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Vol. 12, Issue 2, 309-321, February 2001
and
*Department of Cell Biology and Anatomy, Johns Hopkins University
School of Medicine, Baltimore, Maryland 21205; and
Mitochondria are dynamic organelles that undergo frequent division
and fusion, but the molecular mechanisms of these two events are not
well understood. Dnm1p, a mitochondria-associated, dynamin-related GTPase was previously shown to mediate mitochondrial fission. Recently,
a genome-wide yeast two-hybrid screen identified an uncharacterized
protein that interacts with Dnm1p. Cells disrupted in this new gene,
which we call NET2, contain a single mitochondrion that
consists of a network formed by interconnected tubules, similar to the
phenotype of dnm1Integrated Imaging Center, Department of Biology, The
Johns Hopkins University, Baltimore, Maryland 21218
cells. NET2 encodes
a mitochondria-associated protein with a predicted coiled-coil region
and six WD-40 repeats. Immunofluorescence microscopy indicates that
Net2p is located in distinct, dot-like structures along the
mitochondrial surface, many of which colocalize with the Dnm1 protein.
Fluorescence and immunoelectron microscopy shows that Dnm1p and Net2p
preferentially colocalize at constriction sites along mitochondrial
tubules. Our results suggest that Net2p is a new component of the
mitochondrial division machinery.
Corresponding author. E-mail address:
rjensen{at}jhmi.edu.
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