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Vol. 10, Issue 2, 501-513, February 1999
Department of Biochemistry and Biophysics and the Hormone Research
Institute, University of California, San Francisco, California
94143-0534
The GTPase dynamin has been clearly implicated in clathrin-mediated
endocytosis of synaptic vesicle membranes at the presynaptic nerve
terminal. Here we describe a novel 52-kDa protein in rat brain that
binds the proline-rich C terminus of dynamin. Syndapin I (synaptic,
dynamin-associated protein I) is highly enriched in brain where it
exists in a high molecular weight complex. Syndapin I can be involved
in multiple protein-protein interactions via a src homology 3 (SH3)
domain at the C terminus and two predicted coiled-coil stretches.
Coprecipitation studies and blot overlay analyses revealed that
syndapin I binds the brain-specific proteins dynamin I, synaptojanin,
and synapsin I via an SH3 domain-specific interaction.
Coimmunoprecipitation of dynamin I with antibodies recognizing syndapin
I and colocalization of syndapin I with dynamin I at vesicular
structures in primary neurons indicate that syndapin I associates with
dynamin I in vivo and may play a role in synaptic vesicle endocytosis.
Furthermore, syndapin I associates with the neural Wiskott-Aldrich
syndrome protein, an actin-depolymerizing protein that regulates
cytoskeletal rearrangement. These characteristics of syndapin I suggest
a molecular link between cytoskeletal dynamics and synaptic vesicle
recycling in the nerve terminal.
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