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• W3171559655 abstract "The conformational changes converting BAX from an inert cytosolic monomer into the homo-oligomers that permeabilize the mitochondrial outer membrane (MOM) are crucial steps toward apoptosis. Here, we have explored the potential role of the BAX α1-α2 loop in this process by three mutagenic approaches: replacing loop segments with cognate loop regions from closely related proteins, alanine scanning and analysis of BAX α1-α2 loop missense mutations observed in tumours. Responsiveness to a death signal, such as tBID, was reduced by mutations in the N-terminal but not C-terminal half of the loop. N-terminal loop variants, which were enriched in tumours, impaired MOM integration by allosterically reducing exposure of the BAX α9 transmembrane anchor. Most C-terminal loop variants reduced BAX stability, leading to increased BAX apoptotic function in some variants. Thus, our systematic mutagenesis suggests that the two halves of the α1-α2 loop have distinct functions. We show that the N-terminal half of the loop (its first nine residues) comprises an important allosteric regulator of BAX activation by setting the proportion of MOM-integrated BAX following a death signal. The enrichment of N-terminal loop mutations in tumours indicates that they may promote tumour cell survival and underscore the loop as a target for therapeutic manipulation of BAX function." @default.
• W3171559655 created "2021-06-22" @default.
• W3171559655 creator A5083239994 @default.
• W3171559655 creator A5084729140 @default.
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• W3171559655 date "2021-06-16" @default.
• W3171559655 modified "2023-10-06" @default.
• W3171559655 title "BAX mitochondrial integration is regulated allosterically by its α1−α2 loop" @default.
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• W3171559655 doi "https://doi.org/10.1038/s41418-021-00815-x" @default.
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• W3171559655 hasPublicationYear "2021" @default.
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