T, Wolter. K. G. & Youle, R. J. (1997) Cytosol-to-membrane redistribution of Bax and Bcl-x(L) during apoptosis. Proc. Natl Acad. Sci. USA 94, 3668-3672.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3668-3672
    • Hsu, Y.-T.1    Wolter, K.G.2    Youle, R.J.3
  • 20
    • 0030052107 scopus 로고    scopus 로고
    • Role of mitochondria and C-terminal membrane anchor of Bcl-2 in Bax induced growth arrest and mortality in Saccharomyces cerevisiae
    • Greenhalf, W., Stephan, C. & Chaudhuri, B. (1996) Role of mitochondria and C-terminal membrane anchor of Bcl-2 in Bax induced growth arrest and mortality in Saccharomyces cerevisiae, FEBS Lett. 380, 169-175.
    • (1996) FEBS Lett. , vol.380 , pp. 169-175
    • Greenhalf, W.1    Stephan, C.2    Chaudhuri, B.3
  • 22
    • 7844239016 scopus 로고
    • Analysis of the structure, transcripts, and protein products of Bcl-2, the gene involved in human follicular lymphoma
    • Croce, C. M. (1986) Analysis of the structure, transcripts, and protein products of Bcl-2, the gene involved in human follicular lymphoma, Proc. Natl Acad. Sci. USA 88, 1731-1735.
    • (1986) Proc. Natl Acad. Sci. USA , vol.88 , pp. 1731-1735
    • Croce, C.M.1
  • 24
    • 0026524634 scopus 로고
    • Carbon catabolite repression in yeast
    • Gancedo. J. M. (1992) Carbon catabolite repression in yeast, Eur. J. Biochem. 206, 297-313.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 297-313
    • Gancedo, J.M.1
  • 25
    • 0028533188 scopus 로고
    • Dynamics of the respiratory bottleneck of Saccharomyces cerevisiae
    • Sonnleitner. B. & Hahnemann, U. (1994) Dynamics of the respiratory bottleneck of Saccharomyces cerevisiae, J. Biotechnol. 38, 63-79.
    • (1994) J. Biotechnol. , vol.38 , pp. 63-79
    • Sonnleitner, B.1    Hahnemann, U.2
  • 27
    • 0028019746 scopus 로고
    • Cell-free apoptosis in Xenopus egg extracts: Inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria
    • Newmeyer, D. D., Farschon, D. M. & Reed, J. C. (1994) Cell-free apoptosis in Xenopus egg extracts: inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria, Cell 79, 353-364.
    • (1994) Cell , vol.79 , pp. 353-364
    • Newmeyer, D.D.1    Farschon, D.M.2    Reed, J.C.3
  • 28
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang, J., Liu, X., Bhalla, K., Kirn, N., Ibrado, A. M., Cai, J., Peng, T., Jones, D. P. & Wang, X. (1997) Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked, Science 275, 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kirn, N.4    Ibrado, A.M.5    Cai, J.6    Peng, T.7    Jones, D.P.8    Wang, X.9
  • 30
    • 0343267405 scopus 로고    scopus 로고
    • Energy supply and the shape of death in neurons and lymphoid cells
    • Nicotera, P. & Leist, M. (1997) Energy supply and the shape of death in neurons and lymphoid cells, Cell Death & Diff. 4, 435-442.
    • (1997) Cell Death & Diff. , vol.4 , pp. 435-442
    • Nicotera, P.1    Leist, M.2
  • 31
    • 0032549012 scopus 로고    scopus 로고
    • Death-defying yeast identify novel apoptosis genes
    • Shaham, S., Shuman, M. A. & Herskowitz, I. (1998) Death-defying yeast identify novel apoptosis genes, Cell 92, 425-427.
    • (1998) Cell , vol.92 , pp. 425-427
    • Shaham, S.1    Shuman, M.A.2    Herskowitz, I.3
  • 32
    • 0030777253 scopus 로고    scopus 로고
    • Release of cytochrome c and decrease of cytochrome c-oxidase in Bax-expressing yeast cells, and prevention of these effects by coexpression of Bcl-xL
    • Manon, S., Chaudhuri, B. & Guérin, M. (1997) Release of cytochrome c and decrease of cytochrome c-oxidase in Bax-expressing yeast cells, and prevention of these effects by coexpression of Bcl-xL, FEBS Lett. 415, 29-32.
    • (1997) FEBS Lett. , vol.415 , pp. 29-32
    • Manon, S.1    Chaudhuri, B.2    Guérin, M.3
  • 34
    • 0032571294 scopus 로고    scopus 로고
    • The overexpression of bax produces cell death upon induction of the mitochondrial permeability transition
    • Pastorino, J. G., Chen. S. T., Tafani, M., Snyder, J. W. & Farber, J. L. (1998) The overexpression of bax produces cell death upon induction of the mitochondrial permeability transition, J. Biol. Chem. 273, 7770-7775.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7770-7775
    • Pastorino, J.G.1    Chen, S.T.2    Tafani, M.3    Snyder, J.W.4    Farber, J.L.5
  • 35
    • 0029906828 scopus 로고    scopus 로고
    • Bax-induced cell death may not require interleukin 1-beta-converting enzyme-like proteases
    • Xiang, J. L., Chao, D. T. & Korsmeyer, S. J. (1996) Bax-induced cell death may not require interleukin 1-beta-converting enzyme-like proteases, Proc. Natl Acad. Sci. USA 93, 14559-14563.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14559-14563
    • Xiang, J.L.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 36
    • 0031993255 scopus 로고    scopus 로고
    • Bax inhihitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast
    • Xu, Q. & Reed. J. C. (1998) Bax inhihitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast. Mol. Cell I, 337-346.
    • (1998) Mol. Cell , vol.1 , pp. 337-346
    • Xu, Q.1    Reed, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.