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Vol. 14, Issue 10, 4126-4139, October 2003
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* Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
Submitted February 19, 2003;
Revised May 20, 2003;
Accepted June 3, 2003
Monitoring Editor: Douglas Koshland
The Net2, Fis1, and Dnm1 proteins are required for the division of mitochondria in the yeast Saccharomyces 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, whereas 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.
Abbreviations used: GFP, green fluorescent protein; RFP and DsRed, red fluorescent protein; DIC, differential interference contrast; Sraf, synthetic medium with raffinose.
Online version of this article contains video and supplementary materials for some figures. Online version is available at www.molbiolcell.org.
Corresponding author. E-mail address: rjensen{at}jhmi.edu.
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