This web page was produced as an assignment for Genetics 564, an undergraduate capstone course at UW-Madison.
How do scientists analyze protein-protein interactions?
Protein-protein interactions can be analyzed using mass spectrometry (MS). To perform MS analysis you must first extract proteins from your sample and isolate the protein you wish to study. This can be done by tandem-affinity purification (TAP) and confirmed by yeast two-hybrid or co-immunoprecipitation analyses. Then, the proteins you have purified can be fed into the MS workflow to determine the proteins that are interacting with your protein of interest. [1,2]
What proteins does LIPC interact with?
LIPC mostly interacts with proteins that are involved in lipid and cholesterol homeostasis and metabolism. This is expected as its main function is to convert intermediate-density lipoproteins into low-density lipoproteins. LIPC has also been shown to act as a ligand for the low-density lipoprotein receptor even when enzymatically inactive. When you enrich for proteins related to progesterone synthesis, some connections between LIPC and interacting partners emerge. This may hint at a closer relationship between the pathways LIPC is directly involved in and progesterone synthesis.
LIPC Protein Interaction Network
LIPC Protein Interaction Network Enriched for Progesterone Synthesis Proteins
Conclusion
Proteins have to interact to carry out their functions. We can interrogate these interaction netwroks to learn more about what these proteins do and how they function.
References
[1] What is proteomics? (2018, September 12). Retrieved from https://www.ebi.ac.uk/training/online/course/proteomics-introduction-ebi-resources/what-proteomics
[2] Graves, P. R., & Haystead, T. A. (n.d.). Proteomics and the Molecular Biologist. Handbook of Proteomic Methods, 3-16. doi:10.1385/1-59259-414-x:3
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[2] Graves, P. R., & Haystead, T. A. (n.d.). Proteomics and the Molecular Biologist. Handbook of Proteomic Methods, 3-16. doi:10.1385/1-59259-414-x:3
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