A nonproteolytic proteasome activity controls organelle fission in yeast
Autor: | Michela Esposito, Rémy Saunier, Raynald Cossard, Agnès Delahodde, Line Hofmann, Teresa Rinaldi |
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Přispěvatelé: | Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS) |
Jazyk: | angličtina |
Rok vydání: | 2009 |
Předmět: |
Fission
MESH: Catalytic Domain MESH: Cell Cycle MESH: Amino Acid Sequence Mitochondrion MESH: Saccharomyces cerevisiae Proteins Membrane fission Catalytic Domain fission mitochondria peroxisomes proteasome 0303 health sciences Protein Stability MESH: Proteasome Endopeptidase Complex 030302 biochemistry & molecular biology Cell Cycle Temperature Organelle fission Peroxisome MESH: Saccharomyces cerevisiae MESH: Temperature Cell biology MESH: Glucose Protein Transport [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Biochemistry MESH: Cell Division Mitochondrial fission Cell Division Proteasome Endopeptidase Complex MESH: Protein Transport Saccharomyces cerevisiae Proteins MESH: Mutation MESH: Mitochondria Molecular Sequence Data Vacuole fusion Saccharomyces cerevisiae Biology 03 medical and health sciences MESH: Protein Stability Organelle [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence 030304 developmental biology Organelles MESH: Molecular Sequence Data MESH: Oleic Acid Cell Biology MESH: Peroxisomes Glucose MESH: Protein Processing Post-Translational Mutation Protein Processing Post-Translational Oleic Acid MESH: Organelles |
Zdroj: | Journal of Cell Science Journal of Cell Science, Company of Biologists, 2009, 122 (Pt 20), pp.3673-83. ⟨10.1242/jcs.050229⟩ |
ISSN: | 0021-9533 1477-9137 |
DOI: | 10.1242/jcs.050229⟩ |
Popis: | International audience; To understand the processes underlying organelle function, dynamics and inheritance, it is necessary to identify and characterize the regulatory components involved. Recently in yeast and mammals, proteins of the membrane fission machinery (Dnm1-Mdv1-Caf4-Fis1 in yeast and DLP1-FIS1 in human) have been shown to have a dual localization on mitochondria and peroxisomes, where they control mitochondrial fission and peroxisome division. Here, we show that whereas vacuole fusion is regulated by the proteasome degradation function, mitochondrial fission and peroxisomal division are not controlled by the proteasome activity but rather depend on a new function of the proteasomal lid subunit Rpn11. Rpn11 was found to regulate the Fis1-dependent fission machinery of both organelles. These findings indicate a unique role of the Rpn11 protein in mitochondrial fission and peroxisomal proliferation that is independent of its role in proteasome-associated deubiquitylation. |
Databáze: | OpenAIRE |
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