The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast

AbstractThe role of the mitochondrial protein receptor Tom22p in the interaction of pro-apoptotic protein Bax with yeast mitochondria was investigated. Co-immunoprecipitation assays showed that human Bax interacted with different TOM subunits, including Tom22p. Expression of the cytosolic receptor domain of human Tom22 increased Bax mitochondrial localization, but decreased the proportion of active Bax. BN–PAGE showed that the cytosolic domain of Tom22 interfered with the oligomerization of Bax. These data suggest that the interaction with the cytosolic domain of Tom22 helps Bax to acquire a conformation able to interact with the outer mitochondrial membrane.Structured summary of protein interactionsBAX and BAXphysically interact with TOM22 by anti bait coimmunoprecipitation (View interaction)BAXphysically interacts with TOM70 by anti bait coimmunoprecipitation (View interaction)BAXphysically interacts with TOM22, TOM70 and TOM40 by anti bait coimmunoprecipitation (View interaction)BAXphysically interacts with TOM22 by anti bait coimmunoprecipitation (View interaction)BAX and BAX bind by blue native page (View interaction)BAXphysically interacts with TOM40 by anti bait coimmunoprecipitation (View interaction