A nonproteolytic proteasome activity controls organelle fission in yeast

Autor: Michela Esposito, Rémy Saunier, Raynald Cossard, Agnès Delahodde, Line Hofmann, Teresa Rinaldi
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