Dynamin isoform-specific interaction with the shan...[J Biol Chem. 2001]

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1: J Biol Chem. 2001 Dec 21;276(51):48458-65. Epub 2001 Oct 2. Links

Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton.

Okamoto PM, Gamby C, Wells D, Fallon J, Vallee RB.

Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.

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.

PMID: 11583995 [PubMed - indexed for MEDLINE]

Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. [J Cell Biol. 2000]
Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. [Mol Biol Cell. 1999]
ProSAP/Shank postsynaptic density proteins interact with insulin receptor tyrosine kinase substrate IRSp53. [J Neurochem. 2002]
ReviewScaffolding proteins at the postsynaptic density: shank as the architectural framework. [Handb Exp Pharmacol. 2008]
ReviewProSAP/Shank proteins - a family of higher order organizing molecules of the postsynaptic density with an emerging role in human neurological disease. [J Neurochem. 2002]

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Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton.

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