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Related Concept Videos

G-protein Coupled Receptors01:21

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...

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Related Experiment Video

Updated: Jun 17, 2026

Imaging G-protein Coupled Receptor GPCR-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum
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A Reliable System for Quantitative G-Protein Activation Imaging in Cancer Cells.

Elena Mandrou1, Peter A Thomason1, Peggy I Paschke1

  • 1CRUK Scotland Institute, Garscube Campus, Glasgow G61 1BD, UK.

Cells
|July 12, 2024
PubMed
Summary
This summary is machine-generated.

We developed a superior fluorescence lifetime imaging microscopy (FLIM) method using a novel biosensor to reliably measure G-protein signaling activation in pancreatic cancer cells. This advance aids drug screening and basic cell biology research.

Keywords:
FLIMFRETG-protein signallingGPCRLPALPARPDACfluorescence lifetimelive cell imaging

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Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Signaling

Background:

  • Fluorescence resonance energy transfer (FRET) biosensors are crucial for studying G-protein signaling.
  • Fluorescence lifetime imaging microscopy (FLIM) offers quantitative advantages over intensity-based methods for FRET measurements.
  • Existing FLIM-FRET biosensors and analysis workflows present challenges in reliability and reproducibility.

Purpose of the Study:

  • To establish a robust FLIM-FRET system for detecting G-protein activation in live cells.
  • To compare the performance of a novel biosensor with existing ones.
  • To create a platform for drug screening and fundamental research in G-protein signaling.

Main Methods:

  • Utilized 2-photon time-correlated single-photon counting (TCSPC) FLIM.
  • Developed and implemented an mNeonGreen-Gαi3-mCherry-Gγ2 biosensor.
  • Applied the system to live primary mouse pancreatic ductal adenocarcinoma cells stimulated via lysophosphatidic acid receptor (LPAR).

Main Results:

  • Successfully detected Gαi3 activation using the novel FLIM-FRET biosensor in pancreatic cancer cells.
  • The mNeonGreen-Gαi3-mCherry-Gγ2 biosensor provided a superior signal compared to the mTurquoise2-mVenus biosensor.
  • Established a reproducible workflow for FLIM-FRET data acquisition and analysis.

Conclusions:

  • The developed FLIM-FRET system offers a reliable and sensitive method for studying G-protein signaling.
  • This platform has significant potential for drug discovery and advancing cell biology research.
  • The superior signal of the novel biosensor enhances the study of G-protein dynamics.