The Journal of Organic Chemistry · 2019 · 14 citations · 16 references
Life SciencesBiochemistryMolecular BiologyCell SignalingProtein BiochemistrySignal TransductionProtein Phosphatase SignalingProtein PhosphorylationPhosphatase Activation MechanismsPhosphatase Enzyme ActivityPhotophysical MechanismsProtein Binding Interface DesignProtein Phosphatase Catalysis
We describe here the development of a photoreleasable version of a protein phosphatase-1 (PP1)-disrupting peptide (PDP-Nal) that triggers protein phosphatase-1 activity. PDP-Nal is a 23 mer that binds to PP1 through several interactions. It was photocaged on a tyrosine residue, which required the exchange of phenylalanine in PDP-Nal to tyrosine in order to disrupt the most important binding interface. This PDP-caged can be light-controlled in live cells.
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Elucidating Human Phosphatase-Substrate Networks
Xun Li, Matthias Wilmanns, Janet M. Thornton et al. · Science Signaling · 2013 · 178 citations