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Vol. 10, Issue 12, 4403-4417, December 1999
Department of Biochemistry and Molecular Biology and Center for
Basic Research in Digestive Diseases, Mayo Clinic, Rochester, Minnesota
55905
The dynamin family of large GTPases has been implicated in vesicle
formation from both the plasma membrane and various intracellular membrane compartments. The dynamin-like protein DLP1, recently identified in mammalian tissues, has been shown to be more closely related to the yeast dynamin proteins Vps1p and Dnm1p (42%) than to
the mammalian dynamins (37%). Furthermore, DLP1 has been shown to
associate with punctate vesicles that are in intimate contact with
microtubules and the endoplasmic reticulum (ER) in mammalian cells. To define the function of DLP1, we have transiently
expressed both wild-type and two mutant DLP1 proteins, tagged with
green fluorescent protein, in cultured mammalian cells. Point mutations in the GTP-binding domain of DLP1 (K38A and D231N) dramatically changed
its intracellular distribution from punctate vesicular structures to
either an aggregated or a diffuse pattern. Strikingly, cells expressing
DLP1 mutants or microinjected with DLP1 antibodies showed a marked
reduction in ER fluorescence and a significant aggregation and
tubulation of mitochondria by immunofluorescence microscopy. Consistent
with these observations, electron microscopy of DLP1 mutant cells
revealed a striking and quantitative change in the distribution and
morphology of mitochondria and the ER. These data support very recent
studies by other authors implicating DLP1 in the maintenance of
mitochondrial morphology in both yeast and mammalian cells.
Furthermore, this study provides the first evidence that a dynamin
family member participates in the maintenance and distribution of the
ER. How DLP1 might participate in the biogenesis of two presumably
distinct organelle systems is discussed.
Corresponding author. E-mail address:
mcniven.mark{at}mayo.edu.
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