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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Related Experiment Video

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Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves
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Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

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Visualizing protein interactions by bimolecular fluorescence complementation in Xenopus.

Yasushi Saka1, Anja I Hagemann, James C Smith

  • 1Interdisciplinary Research Institute, CNRS USR3078, Institut de Biologie de Lille, 1 rue du Professeur Calmette, Lille Cedex, France.

Methods (San Diego, Calif.)
|July 1, 2008
PubMed
Summary
This summary is machine-generated.

This study details a new method using Bimolecular Fluorescence Complementation (BiFC) in Xenopus laevis embryos to visualize protein interactions. The optimized Venus fluorescent protein allows real-time monitoring of signaling pathways.

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Related Experiment Videos

Last Updated: Jul 4, 2026

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves
11:10

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Bimolecular Fluorescence Complementation
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Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation (BiFC) System
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Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation (BiFC) System

Published on: September 16, 2011

Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Biochemistry

Background:

  • Bimolecular fluorescence complementation (BiFC) is a powerful technique for visualizing protein-protein interactions in living cells.
  • Real-time in vivo visualization of protein interactions is crucial for understanding dynamic cellular processes.
  • The South African clawed frog, Xenopus laevis, is a widely used model organism in developmental biology.

Purpose of the Study:

  • To establish and optimize methods for implementing Bimolecular Fluorescence Complementation (BiFC) in Xenopus laevis embryos.
  • To develop a modified Venus fluorescent protein for enhanced detection of protein interactions.
  • To demonstrate the utility of this BiFC system for monitoring signaling pathways in vivo.

Main Methods:

  • Implementation of BiFC assays in Xenopus laevis embryos.
  • Utilized Venus, an enhanced yellow fluorescent protein (YFP), for rapid detection.
  • Introduced a T153M point mutation in the N-terminal Venus fragment to minimize self-complementation.
  • Applied the system to monitor transforming growth factor beta (TGF-β) family signaling.

Main Results:

  • Successfully adapted BiFC for use in Xenopus embryos, enabling visualization of protein interactions.
  • The modified Venus protein (T153M) reduced background noise from spontaneous fragment interactions.
  • Demonstrated the ability to monitor TGF-β signaling in real-time within Xenopus embryonic cells.

Conclusions:

  • The developed BiFC method provides a robust tool for studying protein-protein interactions in Xenopus embryos.
  • This technique facilitates real-time monitoring of developmental signaling pathways.
  • The optimized Venus reagent enhances the reliability and sensitivity of BiFC assays.