White, M. J. et al. Apoptotic caspases suppress mtDNA-induced STING-mediated type I IFN production. Cell 159, 1549–1562 (2014).
Article CAS PubMed PubMed Central Google Scholar
Riley, J. S. et al. Mitochondrial inner membrane permeabilisation enables mtDNA release during apoptosis. EMBO J. 37, e99238 (2018).
Article PubMed PubMed Central Google Scholar
Czabotar, P. E. & Garcia-Saez, A. J. Mechanisms of BCL-2 family proteins in mitochondrial apoptosis. Nat. Rev. Mol. Cell Biol. 24, 732–748 (2023).
Article CAS PubMed Google Scholar
Subburaj, Y. et al. Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species. Nat. Commun. 6, 8042 (2015).
Article CAS PubMed Google Scholar
Dewson, G. et al. Bax dimerizes via a symmetric BH3:groove interface during apoptosis. Cell Death Differ. 19, 661–670 (2012).
Article CAS PubMed Google Scholar
Dewson, G. et al. To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions. Mol. Cell 30, 369–380 (2008).
Article CAS PubMed Google Scholar
Czabotar, P. E. et al. Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis. Cell 152, 519–531 (2013).
Article CAS PubMed Google Scholar
Vandenabeele, P., Bultynck, G. & Savvides, S. N. Pore-forming proteins as drivers of membrane permeabilization in cell death pathways. Nat. Rev. Mol. Cell Biol. 24, 312–333 (2023).
Article CAS PubMed Google Scholar
Cowan, A. D. et al. BAK core dimers bind lipids and can be bridged by them. Nat. Struct. Mol. Biol. 27, 1024–1031 (2020).
Article CAS PubMed Google Scholar
Miller, M. S. et al. Sequence differences between BAX and BAK core domains manifest as differences in their interactions with lipids. FEBS J. https://doi.org/10.1111/febs.17031 (2023).
Salvador-Gallego, R. et al. Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores. EMBO J. 35, 389–401 (2016).
Article CAS PubMed PubMed Central Google Scholar
Grosse, L. et al. Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis. EMBO J. 35, 402–413 (2016).
Article CAS PubMed PubMed Central Google Scholar
Cosentino, K. et al. The interplay between BAX and BAK tunes apoptotic pore growth to control mitochondrial-DNA-mediated inflammation. Mol. Cell 82, 933–949 e939 (2022).
Article CAS PubMed PubMed Central Google Scholar
McArthur, K. et al. BAK/BAX macropores facilitate mitochondrial herniation and mtDNA efflux during apoptosis. Science 359, eaao6047 (2018).
Rongvaux, A. et al. Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA. Cell 159, 1563–1577 (2014).
Article CAS PubMed PubMed Central Google Scholar
Shalaby, R., Diwan, A., Flores-Romero, H., Hertlein, V. & Garcia-Saez, A. J. Visualization of BOK pores independent of BAX and BAK reveals a similar mechanism with differing regulation. Cell Death Differ. 30, 731–741 (2023).
Article CAS PubMed Google Scholar
Llambi, F. et al. BOK is a non-canonical BCL-2 family effector of apoptosis regulated by ER-associated degradation. Cell 165, 421–433 (2016).
Article CAS PubMed PubMed Central Google Scholar
Flores-Romero, H. et al. BCL-2-family protein tBID can act as a BAX-like effector of apoptosis. EMBO J. 41, e108690 (2022).
Article CAS PubMed Google Scholar
Ke, F. S. et al. The BCL-2 family member BID plays a role during embryonic development in addition to its BH3-only protein function by acting in parallel to BAX, BAK and BOK. EMBO J. 41, e110300 (2022).
Article CAS PubMed PubMed Central Google Scholar
Diepstraten, S. T. et al. The manipulation of apoptosis for cancer therapy using BH3-mimetic drugs. Nat. Rev. Cancer 22, 45–64 (2022).
Article CAS PubMed Google Scholar
Gitego, N. et al. Chemical modulation of cytosolic BAX homodimer potentiates BAX activation and apoptosis. Nat. Commun. 14, 8381 (2023).
Article CAS PubMed PubMed Central Google Scholar
Li, K., van Delft, M. F. & Dewson, G. Too much death can kill you: inhibiting intrinsic apoptosis to treat disease. EMBO J. 40, e107341 (2021).
Article CAS PubMed PubMed Central Google Scholar
Victorelli, S. et al. Apoptotic stress causes mtDNA release during senescence and drives the SASP. Nature 622, 627–636 (2023).
Article CAS PubMed PubMed Central Google Scholar
Kale, J., Osterlund, E. J. & Andrews, D. W. BCL-2 family proteins: changing partners in the dance towards death. Cell Death Differ. 25, 65–80 (2018).
Article CAS PubMed Google Scholar
Li, P. et al. SUMO modification in apoptosis. J. Mol. Histol. 52, 1–10 (2021).
Phu, L. et al. Dynamic regulation of mitochondrial import by the ubiquitin system. Mol. Cell 77, 1107–1123.e10 (2020).
Article CAS PubMed Google Scholar
Djajawi, T. M. et al. MARCH5 requires MTCH2 to coordinate proteasomal turnover of the MCL1:NOXA complex. Cell Death Differ. 27, 2484–2499 (2020).
Article CAS PubMed PubMed Central Google Scholar
Subramanian, A., Andronache, A., Li, Y. C. & Wade, M. Inhibition of MARCH5 ubiquitin ligase abrogates MCL1-dependent resistance to BH3 mimetics via NOXA. Oncotarget 7, 15986–16002 (2016).
Article PubMed PubMed Central Google Scholar
Haschka, M. D. et al. MARCH5-dependent degradation of MCL1/NOXA complexes defines susceptibility to antimitotic drug treatment. Cell Death Differ. 27, 2297–2312 (2020).
Article CAS PubMed PubMed Central Google Scholar
Huang, A. S. et al. Mitochondrial E3 ubiquitin ligase MARCHF5 controls BAK apoptotic activity independently of BH3-only proteins. Cell Death Differ. 30, 632–646 (2023).
Article CAS PubMed Google Scholar
Narendra, D., Tanaka, A., Suen, D. F. & Youle, R. J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183, 795–803 (2008).
留言 (0)