Inhibition of Bcl-2 leads to the initiation of apoptosis because: A. Bcl-2 binds
ID: 42557 • Letter: I
Question
Inhibition of Bcl-2 leads to the initiation of apoptosis because:
A.
Bcl-2 binds directly to & inactivates SMAC/DIABLO.
B.
Bcl-2 binds directly to & inactivates cytochrome c.
C.
Bcl-2 is the most upstream pro-apoptotic factor in the intrinsic apoptotic pathway.
D.
Bak and Bax are now free to form channels, within the mitochondrial outer membrane, that allow for the movement of cytochrome c and SMAC/DIABLO into the cytosol.
E.
cytochrome c is now free to dissociate from Apaf-1, which leads to full activation of the apoptosome.
A.
Bcl-2 binds directly to & inactivates SMAC/DIABLO.
B.
Bcl-2 binds directly to & inactivates cytochrome c.
C.
Bcl-2 is the most upstream pro-apoptotic factor in the intrinsic apoptotic pathway.
D.
Bak and Bax are now free to form channels, within the mitochondrial outer membrane, that allow for the movement of cytochrome c and SMAC/DIABLO into the cytosol.
E.
cytochrome c is now free to dissociate from Apaf-1, which leads to full activation of the apoptosome.
Explanation / Answer
A. Bcl-2 binds directly to & inactivates SMAC/DIABLO.
SMACs (small mitochondria-derived activator of caspases) are known as Mitochondrial proteins that are released into the cytosol following an increase in permeability. small mitochondria-derived activator of caspases binds to inhibitor of apoptosis proteins (IAPs) and deactivates them, preventing the inhibitor of apoptosis proteins from arresting the apoptotic process and therefore allowing apoptosis to initiate