Related Experiment Video
Updated: Aug 5, 2025
07:02
TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks
Published on: May 17, 2020
24.4K
Identification of Myelin Basic Protein Proximity Interactome Using TurboID Labeling Proteomics.
Evgeniya V Smirnova1, Tatiana V Rakitina1, Rustam H Ziganshin1
1Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia.
Cells
|March 29, 2023
Summary
Myelin basic protein (MBP) interacts with proteins involved in cell adhesion, transport, and metabolism, revealing new roles in myelin sheath integrity and potential links to neurodegeneration.
Area of Science:
- Neuroscience
- Molecular Biology
- Proteomics
Background:
- Myelin basic protein (MBP) is crucial for myelin sheath structure and has autoantigenic properties in multiple sclerosis (MS).
- Understanding MBP's intracellular interactions is challenging due to its unfolded nature, charge, and localization.
- Proximity labeling proteomics, while powerful, can yield high background noise.
Purpose of the Study:
- To identify the interactome of Myelin basic protein (MBP) using proximity labeling.
- To refine MBP interaction data by analyzing deaminated MBP and p21 variants to reduce background noise.
- To elucidate MBP's role in cellular processes beyond its structural function in the myelin sheath.
Main Methods:
- Utilized TurboID-based proximity labeling fused with MBP to map protein interactions.
- Employed deaminated MBP and p21 as controls to distinguish specific MBP interactions from background noise.
- Analyzed protein colocalization and interactions in the plasma membrane region and other cellular compartments.
Main Results:
- Identified MBP colocalization with adhesion proteins (occludin, MPZL1), solute transporters (ZIP6, SNAT1), Ephrin-B1, and vesicle transport machinery (SNAP23, VAMP3, hSec23B, dynein).
- Detected potential MBP interactions with proteins involved in iron and lipid metabolism (GM2 activator, ACSL4, CYB5R1, STEAP3).
- These findings suggest MBP's involvement in ferroptosis and vesicle docking pathways.
Conclusions:
- MBP interacts with a diverse set of proteins beyond its structural role in myelin.
- MBP may play a significant role in regulating iron and lipid metabolism, potentially influencing ferroptosis.
- These newly identified interactions suggest a broader role for MBP in maintaining myelin integrity and potentially in autoimmune neurodegeneration.
Related Concept Videos
01:33Proteomics
7.6K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
7.6K
02:26Protein Networks
4.0K
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,...
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,...
4.0K