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Updated: Jan 1, 2026

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases
Published on: September 6, 2024
Development of a Photoactivatable Protein Phosphatase-1-Disrupting Peptide
Malgorzata Trebacz1,2,3, Yansong Wang3, Leslie Makotta3
1Faculty of Biology, Institute of Biology III , University of Freiburg , Schänzlestraße 18 , 79104 Freiburg , Germany.
Abstract:
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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