• Open Access

Development of a Peptide that Selectively Activates Protein Phosphatase-1 in Living Cells


  • J.C. thanks the Alexander von Humboldt Foundation and EMBO for postdoctoral fellowships. R.S. was funded by the EMBL-EIPOD program. M.K. acknowledges support from the German Science Foundation within the Emmy-Noether program. M.Bo. and M.Be. are supported by Flemish Concerted Research Action (GOA10/16), the National Science Foundation-Flanders (grant G.0478.08), the Prime Minister’s office (IAP-P6/28P, and the Cell Imaging Core of KU Leuven. A. Hoogmartens, T. Jaspers, N. Sente, G. Van der Hoeven, and A. McCarthy provided technical assistance. X-ray data was collected at SOLEIL synchrotron.


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The first cell-penetrating peptide that activates protein phosphatase-1 (PP1) by disrupting a subset of PP1 complexes in living cells has been developed. Activated PP1 rapidly dephosphorylates its substrates, counteracting kinase activity inside cells. Activation of PP1 can thus be a novel approach to study PP1 function and to counteract Ser/Thr kinase activity under pathologically increased kinase signaling.