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Related Experiment Video

Updated: Jul 17, 2026

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation
10:52

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation

Published on: January 6, 2016

Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras.

C Song1, C D Hu, M Masago

  • 1Department of Physiology II, Kobe University School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan.

The Journal of Biological Chemistry
|October 7, 2000
PubMed
Summary

Researchers discovered a new enzyme, Phosphoinositide-specific phospholipase C (PI-PLC) epsilon, that directly interacts with Ras proteins. This interaction regulates cellular signaling pathways by controlling phosphoinositide breakdown.

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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

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Last Updated: Jul 17, 2026

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation
10:52

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation

Published on: January 6, 2016

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Phosphoinositide-specific phospholipase C (PI-PLC) enzymes are crucial for intracellular signal transduction.
  • Over ten human PI-PLC isoforms exist, categorized into beta, gamma, and delta classes with distinct regulatory mechanisms.

Purpose of the Study:

  • To identify and characterize a novel class of human PI-PLC, termed PLCepsilon.
  • To investigate the interaction between PLCepsilon and Ras proteins and its functional consequences.

Main Methods:

  • Identification and domain analysis of the novel PLCepsilon.
  • Ras-associating domain binding assays with GTP-bound Ha-Ras and Rap1A.
  • Co-expression studies to observe PLCepsilon translocation in response to activated Ha-Ras and epidermal growth factor (EGF) stimulation.
  • Liposome-based reconstitution assays to assess PI-PLC activity.

Main Results:

  • PLCepsilon possesses a unique structure with Ras-associating and CDC25-like domains.
  • The Ras-associating domain specifically binds GTP-bound Ha-Ras and Rap1A.
  • Activated Ha-Ras induces PLCepsilon translocation to the plasma membrane, a process regulated by EGF and inhibited by dominant-negative Ha-Ras.
  • Ha-Ras directly stimulates PLCepsilon's phosphoinositide-hydrolyzing activity in a GTP-dependent manner in vitro.

Conclusions:

  • Ras directly regulates phosphoinositide breakdown through the membrane targeting of PLCepsilon.
  • PLCepsilon represents a novel class of PI-PLC regulated by Ras signaling pathways.