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Related Concept Videos

Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Protein-protein Interfaces02:04

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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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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Updated: Sep 14, 2025

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks
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Proximity labeling techniques for protein-protein interaction mapping in plants.

Beyza Özmen1, Leonard Blaschek1, Michael Ogden1

  • 1Copenhagen Plant Science Center (CPSC), Department of Plant & Environmental Sciences, University of Copenhagen, Frederiksberg C, Denmark.

The Journal of Biological Chemistry
|July 23, 2025
PubMed
Summary

Proximity labeling (PL) techniques enable mapping of protein-protein interactions in living cells. This review details enzyme-based PL methods, their challenges, and optimization strategies for plant research.

Keywords:
TOR complexcelluloseplantsprotein-protein interactions (PPIs)proximity labeling (PL)

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Plant Science

Background:

  • Protein-protein interactions (PPIs) are crucial for cellular functions like signaling and metabolism.
  • Studying PPIs in vivo, especially within complex plant cells, is challenging.
  • Proximity labeling (PL) techniques offer a powerful solution for mapping interactions in native environments.

Purpose of the Study:

  • To review enzyme-based proximity labeling methods for studying protein-protein interactions.
  • To discuss the unique challenges and considerations for implementing PL in plants.
  • To propose future directions for enhancing PL technique efficiency and flexibility in plant research.

Main Methods:

  • Summarizing mechanisms, strengths, and weaknesses of various enzyme-based PL methods.
  • Highlighting experimental optimization strategies for plant systems.
  • Identifying areas for future development in PL technologies.

Main Results:

  • Enzyme-based PL methods provide real-time mapping of biomolecular interactions in vivo.
  • PL techniques have emerged as valuable tools in plant biology despite implementation challenges.
  • Key considerations for optimizing PL experiments in plants have been identified.

Conclusions:

  • Proximity labeling is a rapidly advancing field with significant potential for plant science.
  • Further development is needed to improve the efficiency and flexibility of PL tools for plant research.
  • This review provides a comprehensive overview for researchers utilizing or developing PL techniques in plants.