The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis
In a cell-free apoptosis system, mitochondria spontaneously released cytochrome c, which
activated DEVD-specific caspases, leading to fodrin cleavage and apoptotic nuclear …
activated DEVD-specific caspases, leading to fodrin cleavage and apoptotic nuclear …
Ordering the cytochrome c–initiated caspase cascade: hierarchical activation of caspases-2,-3,-6,-7,-8, and-10 in a caspase-9–dependent manner
EA Slee, MT Harte, RM Kluck, BB Wolf… - The Journal of cell …, 1999 - rupress.org
Exit of cytochrome c from mitochondria into the cytosol has been implicated as an important
step in apoptosis. In the cytosol, cytochrome c binds to the CED-4 homologue, Apaf-1, …
step in apoptosis. In the cytosol, cytochrome c binds to the CED-4 homologue, Apaf-1, …
Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak
A central issue in the regulation of apoptosis by the Bcl-2 family is whether its BH3-only
members initiate apoptosis by directly binding to the essential cell-death mediators Bax and Bak, …
members initiate apoptosis by directly binding to the essential cell-death mediators Bax and Bak, …
[HTML][HTML] Molecular biology of Bax and Bak activation and action
…, G Dewson, PE Czabotar, RM Kluck - Biochimica et Biophysica …, 2011 - Elsevier
Bax and Bak are two nuclear-encoded proteins present in higher eukaryotes that are able to
pierce the mitochondrial outer membrane to mediate cell death by apoptosis. Thus, …
pierce the mitochondrial outer membrane to mediate cell death by apoptosis. Thus, …
[HTML][HTML] Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis
In stressed cells, apoptosis ensues when Bcl-2 family members Bax or Bak oligomerize and
permeabilize the mitochondrial outer membrane. Certain BH3-only relatives can directly …
permeabilize the mitochondrial outer membrane. Certain BH3-only relatives can directly …
[HTML][HTML] Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis
D Westphal, RM Kluck, G Dewson - Cell Death & Differentiation, 2014 - nature.com
The central role of the Bcl-2 family in regulating apoptotic cell death was first identified in the
1980s. Since then, significant in-roads have been made in identifying the multiple members …
1980s. Since then, significant in-roads have been made in identifying the multiple members …
Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis
G Dewson, RM Kluck - Journal of cell science, 2009 - journals.biologists.com
… Kluck; Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis. J
Cell Sci 15 August 2009; 122 (16): 2801–2808. doi: https://doi.org/10.1242/jcs.038166 …
Cell Sci 15 August 2009; 122 (16): 2801–2808. doi: https://doi.org/10.1242/jcs.038166 …
[HTML][HTML] To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3: groove interactions
…, H Puthalakath, JM Adams, PM Colman, RM Kluck - Molecular cell, 2008 - cell.com
The Bcl-2 relative Bak is thought to drive apoptosis by forming homo-oligomers that
permeabilize mitochondria, but how it is activated and oligomerizes is unclear. To clarify these …
permeabilize mitochondria, but how it is activated and oligomerizes is unclear. To clarify these …
The pro-apoptotic proteins, Bid and Bax, cause a limited permeabilization of the mitochondrial outer membrane that is enhanced by cytosol
RM Kluck, MD Esposti, G Perkins, C Renken… - The Journal of cell …, 1999 - rupress.org
… 2 F), which also induced complete release of cytochrome c (Kluck and Newmeyer, unpublished).
However, no such pores were observed in mitochondria depleted of cytochrome c by …
However, no such pores were observed in mitochondria depleted of cytochrome c by …
[HTML][HTML] Cytochrome c activation of CPP32‐like proteolysis plays a critical role in a Xenopus cell‐free apoptosis system
RM Kluck, SJ Martin, BM Hoffman, JS Zhou… - The EMBO …, 1997 - embopress.org
… Furthermore, when mitochondria isolated from S.cerevisiae were incubated in Xenopus
extracts, they released yeast cytochrome c but did not induce apoptotic changes (RMKluck, DR…
extracts, they released yeast cytochrome c but did not induce apoptotic changes (RMKluck, DR…