Related Experiment Video
Updated: May 11, 2026
09:39
Mapping Dysfunctional Protein-Protein Interactions in Disease
Published on: October 24, 2025
Protein-protein interaction networks: probing disease mechanisms using model systems
1Banting and Best Department of Medical Research and Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada.
Genome Medicine
|May 3, 2013
Summary
Mass spectrometry-based proteomics reveals protein-protein interactions (PPIs) and complexes critical for cellular function. Mapping these interactions aids in understanding diseases like cancer and neurodegenerative disorders.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Protein-protein interactions (PPIs) and multi-protein complexes are fundamental to cellular processes in all organisms.
- Aberrant PPIs and protein complex alterations are linked to human diseases.
- Mass spectrometry (MS)-based proteomics offers powerful tools for large-scale interaction mapping.
Purpose of the Study:
- To review the application of MS-based proteomics for analyzing PPI networks and protein complexes.
- To highlight the use of various model systems, including human cells, in disease mechanism studies.
Main Methods:
- Utilizing mass spectrometry (MS)-based proteomics techniques.
- Systematic large-scale mapping of physical interactions.
- Analysis of PPI networks and protein complexes.
Main Results:
- MS-based proteomics enables comprehensive analysis of PPIs and complexes.
- This approach is applicable across diverse model systems.
- Facilitates the study of molecular underpinnings of various diseases.
Conclusions:
- MS-based proteomics is a key technology for dissecting PPIs and complexes in health and disease.
- Understanding these interactions is crucial for advancing research in oncology, cardiology, endocrinology, infectious diseases, and neurology.
Related Concept Videos
02:26Protein 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.
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,...
02:26Protein 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.
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,...
02:04Protein-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 polypeptide...
02:04Protein-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 polypeptide...
02:40Ligand Binding Sites
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.