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Interaction profiling methods to map protein and pathway targets of bioactive ligands
Jun X Huang1, John S Coukos1, Raymond E Moellering1
1Department of Chemistry, The University of Chicago, 929 E. 57th Street, Chicago, IL, 60637, USA; Institute for Genomics and Systems Biology, The University of Chicago, 929 E. 57th Street, Chicago, IL, 60637, USA.
Current Opinion in Chemical Biology
|March 9, 2020
Summary
Emerging proteomic technologies map protein interactions in live cells. Combining methods reveals small molecule targets and cellular signaling networks for biological studies.
Area of Science:
- Proteomics
- Systems Biology
- Chemical Biology
Background:
- Omic profiling aims to understand biomolecule function and interactions, not just presence.
- Cellular signaling networks are complex and dynamic, responding to various stimuli.
- Understanding protein interactions is crucial for deciphering cellular functions.
Purpose of the Study:
- To review emerging proteomic technologies for detecting protein interaction networks in live cells.
- To present a framework for integrating 'top-down' and 'bottom-up' proteomic methods.
- To enable direct identification of small molecule binding targets and influenced pathways.
Main Methods:
- Review of live-cell proteomic technologies for interaction network detection.
- Conceptual framework for combining top-down and bottom-up proteomic approaches.
- Integration of interaction profiling with proteomic data analysis.
Main Results:
- Emerging proteomic technologies can detect protein interaction networks in real-time.
- Integrated methods allow for direct identification of small molecule ligand binding targets.
- Unbiased discovery of proteins and pathways influenced by bioactive small molecules is achievable.
Conclusions:
- Integrated, interaction-based proteomic profiling offers a dynamic view of cellular signaling.
- These methods advance basic and translational biological research.
- Holistic mapping of protein responses to stimuli is now feasible.
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