Gene

Caspase 3

Programmed cell death

Cell biology

Bcl-2-associated X protein

Inner mitochondrial membrane

Biology

Cytochrome c

Apoptosis

Biochemistry

Caspase

Bacterial outer membrane

Mitochondrial apoptosis-induced channel

Voltage-dependent anion channel

Bcl-2 family

Effector

Escherichia coli

Mitochondrion

Chemistry

Biochimica et Biophysica Acta (BBA) - Biomembranes

Mitochondrial outer membrane permeabilization (MOMP) is a key checkpoint in apoptosis that activates the caspase cascade and irreversibly causes the majority of cells to die. The proteins of the Bcl-2 family are master regulators of apoptosis that form a complex interaction network within the mitochondrial membrane that determines the induction of MOMP. This culminates in the activation of the effector members Bax and Bak, which permeabilize the mitochondrial outer membrane to mediate MOMP. Although the key role of Bax and Bak has been established, many questions remain unresolved regarding molecular mechanisms that control the apoptotic pore. In this review, we discuss the recent progress in our understanding of the regulation of Bax/Bak activity within the mitochondrial membrane.

Apoptosis regulation at the mitochondria membrane level