The Bax carboxy-terminal hydrophobic helix does not determine organelle-specific targeting but is essential for maintaining Bax in an inactive state and for stable mitochondrial membrane insertion.

Abstract excerpt

Here we address the function of the hydrophobic carboxy-terminal tail of the pro-apoptotic protein Bax. The tail is tucked into a hydrophobic pocket within the closed/inactive conformation of Bax. Apoptotic stimulation changes the Bax conformation, exposing a mitochondrial-targeting signal. We confirmed that the Bax tail alone can specifically target and anchor a passenger protein to the mitochondria....

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