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Étude des rôles et des partenaires du domaine C terminal de Rpn11, une sous-unité du protéasome 26S, dans la dynamique mitochondriale chez Saccharomyces cerevisiae

Abstract : Mitochondria are semi-autonomous organelles, which size, shape and number vary in a wide range in almost every eukaryotic cell. They are famous to be the energy producer of the cells. For this purpose, mitochondria are able to fuse and divide. These events of fusion and fission are also known as the mitochondrial dynamic. This phenomenon is highly controlled and answers to many stimuli. Lately, it has been shown that the ubiquitin proteasome system controls the fusion of mitochondria and that a proteasome subunit controls the mitochondrial fission.The ubiquitin proteasome system is a mechanism that relies on many actors: enzymes recognizing the targets of this system, a protein called ubiquitin and a complex called proteasome in charge of the degradation of the targets. Primarily known for the protein degradation, many investigations suggest that this system has other roles.Our previous studies had already shown that the proteasome subunit named Rpn11 controls the fission of mitochondria independently of the proteolytic activities of the proteasome system. The work shown in this manuscript is focused on the mechanism of action of the C-terminus domain of Rpn11 on various cellular processes, including proteasome assembly, control of mitochondrial and peroxisomal fission, yeast lifespan and also the “Proteasome Storage Granule” formation. The in vivo localisation of Rpn11 and the elucidation of its partners on the mitochondrial fission regulation were also investigated.
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Rémy Saunier. Étude des rôles et des partenaires du domaine C terminal de Rpn11, une sous-unité du protéasome 26S, dans la dynamique mitochondriale chez Saccharomyces cerevisiae. Sciences agricoles. Université Paris Sud - Paris XI, 2012. Français. ⟨NNT : 2012PA112357⟩. ⟨tel-01730295⟩

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