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KMID : 0578319990090060631
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Molecules and Cells
1999 Volume.9 No. 6 p.631 ~ p.637
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The SH2-SH2-SH3 domain of phospholipase C-gamma1 directly binds to translational elongation factor-1alpha
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Kim MJ
Si F/Kim SJ/Hong SB/Hwang JI/Lee HJ/Lee SJ/Chang JS/Lee YH/Ryu SH/Suh PG
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Abstract
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Phospholipase C-gamma1 (PLC-gamma1) is a lipase that hydrolyzes PIP2 to generate two second messengers, IP3 and DAG. By using the yeast two-hybrid system, we identified the translational elongation factor-1alpha (EF-1alpha) as a binding protein of PLC-gamma1 from the human B-lymphocyte library. Direct interaction between EF-1alpha and PLC-gamma1 was confirmed by the in vitro binding experiment using purified PLC-gamma1. Furthermore, from the in vitro binding experiment, we could demonstrate that the carboxyl terminal region of EF-1alpha is involved in the interaction with PLC-gamma1, and that both SH2 and SH3 domains of PLC-gamma1 are required for the interaction with EF-1alpha. In vivo interaction between EF-1alpha and PLC-gamma1 was confirmed by the immunoprecipitation experiment using anti-EF-1alpha antibody. The interaction between EF-1alpha and PLC-gamma1 was enhanced by EGF-treatment. Taken together, we suggest that EF-1alpha might play a role in PLC-gamma1-mediated signal transduction.
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KEYWORD
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