Identification and Characterization of the Interaction between Heat-Shock Protein 90 and Phospholipase C-γ1

Su Jeong Kim, Myung Jong Kim, Yong Kim, Fu Chun Si, Sung Ho Ryu, Pann Ghill Suh*

*Corresponding author for this work

Research output: Contribution to journalArticle

Abstract

Phosphoinositide-specific phospholipase C-γ1 (PLC-γ1) is a pivotal mediator in the signal transduction cascades induced by many growth factors. Using a yeast two-hybrid system, heat-shock protein 90 (Hsp90) was identified as a PLC-γ1-binding protein. A co-immunoprecipitation experiment, using anti-PLC-γ1 antibody, demonstrated an in vivo interaction between Hsp90 and PLC-γ1 in the NIH-3T3 cells. The interaction in NIH-3T3 was unaffected by the PDGF treatment, inducing phosphorylation and activation of PLC- γ1. Direct interaction between Hsp90 and PLC-γ1 was confirmed by in vitro binding experiments using purified Hsp90 and PLC-γ1. Furthermore, Hsp90 increased the PIP2-hydrolyzing activity of PLC-γ1 up to 2-fold at 0.1μM in vitro. Taken together, we show for the first time, the interaction of PLC-γ1 with Hsp90, both in vivo and in vitro. We suggest that Hsp90 may play a role in PLC-γ1-mediated signal transduction.

Original languageEnglish (US)
Pages (from-to)97-102
Number of pages6
JournalJournal of Biochemistry and Molecular Biology
Volume33
Issue number2
StatePublished - Mar 31 2000

Keywords

  • Hsp90
  • In vitro binding experiment
  • PLC-γ1
  • Protein-Protein interaction
  • Yeast two-hybrid system

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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