The SH2-SH2-SH3 domain of phospholipase C-γ1 directly binds to translational elongation factor-1α

Myung Jong Kim, Fuchum Si, Su Jeong Kim, Seung Bum Hong, Jong Ik Hwang, He Jin Lee, Seung Jae Lee, Jong Soo Chang, Young Han Lee, Sung Ho Ryu, Pann Ghill Suh

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Phospholipase C-γ1 (PLC-γ1) 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-1α (EF-1α) as a binding protein of PLC-γ1 from the human B-lymphocyte library. Direct interaction between EF-1α and PLC-γ1 was confirmed by the in vitro binding experiment using purified PLC-γ1. Furthermore, from the in vitro binding experiment, we could demonstrate that the carboxyl terminal region of EF-1α is involved in the interaction with PLC-γ1, and that both SH2 and SH3 domains of PLC-γ1 are required for the interaction with EF-1α. In vivo interaction between EF-1α and PLC-γ1 was confirmed by the immunoprecipitation experiment using anti-EF-1α antibody. The interaction between EF-1α and PLC-γ1 was enhanced by EGF-treatment. Taken together, we suggest that EF-1α might play a role in PLC-γ1-mediated signal transduction.

Original languageEnglish
Pages (from-to)631-637
Number of pages7
JournalMolecules and cells
Volume9
Issue number6
Publication statusPublished - 1999 Dec 31
Externally publishedYes

Keywords

  • EF-1α
  • PLC-γ1
  • Src Homology Domain
  • Yeast Two Hybrid System

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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    Kim, M. J., Si, F., Kim, S. J., Hong, S. B., Hwang, J. I., Lee, H. J., Lee, S. J., Chang, J. S., Lee, Y. H., Ryu, S. H., & Suh, P. G. (1999). The SH2-SH2-SH3 domain of phospholipase C-γ1 directly binds to translational elongation factor-1α. Molecules and cells, 9(6), 631-637.