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Related Experiment Video

Updated: Aug 8, 2025

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks

Published on: May 17, 2020

Proximity Labeling in Plants.

Shou-Ling Xu^1,2, Ruben Shrestha¹, Sumudu S Karunadasa¹

¹Department of Plant Biology, Carnegie Institution for Science, Stanford, California, USA;

Annual Review of Plant Biology

|February 28, 2023

Summary

Proximity-dependent biotinylation labeling combined with mass spectrometry (PL-MS) is a powerful technique to map protein interactions within cells. This review highlights PL-MS applications and strategies for the plant science field.

Keywords:

cell type–specific proteome protein–nucleotide interaction protein–protein interaction proximity labeling quantification subcellular proteome

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Last Updated: Aug 8, 2025

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks

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Published on: May 17, 2020

AirID-Based Proximity Labeling for Protein-Protein Interaction in Plants

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Published on: September 16, 2022

Visualizing Lignification Dynamics in Plants with Click Chemistry: Dual Labeling is BLISS!

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Published on: January 26, 2018

Area of Science:

Molecular Biology
Proteomics
Biochemistry

Background:

Proteins are crucial cellular components involved in dynamic interactions, essential for biological processes.
Understanding these protein networks is key to deciphering cellular function.
Traditional proteomics methods face limitations in dissecting complex cellular networks.

Purpose of the Study:

To review the application of proximity-dependent biotinylation labeling combined with mass spectrometry (PL-MS) in plant science.
To discuss experimental designs, enzyme choices, and quantification strategies for PL-MS.
To explore the potential and future perspectives of PL-MS in plant biology.

Main Methods:

Proximity-dependent biotinylation labeling (PL) enzyme fused to a target protein or localization signal.
Enzymatic labeling of proximal proteins within a defined radius.
Capture of biotinylated proteins using streptavidin beads.
Identification and quantification of proteins via mass spectrometry (MS).

Main Results:

Engineered PL enzymes like TurboID offer enhanced enzymatic activity and improved signal-to-noise ratios.
PL-MS enables spatiotemporal mapping of protein interactions.
This technique overcomes limitations of traditional methods like biochemical fractionation and affinity purification MS.

Conclusions:

PL-MS is a revolutionary proteomics technique for dissecting complex cellular networks.
The review focuses on biotin ligase-based PL-MS applications relevant to plant science.
Future perspectives and validation strategies for PL-MS in plants are discussed.