Bax contains BH1, BH2, and BH3 domains, which are crucial for its pro-apoptotic function. It accelerates programmed cell death by binding to and antagonizing the apoptosis repressor Bcl-2 or its adenovirus homolog E1B 19K protein . Bax induces the release of cytochrome c, activation of caspase-3, and thereby apoptosis .
Bax plays a critical role in the regulation of apoptosis. It promotes cell death by disrupting the mitochondrial membrane potential, leading to the release of cytochrome c and activation of the caspase cascade . This process is essential for maintaining cellular homeostasis and eliminating damaged or unwanted cells.
Upon receiving apoptotic signals, Bax undergoes a conformational change and translocates from the cytosol to the mitochondrial membrane . This translocation is triggered by various factors, including heat, pH changes, and oxidative stress . Bax can also be activated by binding to other Bcl-2 family proteins, such as Bcl-2, Bcl-xL, and Bid .
The expression and activity of Bax are tightly regulated by multiple mechanisms. The tumor suppressor protein p53 upregulates Bax expression in response to cellular stress . Additionally, post-translational modifications, such as phosphorylation and ubiquitination, can modulate Bax activity and stability .