Final answer:
Effector caspases activated through the extrinsic pathway of apoptosis, lead to the inhibition of Bcl2 by proapoptotic factors.
Step-by-step explanation:
After being activated by effector caspases through the extrinsic pathway of apoptosis, proapoptotic factors inhibit Bcl2. Caspases are a family of proteolytic enzymes that are essential in the process of programmed cell death or apoptosis. During apoptosis, various caspases are involved in a cascade where they are sequentially activated. The active caspases, specifically the effector caspases like caspase-3, start the auto-digestion of the cell by cleaving cellular substrates and triggering the apoptotic changes.
It is not explicitly given in the reference information which molecule specifically inhibits Bcl2 after caspase activation, but typically, in the intrinsic pathway of apoptosis, proapoptotic members of the Bcl2 family such as Bax and Bak are involved in this process. They counter the anti-apoptotic effects of Bcl2 by promoting mitochondrial outer membrane permeabilization (MOMP) and the subsequent release of cytochrome c leading to caspase activation.