What role do caspases play in the process of apoptosis?

Caspases are a family of cysteine proteases that play a pivotal role in the process of apoptosis, which is the programmed cell death that is essential for maintaining homeostasis and development in multicellular organisms. Apoptosis involves a series of tightly regulated biochemical events, and caspases are critical to executing these events.

When apoptosis is triggered, caspases become activated in a cascade-like manner. They cleave a variety of specific cellular proteins, leading to the systematic dismantling of the cell. This cleavage of proteins includes structural proteins of the cytoskeleton, lamin proteins of the nuclear envelope, and various signaling molecules, ultimately resulting in the morphological changes associated with apoptosis such as cell shrinkage, membrane blebbing, and DNA fragmentation. By cleaving these proteins, caspases help ensure that the cell dismantles in a controlled manner without spilling its contents into the surrounding tissue, which would provoke inflammation.

In this context, the other options do not appropriately describe the role of caspases in apoptosis. While signal transduction involves the transmission of molecular signals from a cell’s exterior to its interior, it is not a direct function of caspases. DNA damage repair is a process primarily mediated by other mechanisms and proteins that address and