Papers In Press, published online ahead of print October 2, 2001
J. Biol. Chem, 10.1074/jbc.M104927200
Submitted on May 30, 2001
Revised on September 11, 2001
Accepted on October 2, 2001
Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton
Patricia M. Okamoto, Chantal Gamby, David Wells, Justin Fallon, and Richard B. Vallee
Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01605
Corresponding Author: richard.vallee{at}umassmed.edu
SUMMARY Dynamin is a GTPase involved in endocytosis and other aspects of membrane trafficking. A critical function in the presynaptic compartment attributed to the brain-specific dynamin isoform, dynamin-1, is in synaptic vesicle recycling. We report that dynamin-2 specifically interacts with members of the Shank/ProSAP family of postsynaptic density (PSD)1 scaffolding proteins, and present evidence that dynamin-2 is specifically associated with the PSD. These data are consistent with a role for this otherwise broadly distributed form of dynamin in glutamate receptor down-regulation and other aspects of postsynaptic membrane turnover.
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