title: Regulation of Bax/mitochondria interaction by AKT.
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.
authors.affiliation: CNRS, Université de Bordeaux, UMR5095, Bordeaux, France.
authors.forename: Lilit
authors.initials: L
authors.lastname: Simonyan
authors.affiliation: CNRS, Université de Bordeaux, UMR5095, Bordeaux, France.
authors.forename: Thibaud T
authors.initials: TT
authors.lastname: Renault
authors.affiliation: CNRS, Université de Bordeaux, UMR5095, Bordeaux, France.|CBMA, Universidade do Minho, Braga, Portugal.
authors.forename: Maria João da Costa
authors.initials: MJ
authors.lastname: Novais
authors.affiliation: CBMA, Universidade do Minho, Braga, Portugal.
authors.forename: Maria João
authors.initials: MJ
authors.lastname: Sousa
authors.affiliation: CBMA, Universidade do Minho, Braga, Portugal.
authors.forename: Manuela
authors.initials: M
authors.lastname: Côrte-Real
authors.affiliation: CNRS, Université de Bordeaux, UMR5095, Bordeaux, France.
authors.forename: Nadine
authors.initials: N
authors.lastname: Camougrand
authors.affiliation: CNRS, Université de Bordeaux, UMR5095, Bordeaux, France.
authors.forename: Cécile
authors.initials: C
authors.lastname: Gonzalez
authors.affiliation: CNRS, Université de Bordeaux, UMR5095, Bordeaux, France.
authors.forename: Stéphen
authors.initials: S
authors.lastname: Manon
mesh_terms: D019943:Amino Acid Substitution; D017209:Apoptosis; D003600:Cytosol / Q000201:enzymology / Q000378:metabolism; D017353:Gene Deletion; D006238:Haploidy; D006801:Humans; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism*; D009154:Mutation; D010766:Phosphorylation; D010768:Phosphoserine / Q000031:analogs & derivatives / Q000378:metabolism; D054730:Protein Interaction Domains and Motifs; D011499:Protein Processing, Post-Translational; D055550:Protein Stability; D021381:Protein Transport; D051057:Proto-Oncogene Proteins c-akt / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D012694:Serine / Q000378:metabolism; D051028:bcl-2-Associated X Protein / Q000819:agonists / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051020:bcl-X Protein / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: C494826:BAX protein, human; C494811:BCL2L1 protein, human; D011994:Recombinant Proteins; D051028:bcl-2-Associated X Protein; D051020:bcl-X Protein; D010768:Phosphoserine; D012694:Serine; C494918:AKT1 protein, human; D051057:Proto-Oncogene Proteins c-akt
keywords: AKT; Bcl-2 family; apoptosis; mitochondria; yeast model