Title

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

UMMS Affiliation

Department of Cell Biology

Date

10-5-2001

Document Type

Article

Subjects

Actins; *Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Animals; COS Cells; Carrier Proteins; Cloning, Molecular; Dynamin I; Dynamins; GTP Phosphohydrolases; Nerve Tissue Proteins; Precipitin Tests; Protein Binding; Protein Isoforms; Synapses; Two-Hybrid System Techniques

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: J Biol Chem. 2001 Dec 21;276(51):48458-65. Epub 2001 Oct 2. Link to article on publisher's site

DOI of Published Version

10.1074/jbc.M104927200

Related Resources

Link to Article in PubMed

Journal Title

The Journal of biological chemistry

PubMed ID

11583995