Protein-protein interactions (PPIs) play a fundamental role in all cellular processes. Understanding the PPIs illuminates the protein placement in cellular signaling pathways. The effects of TSC1 and TSC2 in mTOR signaling pathway and in tuberous sclerosis have been reported in existing literature. However, it’s primary role still remains an unanswered question. TSC1 acts as cochaperone for both Hsp70 and Hsp90. Most cancer cells have elevated levels of Hsp70 and Hsp90. Therefore, understanding the interaction of TSC1, TSC2, Hsp70, and Hsp90 will provide an understanding in cancer cell signaling pathway. In our work, we focus on the synthesis, structural characterization and carry out biochemical assays to understand the underlying molecular mechanism in these proteins and to identify the role of cochaperones. This research will help in understanding the chaperone cycle as well, in addition to the cell signaling pathway. These interactions, in response to varied cellular stresses - in cancer cells and in various cell types - will help understand the exact role of these proteins in chaperone machinery.

Tuberous Sclerosis Complex as molecular switch and co-chaperone

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27th CRSI National Symposium in Chemistry

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