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Vol. 8, Issue 12, 2553-2562, December 1997
Department of Cell Biology, The Scripps Research Institute, La
Jolla, California 92037
To begin to understand mechanistic differences in endocytosis in
neurons and nonneuronal cells, we have compared the biochemical properties of the ubiquitously expressed dynamin-II isoform with those
of neuron-specific dynamin-I. Like dynamin-I, dynamin-II is
specifically localized to and highly concentrated in coated pits on the
plasma membrane and can assemble in vitro into rings and helical
arrays. As expected, the two closely related isoforms share a similar
mechanism for GTP hydrolysis: both are stimulated in vitro by
self-assembly and by interaction with microtubules or the SH3
domain-containing protein, grb2. Deletion of the C-terminal proline/arginine-rich domain from either isoform abrogates
self-assembly and assembly-dependent increases in GTP hydrolysis.
However, dynamin-II exhibits a ~threefold higher rate of intrinsic
GTP hydrolysis and higher affinity for GTP than dynamin-I. Strikingly,
the stimulated GTPase activity of dynamin-II can be >40-fold higher
than dynamin-I, due principally to its greater propensity for
self-assembly and the increased resistance of assembled dynamin-II to
GTP-triggered disassembly. These results are consistent with the
hypothesis that self-assembly is a major regulator of dynamin GTPase
activity and that the intrinsic rate of GTP hydrolysis reflects a
dynamic, GTP-dependent equilibrium of assembly and disassembly.
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