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Volume 271, Number 44, Issue of November 1, 1996 pp. 27770-27775
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Isoform-specific, Calcium-regulated Interaction of the Synaptic Vesicle Proteins SV2 and Synaptotagmin

(Received for publication, July 1, 1996, and in revised form, August 16, 1996)

Amanda E. Schivell Dagger , Robert H. Batchelor § and Sandra M. Bajjalieh §

From the Dagger  Graduate Program in Neurobiology and Behavior and § Department of Pharmacology, University of Washington School of Medicine, Seattle, Washington 98195

The identification and functional characterization of proteins localized to synaptic vesicles has contributed significantly to our understanding of neurotransmission. Studies of synaptic vesicle protein interactions have both led to the identification of novel synaptic proteins and suggested hypotheses of protein function. Synaptic vesicle protein 2 (SV2), is an integral membrane glycoprotein present in all synaptic vesicles. There are two characterized isoforms, SV2A and SV2B. Despite their homology to transporter proteins, the function of the SV2s remains unknown. In an effort to determine SV2 function and identify cofactors required for SV2 activity, we examined the protein interactions of SV2 using a combination of cross-linking, immunoprecipitation, and recombinant protein affinity chromatography. We report that SV2 is part of a large protein complex that contains the synaptic vesicle protein synaptotagmin. The interaction between SV2 and synaptotagmin is direct, specific to SV2A, and inhibited by calcium with an EC50 of approximately 10 µM. Interaction is mediated by the cytoplasmic amino terminus of SV2A and the C2B domain of synaptotagmin. Our observations suggest a regulatory relationship between these two proteins.


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