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(Received for publication, April 24, 1996, and in revised form, June 10, 1996)
From the Department of Cell Biology, The Scripps Research
Institute, La Jolla, California 92037
GTP hydrolysis by dynamin is required to drive
coated vesicle budding at the plasma membrane. A diverse set of
molecules including microtubules, grb2, and acidic phospholipids
stimulate dynamin GTPase activity in vitro, although the
physiological relevance of these effectors remains to be determined.
Dynamin has been shown to assemble around microtubules, the most potent
stimulatory molecule, into structures indistinguishable by electron
microscopy from collars captured in vivo at the necks of
endocytic coated pits. Under low ionic strength conditions purified
dynamin self-assembles into rings and helical stacks of rings. Here we
show that dynamin self-assembly stimulates its GTPase activity as much
as 10-fold. Thus, we identify dynamin, itself, as the first effector of
dynamin GTPase activity known to be physiologically relevant. Assembled
dynamin's stimulated GTPase activity is not dependent on the direct
interaction of high affinity GTP binding sites since a mutant defective
in GTP binding and hydrolysis can coassemble with and stimulate GTP
hydrolysis by wild-type dynamin. Finally, we find that GTP destabilizes
assembled dynamin structures, suggesting that the activated rates of
GTP hydrolysis reflect a continuing cycle of assembly, GTP hydrolysis,
and disassembly.
Volume 271, Number 37,
Issue of September 13, 1996
pp. 22310-22314
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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