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Vol. 12, Issue 9, 2578-2589, September 2001
*Department of Cell Biology, The Scripps Research Institute, La
Jolla, California 92037; Abundant evidence has shown that the GTPase dynamin is required for
receptor-mediated endocytosis, but its exact role in endocytic clathrin-coated vesicle formation remains to be established. Whereas dynamin GTPase domain mutants that are defective in GTP binding and
hydrolysis are potent dominant-negative inhibitors of receptor-mediated endocytosis, overexpression of dynamin GTPase effector domain (GED)
mutants that are selectively defective in assembly-stimulated GTPase-activating protein activity can stimulate the formation of constricted coated pits and receptor-mediated endocytosis. These apparently conflicting results suggest that a complex
relationship exists between dynamin's GTPase cycle of binding and
hydrolysis and its role in endocytic coated vesicle formation. We
sought to explore this complex relationship by generating dynamin
GTPase mutants predicted to be defective at distinct stages of its
GTPase cycle and examining the structural intermediates that accumulate in cells overexpressing these mutants. We report that the effects of
nucleotide-binding domain mutants on dynamin's GTPase cycle in vitro
are not as predicted by comparison to other GTPase superfamily members.
Specifically, GTP and GDP association was destabilized for each of the
GTPase domain mutants we analyzed. Nonetheless, we find that
overexpression of dynamin mutants with subtle differences in their
GTPase properties can lead to the accumulation of distinct intermediates in endocytic coated vesicle formation.
Department of Pharmacology,
University of Texas Southwestern Medical Center, Dallas, Texas 75390;
Department of Anatomy, Yamanashi Medical University,
1110 Shimokato, Tamaho, Yamanashi 409-3898, Japan
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