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Vol. 9, Issue 11, 3227-3239, November 1998
Department of Biological Chemistry, University of California Los
Angeles School of Medicine, Los Angeles, California 90095
Caenorhabditis elegans dynamin is
expressed at high levels in neurons and at lower levels in other cell
types, consistent with the important role that dynamin plays in the
recycling of synaptic vesicles. Indirect immunofluorescence showed that
dynamin is concentrated along the dorsal and ventral nerve cords and in the synapse-rich nerve ring. Green fluorescent protein (GFP) fused to
the N terminus of dynamin is localized to synapse-rich regions. Furthermore, this chimera was detected along the apical membrane of
intestinal cells, in spermathecae, and in coelomocytes. Dynamin localization was not affected by disrupting axonal transport of synaptic vesicles in the unc-104 (kinesin) mutant. To
investigate the alternative mechanisms that dynamin might use for
translocation to the synapse, we systematically tested the localization
of different protein domains by fusion to GFP. Localization of each
chimera was measured in one specific neuron, the ALM. The
GTPase, a middle domain, and the putative coiled coil each contribute
to synaptic localization. Surprisingly, the pleckstrin homology domain
and the proline-rich domain, which are known to bind to coated-pit constituents, did not contribute to synaptic localization. The GFP-GTPase chimera was most strongly localized, although the GTPase domain has no known interactions with proteins other than with dynamin
itself. Our results suggest that different dynamin domains contribute
to axonal transport and the sequestration of a pool of dynamin
molecules in synaptic cytosol.
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