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Abstract
The pro-apoptotic Bax protein is the main effector of mitochondrial permeabilization during apoptosis. Bax is controlled at several levels, including post-translational modifications such as phosphorylation and S-palmitoylation. However, little is known about the contribution of other protein modifications to Bax activity. Here, we used heterologous expression of human Bax in yeast to study the involvement of N-terminal acetylation by yNaa20p (yNatB) on Bax function. We found that human Bax is N-terminal (Nt-)acetylated by yNaa2Op and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast and Mouse Embryonic Fibroblast (MEF) cells. Bax accumulates in the mitochondria of yeast naa20A and Naa25(-/-) MEF cells, but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax. Altogether, our results show that Bax N-terminal acetylation by NatB is involved in its mitochondrial targeting.
Keywords
Apoptosis, Bax, N-terminal acetyltransferase, NatB, N-terminal acetylation, Mitochondria, INDUCED CELL-DEATH, KINASE-C ISOFORMS, INTRACELLULAR-LOCALIZATION, YEAST MITOCHONDRIA, ALPHA-ACETYLATION, PROTEIN, APOPTOSIS, ACETYLTRANSFERASES, SURVIVAL, CANCER

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MLA
Alves, Sara, et al. “N-Terminal Acetylation Modulates Bax Targeting to Mitochondria.” INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, vol. 95, 2018, pp. 35–42.
APA
Alves, S., Neiri, L., Chaves, S. R., Vieira, S., Trindade, D., Manon, S., … Côrte-Real, M. (2018). N-terminal acetylation modulates Bax targeting to mitochondria. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 95, 35–42.
Chicago author-date
Alves, Sara, Leire Neiri, Susana Rodrigues Chaves, Selma Vieira, Dário Trindade, Stephen Manon, Veronica Dominguez, et al. 2018. “N-Terminal Acetylation Modulates Bax Targeting to Mitochondria.” INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY 95: 35–42.
Chicago author-date (all authors)
Alves, Sara, Leire Neiri, Susana Rodrigues Chaves, Selma Vieira, Dário Trindade, Stephen Manon, Veronica Dominguez, Belen Pintado, Veronique Jonckheere, Petra Van Damme, Rui Duarte Silva, Rafael Aldabe, and Manuela Côrte-Real. 2018. “N-Terminal Acetylation Modulates Bax Targeting to Mitochondria.” INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY 95: 35–42.
Vancouver
1.
Alves S, Neiri L, Chaves SR, Vieira S, Trindade D, Manon S, et al. N-terminal acetylation modulates Bax targeting to mitochondria. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY. 2018;95:35–42.
IEEE
[1]
S. Alves et al., “N-terminal acetylation modulates Bax targeting to mitochondria,” INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, vol. 95, pp. 35–42, 2018.
@article{8553810,
  abstract     = {The pro-apoptotic Bax protein is the main effector of mitochondrial permeabilization during apoptosis. Bax is controlled at several levels, including post-translational modifications such as phosphorylation and S-palmitoylation. However, little is known about the contribution of other protein modifications to Bax activity. Here, we used heterologous expression of human Bax in yeast to study the involvement of N-terminal acetylation by yNaa20p (yNatB) on Bax function. We found that human Bax is N-terminal (Nt-)acetylated by yNaa2Op and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast and Mouse Embryonic Fibroblast (MEF) cells. Bax accumulates in the mitochondria of yeast naa20A and Naa25(-/-) MEF cells, but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax. Altogether, our results show that Bax N-terminal acetylation by NatB is involved in its mitochondrial targeting.},
  author       = {Alves, Sara and Neiri, Leire and Chaves, Susana Rodrigues and Vieira, Selma and Trindade, Dário and Manon, Stephen and Dominguez, Veronica and Pintado, Belen and Jonckheere, Veronique and Van Damme, Petra and Silva, Rui Duarte and Aldabe, Rafael and Côrte-Real, Manuela},
  issn         = {1357-2725},
  journal      = {INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY},
  keywords     = {Apoptosis,Bax,N-terminal acetyltransferase,NatB,N-terminal acetylation,Mitochondria,INDUCED CELL-DEATH,KINASE-C ISOFORMS,INTRACELLULAR-LOCALIZATION,YEAST MITOCHONDRIA,ALPHA-ACETYLATION,PROTEIN,APOPTOSIS,ACETYLTRANSFERASES,SURVIVAL,CANCER},
  language     = {eng},
  pages        = {35--42},
  title        = {N-terminal acetylation modulates Bax targeting to mitochondria},
  url          = {http://dx.doi.org/10.1016/j.biocel.2017.12.004},
  volume       = {95},
  year         = {2018},
}

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