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The Interaction of Phospholipase C-{beta}3 with Shank2 Regulates mGluR-mediated Calcium Signal

Hwang, Jong-Ik and Kim, Hyeon Soo and Lee, Jae Ran and Kim, Eunjoon and Ryu, Sung Ho and Suh, Pann-Ghil (2005) The Interaction of Phospholipase C-{beta}3 with Shank2 Regulates mGluR-mediated Calcium Signal. Journal of Biological Chemistry, 280 (13). pp. 12467-12473. ISSN 0021-9258. http://resolver.caltech.edu/CaltechAUTHORS:HWAjbc05

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Abstract

Phospholipase C-{beta} isozymes that are activated by G protein-coupled receptors (GPCR) and heterotrimeric G proteins carry a PSD-95/Dlg/ZO-1 (PDZ) domain binding motif at their C terminus. Through interactions with PDZ domains, this motif may endow the PLC-{beta} isozyme with specific roles in GPCR signaling events that occur in compartmentalized regions of the plasma membrane. In this study, we identified the interaction of PLC-{beta}3 with Shank2, a PDZ domain-containing multimodular scaffold in the postsynaptic density (PSD). The C terminus of PLC-{beta}3, but not other PLC-{beta} isotypes, specifically interacts with the PDZ domain of Shank2. Homer 1b, a Shank-interacting protein that is linked to group I metabotropic glutamate receptors and IP3 receptors, forms a multiple complex with Shank2 and PLC-{beta}3. Importantly, microinjection of a synthetic peptide specifically mimicking the C terminus of PLC-{beta}3 markedly reduces the mGluR-mediated intracellular calcium response. These results demonstrate that Shank2 brings PLC-{beta}3 closer to Homer 1b and constitutes an efficient mGluR-coupled signaling pathway in the PSD region of neuronal synapses.


Item Type:Article
Additional Information:Copyright © 2005 by the American Society for Biochemistry and Molecular Biology. Received for publication, September 17, 2004, and in revised form, December 30, 2004. Originally published In Press as doi:10.1074/jbc.M410740200 on January 4, 2005 This study was supported by the National R & D Program for Fusion Strategy of Advanced Technologies of Ministry of Science & Technology (MOST) and by Korea Science and Engineering Foundation (KOSEF) through the Center for Cell Signaling Research at Ewha Womans University, Korea. 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.
Record Number:CaltechAUTHORS:HWAjbc05
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:HWAjbc05
Alternative URL:http://dx.doi.org/10.1074/jbc.M410740200
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:4804
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:07 Sep 2006
Last Modified:26 Dec 2012 09:01

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