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Originally published In Press as doi:10.1074/jbc.M208781200 on September 25, 2002

J. Biol. Chem., Vol. 277, Issue 48, 46730-46735, November 29, 2002
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Identification of Multiple Binding Partners for the Amino-terminal Domain of Synapse-associated Protein 97*

David KarnakDagger §, Seonok LeeDagger , and Ben MargolisDagger ||**Dagger Dagger

From the Departments of Dagger  Biological Chemistry, || Internal Medicine, and the ** Howard Hughes Medical Institute, University of Michigan, Ann Arbor, Michigan 48109

Multiprotein complexes mediate static and dynamic functions to establish and maintain cell polarity in both epithelial cells and neurons. Membrane-associated guanylate kinase (MAGUK) proteins are thought to be scaffolding molecules in these processes and bind multiple proteins via their obligate postsynaptic density (PSD)-95/Disc Large/Zona Occludens-1, Src homology 3, and guanylate kinase-like domains. Subsets of MAGUK proteins have additional protein-protein interaction domains. An additional domain we identified in SAP97 called the MAGUK recruitment (MRE) domain binds the LIN-2,7 amino-terminal (L27N) domain of mLIN-2/CASK, a MAGUK known to bind mLIN-7. Here we show that SAP97 binds two other mLIN-7 binding MAGUK proteins. One of these MAGUK proteins, DLG3, coimmunoprecipitates with SAP97 in lysates from rat brain and transfected Madin-Darby canine kidney cells. This interaction requires the MRE domain of SAP97 and surprisingly, both the L27N and L27 carboxyl-terminal (L27C) domains of DLG3. We also demonstrate that SAP97 can interact with the MAGUK protein, DLG2, but not the highly related protein, PALS2. The ability of SAP97 to interact with multiple MAGUK proteins is likely to be important for the targeting of specific protein complexes in polarized cells.

* This work was supported in part by National Institute of Diabetes and Digestive and Kidney Diseases Grant 2-P50-DK39255.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.

§ Supported by a National Institutes of Health Cellular Biotechnology Training Program Grant (GM08353).

Supported by a National Institutes of Health Genetics Training Grant (5-T32-GM07544).

Dagger Dagger Investigator of the Howard Hughes Medical Institute. To whom correspondence should be addressed. Tel.: 734-764-3567; Fax: 734-763-9323; E-mail: bmargoli@umich.edu.

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