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Protein Networks

Protein Networks

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.
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Protein-protein Interfaces

Protein-protein Interfaces

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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Related Experiment Video

Updated: Aug 26, 2025

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

Deciphering Spatial Protein-Protein Interactions in Brain Using Proximity Labeling.

Boby Mathew¹, Shveta Bathla², Kenneth R Williams¹

¹Yale/NIDA Neuroproteomics Center, New Haven, Connecticut, USA; Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut, USA.

Molecular & Cellular Proteomics : MCP

|October 5, 2022

Summary

This summary is machine-generated.

Proximity labeling identifies protein interactions in the brain, aiding understanding of neurobiology and disorders. This powerful technique maps cellular functions and protein-protein interactions (PPIs) in challenging neural environments.

Keywords:

biotinylation neuroproteomics protein interaction network protein–protein interactions proximity labeling

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Area of Science:

Neurobiology
Molecular Biology
Biochemistry

Background:

Cellular functions are governed by biomolecular complexes, including protein-protein interactions (PPIs).
PPIs are critical for nerve cell functions and their dysregulation is implicated in neurobiological disorders.
A comprehensive understanding of cellular biology necessitates cataloging protein interactions.

Purpose of the Study:

To review recent advancements in proximity labeling techniques.
To highlight the application of proximity labeling in neurobiology research.
To demonstrate the utility of proximity labeling for characterizing complex PPIs in the brain.

Main Methods:

Utilizes enzyme-catalyzed biotinylation to label proximal interacting proteins within 10-300 nm.
Applies proximity labeling to identify proteomes in specific brain cell types.
Employs proximity labeling to analyze proteomes and PPIs in difficult-to-isolate structures like the synaptic cleft.

Main Results:

Proximity labeling enables characterization of spatiotemporal features of complex PPIs in the brain.
Identifies proteomes within distinct neuronal and glial cell populations.
Facilitates the study of protein interactions in challenging subcellular and extracellular spaces.

Conclusions:

Proximity labeling is a powerful tool for dissecting cellular and molecular mechanisms in neurobiology.
This technique enhances the understanding of protein-protein interactions relevant to brain function and disease.
Recent advances offer new avenues for exploring the intricate proteomic landscape of the nervous system.