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Originally published In Press as doi:10.1074/jbc.M205618200 on August 19, 2002

J. Biol. Chem., Vol. 277, Issue 43, 40832-40838, October 25, 2002
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Formation of Complexes between Ca2+·Calmodulin and the Synapse-associated Protein SAP97 Requires the SH3 Domain-Guanylate Kinase Domain-connecting HOOK Region*

Ingo PaarmannDagger , Oliver SpangenbergDagger , Arnon Lavie§, and Manfred KonradDagger

From the Dagger  Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, Göttingen D-37070, Germany and the § Department of Biochemistry and Molecular Biology, University of Illinois at Chicago, Chicago, Illinois 60607

Mammalian synapse-associated protein SAP97, a structural and functional homolog of Drosophila Dlg, is a membrane-associated guanylate kinase (MAGUK) that is present at pre- and postsynaptic sites as well as in epithelial cell-cell contact sites. It is a multidomain scaffolding protein that shares with other members of the MAGUK protein family a characteristic modular organization composed of three sequential protein interaction motifs known as PDZ domains, followed by an Src homology 3 (SH3) domain, and an enzymatically inactive guanylate kinase (GK)-like domain. Specific binding partners are known for each domain, and different modes of intramolecular interactions have been proposed that particularly involve the SH3 and GK domains and the so-called HOOK region located between these two domains. We identified the HOOK region as a specific site for calmodulin binding and studied the dynamics of complex formation of recombinant calmodulin and SAP97 by surface plasmon resonance spectroscopy. Binding of various SAP97 deletion constructs to immobilized calmodulin was strictly calcium-dependent. From the rate constants of association and dissociation we determined an equilibrium dissociation constant Kd of 122 nM for the association of calcium-saturated calmodulin and a SAP97 fragment, which encompassed the entire SH3-HOOK-GK module. Comparative structure-based sequence analysis of calmodulin binding regions from various target proteins predicts variable affinities for the interaction of calmodulin with members of the MAGUK protein family. Our findings suggest that calmodulin could regulate the intramolecular interaction between the SH3, HOOK, and GK domains of SAP97.

* This work was supported by Research Grant RG 0120/1999-B of the Human Frontier Science Program (to I. P., A. L., and M. K.), by the Deutsche Forschungsgemeinschaft, and by the Max Planck Society (to O. S. and M. K.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 49-551-201-1706; Fax: 49-551-201-1718; E-mail: mkonrad@gwdg.de.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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