The interaction of phospholipase C-beta 3 with Shank2 regulates mGluR-mediated calcium signal
SCIE
SCOPUS
- Title
- The interaction of phospholipase C-beta 3 with Shank2 regulates mGluR-mediated calcium signal
- Authors
- Hwang, JI; Kim, HS; Lee, JR; Kim, E; Ryu, SH; Suh, PG
- Date Issued
- 2005-04-01
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLO
- 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.
- Keywords
- METABOTROPIC GLUTAMATE RECEPTORS; POSTSYNAPTIC DENSITY; SYNAPTIC PROTEINS; INTRAMOLECULAR INTERACTION; PDZ DOMAINS; FAMILY; BRAIN; HOMER; EXPRESSION; COMPLEXES
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/24696
- DOI
- 10.1074/jbc.M410740200
- ISSN
- 0021-9258
- Article Type
- Article
- Citation
- JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 280, no. 13, page. 12467 - 12473, 2005-04-01
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