Dynamin Isoform-specific Interaction with the Shank/ProSAP Scaffolding Proteins of the Postsynaptic Density and Actin Cytoskeleton

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...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-12, Vol.276 (51), p.48458-48465
Main Authors: Okamoto, Patricia M., Gamby, Chantal, Wells, David, Fallon, Justin, Vallee, Richard B.
Format: Article
Language:English
Subjects:
Actins - metabolism
Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Animals
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Cloning, Molecular
COS Cells
Dynamin I
Dynamins
GTP Phosphohydrolases - metabolism
Nerve Tissue Proteins - chemistry
Nerve Tissue Proteins - metabolism
Precipitin Tests
Protein Binding
Protein Isoforms - metabolism
Synapses - metabolism
Two-Hybrid System Techniques
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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 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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M104927200