Abstract: Objective To identify the interaction between PLC-β3 and the PDZ domain-containing protein syntrophin, providing clues to the underlying roles of PLC-β3 in signaling pathway of the nervous system. Methods The carboxyl-terminal of PLC-β3 (PLC-β3-CT) was fused to GST protein by gene cloning. The resultant protein was used for examining interactions of PLC-β3-CT with the PDZ-domain of β2-syntrophin and γ2-syntrophin respectively by GST pull-down assay. Results PLC-β3-CT cDNA was cloned into the expression vector pGEX-4T-1 successfully, and the GST fusion protein was overexpressed and purified in E.coli system. GST pull-down experiments revealed that the PDZ domain of β2-syntrophin, but not γ2-syntrophin was robustly pulled down by the carboxyl-terminal of PLC-β3. Conclusion These results provide a strong evidence for further studying the intracellular association of the PLC-β3 and β2-syntrophin and helping in exploring their potential physiological significances in signaling pathway of the nervous system.

Key words: PLC-β3, syntrophin, protein interaction