Abstract
Phospholipase C-β 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-β 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-β3 with Shank2, a PDZ domain-containing multimodular scaffold in the postsynaptic density (PSD). The C terminus of PLC-β3, but not other PLC-β 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-β3. Importantly, microinjection of a synthetic peptide specifically mimicking the C terminus of PLC-β3 markedly reduces the mGluR-mediated intracellular calcium response. These results demonstrate that Shank2 brings PLC-β3 closer to Homer 1b and constitutes an efficient mGluR-coupled signaling pathway in the PSD region of neuronal synapses.
| Original language | English |
|---|---|
| Pages (from-to) | 12467-12473 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 280 |
| Issue number | 13 |
| DOIs | |
| Publication status | Published - 2005 Apr 1 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
The interaction of phospholipase C-β3 with Shank2 regulates mGluR-mediated calcium signal. / Hwang, Jong-Ik; Kim, Hyeon Soo; Jae, Ran Lee; Kim, Eunjoon; Sung, Ho Ryu; Suh, Pann Ghill.
In: Journal of Biological Chemistry, Vol. 280, No. 13, 01.04.2005, p. 12467-12473.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The interaction of phospholipase C-β3 with Shank2 regulates mGluR-mediated calcium signal
AU - Hwang, Jong-Ik
AU - Kim, Hyeon Soo
AU - Jae, Ran Lee
AU - Kim, Eunjoon
AU - Sung, Ho Ryu
AU - Suh, Pann Ghill
PY - 2005/4/1
Y1 - 2005/4/1
N2 - Phospholipase C-β 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-β 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-β3 with Shank2, a PDZ domain-containing multimodular scaffold in the postsynaptic density (PSD). The C terminus of PLC-β3, but not other PLC-β 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-β3. Importantly, microinjection of a synthetic peptide specifically mimicking the C terminus of PLC-β3 markedly reduces the mGluR-mediated intracellular calcium response. These results demonstrate that Shank2 brings PLC-β3 closer to Homer 1b and constitutes an efficient mGluR-coupled signaling pathway in the PSD region of neuronal synapses.
AB - Phospholipase C-β 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-β 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-β3 with Shank2, a PDZ domain-containing multimodular scaffold in the postsynaptic density (PSD). The C terminus of PLC-β3, but not other PLC-β 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-β3. Importantly, microinjection of a synthetic peptide specifically mimicking the C terminus of PLC-β3 markedly reduces the mGluR-mediated intracellular calcium response. These results demonstrate that Shank2 brings PLC-β3 closer to Homer 1b and constitutes an efficient mGluR-coupled signaling pathway in the PSD region of neuronal synapses.
UR - http://www.scopus.com/inward/record.url?scp=16844362568&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=16844362568&partnerID=8YFLogxK
U2 - 10.1074/jbc.M410740200
DO - 10.1074/jbc.M410740200
M3 - Article
C2 - 15632121
AN - SCOPUS:16844362568
VL - 280
SP - 12467
EP - 12473
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 13
ER -