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MBC in Press, published online ahead of print January 2, 2008
Mol. Biol. Cell 10.1091/mbc.E07-07-0717

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Submitted on July 28, 2007
Revised on December 6, 2007
Accepted on December 20, 2007

Dissection of the Carboxyl-Terminal Domain of the Proteasomal Subunit Rpn11 in Maintenance of Mitochondrial Structure and Function

Teresa Rinaldi,*{dagger} Line Hofmann,{dagger}{ddagger} Alessia Gambadoro,* Raynald Cossard,{ddagger} Nurit Livnat-Levanon,{sect} Michael H. Glickman,{sect} Laura Frontali,* and Agnès Delahodde{ddagger}

*Pasteur Institute-Cenci Bolognetti Foundation, Department of Cell and Developmental Biology, University of Rome La Sapienza, 00185 Rome, Italy; {ddagger}Université Paris-Sud, Centre National de la Recherche Scientifique 91405 Orsay Cedex, France; {sect}Department of Biology, Technion - Israel Institute of Technology, 32000 Haifa, Israel

Monitoring Editor: Janet Shaw

We have previously demonstrated that the C-terminal part of Rpn11, a deubiquitinating enzyme in the lid of the proteasome, is essential for maintaining a correct cell cycle and normal mitochondrial morphology and function. The two roles are apparently unlinked as the mitochondrial role is mapped to the Carboxy-terminus, whereas the catalytic deubiquitinating activity is found within the N-terminal region. The mitochondrial defects are observed in rpn11-m1 (originally termed mpr1–1), a mutation that generates Rpn11 lacking the last 31 amino acids. No mitochondrial phenotypes are recorded for mutations in the MPN+/JAMM motif. In the present study, we investigated the participation of the last 31 aminoacids of the Rpn11 protein by analysis of intragenic revertants and site specific mutants. We identified a putative {alpha}-helix necessary for the maintenance of a correct cell cycle and determined that a very short region at the C-terminus of Rpn11 is essential for the maintenance of tubular mitochondrial morphology. Furthermore, we show that expression of the C-terminal part of Rpn11 is able to complement in trans all of the rpn11-m1 mitochondrial phenotypes. Finally, we investigate the mechanisms by which Rpn11 controls the mitochondrial shape and show that Rpn11 may regulate the mitochondrial fission and tubulation processes.

{dagger}These authors contributed equally to this work.

Address correspondence to: Teresa Rinaldi (teresa.rinaldi{at}uniroma1.it)






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