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J. Biol. Chem., Vol. 281, Issue 19, 13805-13816, May 12, 2006

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ProSAP-interacting Protein 1 (ProSAPiP1), a Novel Protein of the Postsynaptic Density That Links the Spine-associated Rap-Gap (SPAR) to the Scaffolding Protein ProSAP2/Shank3^*

Doreen Wendholt, Christina Spilker, Angelika Schmitt, Anna Dolnik, Karl-Heinz Smalla, Christian Proepper, Juergen Bockmann, Kenji Sobue^¶, Eckart D. Gundelfinger, Michael R. Kreutz¹, and Tobias M. Boeckers²

From the Institute for Anatomy and Cell Biology, Ulm University, 89081 Ulm, Germany, AG Molecular Mechanisms of Plasticity, Department of Neurochemistry/Molecular Biology, Leibniz Institute for Neurobiology, 39118 Magdeburg, Germany, and the ^¶Department of Neuroscience, Osaka University School of Medicine, Suita, Osaka 565, Japan

ProSAPs/Shanks are a family of proteins that have a major scaffolding function for components of the postsynaptic density (PSD) of excitatory brain synapses. Members of the family harbor a variety of domains for protein-protein interactions, one of which is a unique PDZ domain that differs significantly from those of other proteins. We have identified a novel binding partner for this PDZ domain, termed ProSAPiP1, that is highly enriched in the PSD and shares significant sequence homology with the PSD protein PSD-Zip70. Both molecules code for a Fez1 domain that can be found in a total of four related proteins. ProSAPiP1 is widely expressed in rat brain and co-localizes with ProSAP2/Shank3 in excitatory spines and synapses. ProSAP2/Shank3 co-immunoprecipitates with ProSAPiP1 but not with PSD-Zip70. Both proteins, however, bind and recruit SPAR to synapses with a central coiled-coil region that harbors a leucine zipper motif. This region is also responsible for homo- and heteromultimerization of ProSAPiP1 and PSD-Zip70. Thus, ProSAPiP1 and PSD-Zip70 are founders of a novel family of scaffolding proteins, the "Fezzins," which adds further complexity to the organization of the PSD protein network.

Received for publication, February 6, 2006 , and in revised form, March 1, 2006.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ278801 [GenBank] and NM_014731 [GenBank] .

^* This work was supported by Deutsche Forschungsgemeinschaft Grants Bo1718/2-2, SFB497-B8 (to T. M. B. and J. B.), and Kr1879/2-2 (to M. R. K.), European Union Grant QLG3-CT-2001-01181 (to E. D. G.), and the Fond der Chemischen Industrie. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence may be addressed: AG "Molecular Mechanisms of Plasticity," Dept. of Neurochemistry/Molecular Biology, Leibniz Institute for Neurobiology, Brenneckestr. 6, 39118 Magdeburg, Germany. Tel.: 49-391-6263518; Fax: 49-391-6263229; E-mail: michael.kreutz{at}ifn-magdeburg.de.

² To whom correspondence may be addressed: Institute of Anatomy and Cell Biology, Ulm University, Albert Einstein Allee 11, 89081 Ulm, Germany. Tel.: 49-731-50023220; Fax: 49-731-50023217; E-mail: tobias.boeckers{at}uni-ulm.de.

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