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. 2016 Jan;590(1):13-21.
doi: 10.1002/1873-3468.12030. Epub 2015 Dec 30.

Regulation of Bax/mitochondria interaction by AKT

Lilit Simonyan  1 , Thibaud T Renault  1 , Maria João da Costa Novais  1   2 , Maria João Sousa  2 , Manuela Côrte-Real  2 , Nadine Camougrand  1 , Cécile Gonzalez  1 , Stéphen Manon  1
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Free article

Regulation of Bax/mitochondria interaction by AKT

Lilit Simonyan et al. FEBS Lett. 2016 Jan.
Free article

Abstract

Bax-dependent mitochondrial permeabilization during apoptosis is controlled by multiple factors, including the phosphorylation by the protein kinase AKT. We used the heterologous co-expression of human Bax and AKT1 in yeast to investigate how the kinase modulates the different steps underlying Bax activation. We found that AKT activated Bax and increased its cellular content. Both effects were dependent on Ser184, but a phosphorylation of this residue did not fully explain the effects of AKT. Additional experiments with mutants substituted on Ser184 suggested that the regulation of Bax dynamic equilibrium between the cytosol and mitochondria might be more tightly regulated by Bcl-xL when Bax is phosphorylated.

Keywords: AKT; Bcl-2 family; apoptosis; mitochondria; yeast model.

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