Protein phosphatase-1 (PP1) is a 37 KDa highly conserved ubiquitous Ser/Thr phosphatase that catalyzes 1/3rd of all dephosphorylation reactions in cells. The catalytic activity of PP1 is tightly regulated inside the cells by the formation of holoenzyme complexes with more than 200 regulatory proteins that convey specificity to the catalytic subunit of PP1. The first part of the talk would be focused on a reverse chemical genetics approach, which we have used to identify a cell-permeable peptide disruptor of PP1 holoenzyme complexes; a chemical tool that was long sought by the biological community to selectively interfere with PP1 signaling pathways. The compound disrupts several PP1 holoenzyme complexes in living cells eventually activating PP1; making it the first well characterized PP1 activator. A tool that will unravel several unsolved mysteries in cellular signaling processes. The second part of the talk deals with future research plans to develop a ‘chemical-toolbox’ to study PP1 signaling events inside cells and develop lead compounds targeted towards PP1 as novel cancer chemotherapeutics.
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