BAT3 modulates p300-dependent acetylation of p53 and autophagy-related protein 7 (ATG7) during autophagy
| Autor: | Laetitia K. Linares, Andrew V. Hubberstey, Emmanuelle Liaudet-Coopman, Nelly Pirot, Fabienne Desmots, Guy Berchem, Anne-Sophie Bach, Esther Pérez-Gracia, Christine Prébois, Valérie Palissot, Patrice Codogno, Céline Gongora, Salwa Sebti, Sophie Pattingre, Chantal Bauvy |
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| Přispěvatelé: | Institut de recherche en cancérologie de Montpellier ( IRCM - U896 Inserm - UM1 ), Université Montpellier 1 ( UM1 ) -CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université de Montpellier ( UM ), Institut Necker Enfants-Malades (INEM) ( INEM - UM 111 (UMR 8253 / U1151) ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Service d'Hématologie, Immunologie et de Thérapie Cellulaire ( HITC ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -Hôpital Pontchaillou-CHU Pontchaillou [Rennes], Department of Biological Sciences [Windsor], University of Windsor [Ca], Laboratory of Experimental Hemato-Oncology ( CRP-Santé ), Centre de Recherche Public-Santé, This work is supported by INSERM, ARC (SP), La Ligue Régionale contre Le Cancer (Comités du Gard et de l'Hérault) (SP), Cancéropole GSO (SP) and CHEMORES consortium (EU FP6, ELC). SS has fellowships from the FNR Luxembourg and La Ligue Nationale contre le Cancer., Institut de recherche en cancérologie de Montpellier (IRCM - U896 Inserm - UM1), CRLCC Val d'Aurelle - Paul Lamarque-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 1 (UM1), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Service d'Hématologie, Immunologie et de Thérapie Cellulaire (HITC), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Hôpital Pontchaillou-CHU Pontchaillou [Rennes], Laboratory of Experimental Hemato-Oncology (CRP-Santé), Le Ster, Yves, Université Montpellier 1 (UM1)-CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Université de Rennes (UR)-Hôpital Pontchaillou-CHU Pontchaillou [Rennes] |
| Rok vydání: | 2014 |
| Předmět: |
p53
Autophagy-Related Protein 7 MESH: Mice Knockout Mice Cytosol MESH: Cytosol MESH : Embryo Mammalian MESH: Animals Nuclear protein MESH: Tumor Suppressor Protein p53 Mice Knockout MESH : Cell Nucleus Multidisciplinary MESH: Real-Time Polymerase Chain Reaction MESH : Cytosol Life Sciences Nuclear Proteins Biological Sciences Cell biology medicine.anatomical_structure MESH : Cell Fractionation MESH: Cell Fractionation MESH : DNA Primers MESH: Molecular Chaperones Microtubule-Associated Proteins MESH: Acetylation MESH: Cell Nucleus MESH: DNA Primers MESH : Real-Time Polymerase Chain Reaction [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology Cell Fractionation Real-Time Polymerase Chain Reaction MESH : Acetylation BAG3 MESH : E1A-Associated p300 Protein MESH : Immunoprecipitation BAT3 MESH : Mice [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology Autophagy medicine Animals Immunoprecipitation MESH: Autophagy [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology [SDV.BC] Life Sciences [q-bio]/Cellular Biology MESH: Mice [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology DNA Primers acetylation Cell Nucleus MESH: Immunoprecipitation [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology MESH: Embryo Mammalian MESH : Molecular Chaperones MESH : Nuclear Proteins Embryo Mammalian MESH : Autophagy Molecular biology ATG MESH: Microtubule-Associated Proteins MESH : Tumor Suppressor Protein p53 Cell nucleus MESH : Microtubule-Associated Proteins Acetylation MESH : Mice Knockout MESH: E1A-Associated p300 Protein MESH : Animals Tumor Suppressor Protein p53 E1A-Associated p300 Protein MESH: Nuclear Proteins Nuclear localization sequence Molecular Chaperones |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2014, 111 (11), pp.4115-20. 〈10.1073/pnas.1313618111〉 Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2014, 111 (11), pp.4115-20. ⟨10.1073/pnas.1313618111⟩ Proceedings of the National Academy of Sciences of the United States of America, 2014, 111 (11), pp.4115-20. ⟨10.1073/pnas.1313618111⟩ Biological Sciences Publications |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.1313618111 |
| Popis: | International audience; Autophagy is regulated by posttranslational modifications, including acetylation. Here we show that HLA-B-associated transcript 3 (BAT3) is essential for basal and starvation-induced autophagy in embryonic day 18.5 BAT3(-/-) mouse embryos and in mouse embryonic fibroblasts (MEFs) through the modulation of p300-dependent acetylation of p53 and ATG7. Specifically, BAT3 increases p53 acetylation and proautophagic p53 target gene expression, while limiting p300-dependent acetylation of ATG7, a mechanism known to inhibit autophagy. In the absence of BAT3 or when BAT3 is located exclusively in the cytosol, autophagy is abrogated, ATG7 is hyperacetylated, p53 acetylation is abolished, and p300 accumulates in the cytosol, indicating that BAT3 regulates the nuclear localization of p300. In addition, the interaction between BAT3 and p300 is stronger in the cytosol than in the nucleus and, during starvation, the level of p300 decreases in the cytosol but increases in the nucleus only in the presence of BAT3. We conclude that BAT3 tightly controls autophagy by modulating p300 intracellular localization, affecting the accessibility of p300 to its substrates, p53 and ATG7. |
| Databáze: | OpenAIRE |
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