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Inhibition of BAK-mediated apoptosis by the BH3-only protein BNIP5
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Inhibition of BAK-mediated apoptosis by the BH3-only protein BNIP5
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Inhibition of BAK-mediated apoptosis by the BH3-only protein BNIP5
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Journal Article
Inhibition of BAK-mediated apoptosis by the BH3-only protein BNIP5
2025
Overview
BCL-2 family proteins regulate apoptosis by initiating mitochondrial outer membrane permeabilization (MOMP). Activation of the MOMP effectors BAX and BAK is controlled by the interplay of anti-apoptotic BCL-2 proteins (e.g., MCL-1) and pro-apoptotic BH3-only proteins (e.g., BIM). Using a genome-wide CRISPR-dCas9 transactivation screen we identified BNIP5 as an inhibitor of BAK-, but not BAX-induced apoptosis. BNIP5 blocked BAK activation in different cell types and in response to various cytotoxic therapies. The BH3 domain of BNIP5 was both necessary and sufficient to block BAK activation. Mechanistically, the BH3 domain of BNIP5 acts as a selective BAK activator, but a poor de-repressor of complexes between BAK and pro-survival BCL-2 family proteins. By promoting the binding of activated BAK to MCL-1 or BCL-xL, BNIP5 inhibits apoptosis when BAX is absent. Based on our observations, BNIP5 can act functionally as an anti-apoptotic BH3-only protein.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 14/19
/ 82/1
/ 96/31
/ 96/35
/ 96/63
/ Animals
/ bcl-2 Homologous Antagonist-Killer Protein - antagonists & inhibitors
/ bcl-2 Homologous Antagonist-Killer Protein - metabolism
/ bcl-2-Associated X Protein - metabolism
/ Biomedical and Life Sciences
/ CRISPR
/ Humans
/ Major outer membrane protein
/ Myeloid Cell Leukemia Sequence 1 Protein - metabolism
/ Proteins
