BAK1
Description
The BAK1 (BCL2 antagonist/killer 1) is a protein-coding gene located on chromosome 6.
BAK1, encoded by the BAK1 gene on chromosome 6, is a member of the BCL2 protein family. It is localized to mitochondria and functions as an apoptosis inducer. BAK1 interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, leading to a loss of membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 in response to cellular stress. It contains four Bcl-2 homology (BH) domains (BH1, BH2, BH3, and BH4), organized as nine α-helices. The hydrophobic α-helix core is surrounded by amphipathic helices, with a transmembrane C-terminal α-helix anchoring it to the mitochondrial outer membrane. In its active form, BAK1 possesses a hydrophobic groove that binds the BH3 domain of other BCL-2 proteins. As a pro-apoptotic regulator, BAK1 participates in various cellular activities.
BAK1 is a crucial player in the mitochondrial apoptotic pathway. When the cell receives signals indicating death, BAK1 orchestrates the permeabilization of the mitochondrial outer membrane (MOM). It achieves this by forming oligomers, creating pores within the MOM. These pores release pro-apoptotic factors into the cytosol, including cytochrome c. This release triggers the activation of caspase 9, which subsequently activates effector caspases, leading to the execution of programmed cell death.
BAK1 is also known as BAK, BAK-LIKE, BCL2L7, CDN1.
