|
|
|
|
|
|
|
||
J. Cell Biol.,
Volume 143, Number 2, October 19, 1998 333-349
Department of Biology, University of Utah, Salt Lake City, Utah 84112
The Saccharomyces cerevisiae Dnm1 protein
is structurally related to dynamin, a GTPase required
for membrane scission during endocytosis. Here we
show that Dnm1p is essential for the maintenance of
mitochondrial morphology. Disruption of the DNM1
gene causes the wild-type network of tubular mitochondrial membranes to collapse to one side of the cell but
does not affect the morphology or distribution of other
cytoplasmic organelles. Dnm1 proteins containing point mutations in the predicted GTP-binding domain
or completely lacking the GTP-binding domain fail to
rescue mitochondrial morphology defects in a dnm1
mutant and induce dominant mitochondrial morphology defects in wild-type cells. Indirect immunofluorescence reveals that Dnm1p is distributed in punctate
structures at the cell cortex that colocalize with the mitochondrial compartment. These Dnm1p-containing structures remain associated with the spherical mitochondria found in an mdm10 mutant strain. In addition,
a portion of Dnm1p cofractionates with mitochondrial
membranes during differential sedimentation and sucrose gradient fractionation of wild-type cells. Our results demonstrate that Dnm1p is required for the cortical distribution of the mitochondrial network in yeast, a
novel function for a dynamin-related protein.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
