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Vol. 273, Issue 3, 1425-1429, January 16, 1998

Synapsins I and II Are ATP-binding Proteins with Differential Ca2+ Regulation

Masahiro Hosaka and Thomas C. Südhof

From the Howard Hughes Medical Institute and Department of Molecular Genetics, University of Texas Southwestern Medical School, Dallas, Texas 75235

Synapsins I and II are abundant phosphoproteins that are localized to synaptic vesicles and have essential functions in regulating synaptic vesicle exocytosis. Synapsins contain a single evolutionarily conserved, large central domain, the C-domain, that accounts for the majority of their sequences. Unexpectedly, the crystal structure of the C-domain from synapsin I revealed that it is structurally closely related to several ATPases despite the absence of sequence similarities (Esser, L., Wang, C.-R., Hosaka, M., Smagula, C. S., Südhof, T. C., and Deisenhofer, J. (1998) EMBO J., in press). We now show that the C-domains of both synapsin I and synapsin II constitute high affinity ATP-binding modules. The two C-domains exhibit similar ATP affinities but are differentially regulated; ATP binding to synapsin I is Ca2+-dependent whereas ATP binding to synapsin II is Ca2+-independent. In synapsin I, the Ca2+ requirement for ATP binding is mediated by a single, evolutionarily conserved glutamate residue (Glu373) at a position where synapsin II contains a lysine residue. Exchange of Glu373 for lysine converts synapsin I from a Ca2+-dependent protein into a Ca2+-independent ATP-binding protein. Our studies suggest that synapsins I and II function on synaptic vesicles as ATP-binding proteins that are differentially regulated by Ca2+.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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