HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Deguchi, M. Articles by Takai, Y. Search for Related Content PubMed PubMed Citation Articles by Deguchi, M. Articles by Takai, Y.

J Biol Chem, Vol. 273, Issue 41, 26269-26272, October 9, 1998

COMMUNICATION
BEGAIN (Brain-enriched Guanylate Kinase-associated Protein), a Novel Neuronal PSD-95/SAP90-binding Protein

Maki Deguchi, Yutaka Hata, Masakazu Takeuchi, Nobuyuki Ide, Kazuyo Hirao, Ikuko Yao, Mina Irie, Atsushi Toyoda, and Yoshimi Takai

From the  Takai Biotimer Project, ERATO, Japan Science and Technology Corporation, c/o JCR Pharmaceuticals Co. Ltd., 2-2-10 Murotani, Nishi-ku, Kobe 651-2241, Japan and the  Department of Molecular Biology and Biochemistry, Osaka University Medical School, 2-2 Yamada-Oka, Suita, Osaka 565, Japan

PSD-95/SAP90 is a synaptic membrane-associated guanylate kinase with three PDZ, one SH3, and one guanylate kinase (GK) domain. PSD-95/SAP90 binds various proteins through the PDZ domains and organizes synaptic junctions. PSD-95/SAP90 also interacts with the postsynaptic density (PSD) fraction-enriched protein, named SAPAP (also called GKAP and DAP), through the GK domain. SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD. Here we report a novel protein interacting with the GK domain of PSD-95/SAP90, BEGAIN. BEGAIN is specifically expressed in brain and enriched in the PSD fraction. BEGAIN is Triton X-100-soluble in the transfected cells but is recruited to the Triton X-100-insoluble fraction by SAPAP when coexpressed with PSD-95/SAP90. BEGAIN may be a novel PSD component associated with the core complex of PSD-95/SAP90 and SAPAP.

---

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

This article has been cited by other articles:

				M. Richter, K. K. Murai, C. Bourgin, D. T. Pak, and E. B. Pasquale The EphA4 Receptor Regulates Neuronal Morphology through SPAR-Mediated Inactivation of Rap GTPases J. Neurosci., December 19, 2007; 27(51): 14205 - 14215. [Abstract] [Full Text] [PDF]

				N. Asaba, T. Hanada, A. Takeuchi, and A. H. Chishti Direct Interaction with a Kinesin-related Motor Mediates Transport of Mammalian Discs Large Tumor Suppressor Homologue in Epithelial Cells J. Biol. Chem., February 28, 2003; 278(10): 8395 - 8400. [Abstract] [Full Text] [PDF]

				O. Olsen and D. S. Bredt Functional Analysis of the Nucleotide Binding Domain of Membrane-associated Guanylate Kinases J. Biol. Chem., February 21, 2003; 278(9): 6873 - 6878. [Abstract] [Full Text] [PDF]

				I. Paarmann, O. Spangenberg, A. Lavie, and M. Konrad Formation of Complexes between Ca2+{middle dot}Calmodulin and the Synapse-associated Protein SAP97 Requires the SH3 Domain-Guanylate Kinase Domain-connecting HOOK Region J. Biol. Chem., October 18, 2002; 277(43): 40832 - 40838. [Abstract] [Full Text] [PDF]

				I. Yao, J. Iida, W. Nishimura, and Y. Hata Synaptic and Nuclear Localization of Brain-Enriched Guanylate Kinase-Associated Protein J. Neurosci., July 1, 2002; 22(13): 5354 - 5364. [Abstract] [Full Text] [PDF]

				L. McMahon, R. Legouis, J.-L. Vonesch, and M. Labouesse Assembly of C. elegans apical junctions involves positioning and compaction by LET-413 and protein aggregation by the MAGUK protein DLG-1 J. Cell Sci., March 8, 2002; 114(12): 2265 - 2277. [Abstract] [Full Text] [PDF]

				Y. Li, O. Spangenberg, I. Paarmann, M. Konrad, and A. Lavie Structural Basis for Nucleotide-dependent Regulation of Membrane-associated Guanylate Kinase-like Domains J. Biol. Chem., February 1, 2002; 277(6): 4159 - 4165. [Abstract] [Full Text] [PDF]

				F. Imamura, S. Maeda, T. Doi, and Y. Fujiyoshi Ligand Binding of the Second PDZ Domain Regulates Clustering of PSD-95 with the Kv1.4 Potassium Channel J. Biol. Chem., January 25, 2002; 277(5): 3640 - 3646. [Abstract] [Full Text] [PDF]

				H. Kawabe, H. Nakanishi, M. Asada, A. Fukuhara, K. Morimoto, M. Takeuchi, and Y. Takai Pilt, a Novel Peripheral Membrane Protein at Tight Junctions in Epithelial Cells J. Biol. Chem., December 14, 2001; 276(51): 48350 - 48355. [Abstract] [Full Text] [PDF]

				H. Shin, Y.-P. Hsueh, F.-C. Yang, E. Kim, and M. Sheng An Intramolecular Interaction between Src Homology 3 Domain and Guanylate Kinase-Like Domain Required for Channel Clustering by Postsynaptic Density-95/SAP90 J. Neurosci., May 15, 2000; 20(10): 3580 - 3587. [Abstract] [Full Text] [PDF]

				K. Hirao, Y. Hata, I. Yao, M. Deguchi, H. Kawabe, A. Mizoguchi, and Y. Takai Three Isoforms of Synaptic Scaffolding Molecule and Their Characterization. MULTIMERIZATION BETWEEN THE ISOFORMS AND THEIR INTERACTION WITH N-METHYL-D-ASPARTATE RECEPTORS AND SAP90/PSD-95-ASSOCIATED PROTEIN J. Biol. Chem., January 28, 2000; 275(4): 2966 - 2972. [Abstract] [Full Text] [PDF]

				H. Kawabe, Y. Hata, M. Takeuchi, N. Ide, A. Mizoguchi, and Y. Takai nArgBP2, a Novel Neural Member of Ponsin/ArgBP2/Vinexin Family That Interacts with Synapse-associated Protein 90/Postsynaptic Density-95-associated Protein (SAPAP) J. Biol. Chem., October 22, 1999; 274(43): 30914 - 30918. [Abstract] [Full Text] [PDF]

				I. Yao, Y. Hata, K. Hirao, M. Deguchi, N. Ide, M. Takeuchi, and Y. Takai Synamon, a Novel Neuronal Protein Interacting with Synapse-associated Protein 90/Postsynaptic Density-95-associated Protein J. Biol. Chem., September 24, 1999; 274(39): 27463 - 27466. [Abstract] [Full Text] [PDF]

				I. Yao, Y. Hata, N. Ide, K. Hirao, M. Deguchi, H. Nishioka, A. Mizoguchi, and Y. Takai MAGUIN, a Novel Neuronal Membrane-associated Guanylate Kinase-interacting Protein J. Biol. Chem., April 23, 1999; 274(17): 11889 - 11896. [Abstract] [Full Text] [PDF]

				T. Hanada, L. Lin, E. V. Tibaldi, E. L. Reinherz, and A. H. Chishti GAKIN, a Novel Kinesin-like Protein Associates with the Human Homologue of the Drosophila Discs Large Tumor Suppressor in T Lymphocytes J. Biol. Chem., September 8, 2000; 275(37): 28774 - 28784. [Abstract] [Full Text] [PDF]

				S. L. Nix, A. H. Chishti, J. M. Anderson, and Z. Walther hCASK and hDlg Associate in Epithelia, and Their Src Homology 3 and Guanylate Kinase Domains Participate in Both Intramolecular and Intermolecular Interactions J. Biol. Chem., December 22, 2000; 275(52): 41192 - 41200. [Abstract] [Full Text] [PDF]