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MBC in Press, published online ahead of print July 11, 2003
Mol. Biol. Cell 10.1091/mbc.E03-02-0092

A more recent version of this article appeared on October 1, 2003
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Submitted on February 19, 2003
Revised on May 20, 2003
Accepted on June 3, 2003

The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria

Kara L. Cerveny1 and Robert E. Jensen1*

1 Department of Cell Biology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, Maryland 21205

* Corresponding author. E-mail address: rjensen{at}jhmi.edu.

The Net2, Fis1, and Dnm1 proteins are required for the division of mitochondria in the yeast S. cerevisiae. Net2p has an amino-terminal region that contains predicted coiled-coil motifs and a carboxyl-terminal domain composed of WD-40 repeats. We found that the amino-terminal part of Net2p interacts with Fis1p, while the carboxyl-terminal region interacts with both Dnm1p and Fis1p. Overproduction of either domain of Net2p in yeast cells poisons mitochondrial fission, and the dominant-negative effect caused by the WD-repeats of Net2p is suppressed by increased levels of Dnm1p. Point mutations in the WD-region of Net2p or in the GTPase region of Dnm1p disrupt the normal Net2p-Dnm1p interaction, causing Net2p to lose its normal punctate distribution. Our results suggest that Dnm1p interacts with the WD-repeats of Net2p, and in a GTP-dependent manner recruits Net2p to sites of mitochondrial division. Furthermore, our results indicate that Net2p is required for proper assembly of the mitochondrial fission components to regulate organelle division.




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