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Originally published In Press as doi:10.1074/jbc.M104927200 on October 2, 2001

J. Biol. Chem., Vol. 276, Issue 51, 48458-48465, December 21, 2001
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Dynamin Isoform-specific Interaction with the Shank/ProSAP Scaffolding Proteins of the Postsynaptic Density and Actin Cytoskeleton*

Patricia M. OkamotoDagger , Chantal GambyDagger , David Wells§, Justin Fallon§, and Richard B. ValleeDagger ||

From the Dagger  Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605 and the § Department of Neuroscience, Brown University, Providence, Rhode Island 02912

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 scaffolding proteins and present evidence that dynamin-2 is specifically associated with the postsynaptic density. 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.

* This work was supported by National Institutes of Health Grant GM26701 (to R. B. V.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Dept. of Molecular, Cellular, and Developmental Biology, Yale University, 219 Prospect Ave., New Haven, CT 06520.

|| To whom correspondence should be addressed: Dept. of Cell Biology, University of Massachusetts Medical School, 377 Plantation St., Worcester, MA 01605. Tel.: 508-856-8504; Fax: 508-856-8987; E-mail: Richard.Vallee@umassmed.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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