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      BAG6/BAT3 modulates autophagy by affecting EP300/p300 intracellular localization.

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          Abstract

          We recently reported that BAG6/BAT3 (BCL2-associated athanogene 6) is essential for basal and starvation-induced autophagy in E18.5 bag6(-/-) mouse embryos and in mouse embryonic fibroblasts (MEFs) through the modulation of the EP300/p300-dependent acetylation of TRP53 and autophagy-related (ATG) proteins. We observed that BAG6 increases TRP53 acetylation during starvation and pro-autophagic TRP53-target gene expression. BAG6 also decreases the EP300 dependent-acetylation of ATG5, ATG7, and LC3-I, posttranslational modifications that inhibit autophagy. In addition, in the absence of BAG6 or when using a mutant of BAG6 exclusively located in the cytoplasm, autophagy is inhibited, ATG7 is hyperacetylated, TRP53 acetylation is abrogated, and EP300 accumulates in the cytoplasm indicating that BAG6 is involved in the regulation of the nuclear localization of EP300. We also reported that the interaction between BAG6 and EP300 occurs in the cytoplasm rather than the nucleus. Moreover, during starvation, EP300 is transported to the nucleus in a BAG6-dependent manner. We concluded that BAG6 regulates autophagy by controlling the localization of EP300 and its accessibility to nuclear (TRP53) and cytoplasmic (ATGs) substrates.

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          Author and article information

          Journal
          Autophagy
          Autophagy
          Informa UK Limited
          1554-8635
          1554-8627
          Jul 2014
          : 10
          : 7
          Affiliations
          [1 ] Institut de Recherche en Cancérologie de Montpellier; Montpellier, France; Institut National de la Santé et de la Recherche Médicale U896; Montpellier, France; Université Montpellier 1; Montpellier, France; Institut Régional du Cancer Montpellier; Montpellier, France.
          [2 ] Institut Necker Enfants-Malades; Paris, France; Institut National de la Santé et de la Recherche Médicale (INSERM) U1151; Paris, France; CNRS UMR 8243; Paris, France; Université Paris Descartes-Sorbonne Paris Cité; Paris, France.
          [3 ] Service d'Hématologie; Immunologie et Thérapie Cellulaire; CHU de Rennes; Hôpital Pontchaillou; Rennes, France.
          [4 ] Department of Biological Sciences; University of Windsor; Windsor, Ontario CA.
          [5 ] Laboratory of Experimental Hemato-Oncology; Centre de Recherche Public-Santé; Luxembourg, Luxembourg.
          Article
          28979
          10.4161/auto.28979
          4203559
          24852146

          p53, autophagy, acetylation, BAT3, ATG, nucleocytoplasmic shuttling

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