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First published online 22 September 2009
doi: 10.1242/jcs.050229

Journal of Cell Science 122, 3673-3683 (2009)
Published by The Company of Biologists 2009
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Research Article

A nonproteolytic proteasome activity controls organelle fission in yeast

Line Hofmann1, Rémy Saunier1, Raynald Cossard1, Michela Esposito2, Teresa Rinaldi2 and Agnès Delahodde1,*

1 University of Paris-Sud, CNRS, UMR 8621, Institute of Genetics and Microbiology, Orsay, 91405, France
2 Pasteur Institute-Cenci Bolognetti Foundation, Department of Cell and Developmental Biology, University of Rome I, 00185 Rome, Italy

* Author for correspondence (agnes.delahodde{at}igmors.u-psud.fr)

Accepted 3 August 2009

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.

Key words: Mitochondria, Peroxisomes, Fission, Proteasome


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Keeping a lid on organelle fission

JCS 2009 122: 2002. [Full Text]  





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