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First published online March 21, 2007

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SUMO wrestling in mitochondria

Mitochondria undergo regulated fission and fusion events that are necessary for metabolic stability. One protein that helps to control these events is DRP1. This GTPase can be post-translationally modified by addition of the ubiquitin-related molecule SUMO; so might SUMOylation help to regulate mitochondrial function? On p. 1178, Heidi McBride and colleagues provide evidence that it does by showing that the SUMO protease SENP5 is needed to maintain normal mitochondrial morphology and to control intracellular levels of reactive oxygen species (ROS). Overexpression of SUMO1 increases fragmentation of mitochondria and stabilizes DRP1. The authors show that overexpression of SENP5 reduces the amount of SUMO1 conjugation and DRP1 levels and rescues SUMO1-induced mitochondrial fragmentation. By contrast, knocking down SENP5 by RNAi stabilizes DRP1, increases mitochondrial fragmentation, and increases ROS production. Finally the authors report that knocking down DRP1 rescues the effects of SENP5 downregulation. Their data represent the first report of a function for a SUMO protease in the regulation of mitochondrial dynamics and reveal a new mechanism for the regulation of mitochondrial morphology and metabolism.

Related articles in JCS:

The SUMO protease SENP5 is required to maintain mitochondrial morphology and function

Rodolfo Zunino, Astrid Schauss, Peter Rippstein, Miguel Andrade-Navarro, and Heidi M. McBride
JCS 2007 120: 1178-1188. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content