Optogenetic actuators—genetically encodable proteins that undergo light-induced changes in conformation—are useful tools for placing biochemical events under optical control but, at present, remain difficult to couple to biocatalysts without interfering with their native structures or activities. This study develops a minimally disruptive approach to control PTP1B—a phosphatase implicated in diabetes, obesity, and cancer—with light. The resulting photowitchable construct enables measurements of mechanical coupling between actuator and catalytic domains, permits detailed perturbational studies of allosteric communication in PTPs, and enables optical modulation of spatially distinct subpopulations of enzymes in living cells. The central findings illustrate a new approach for using photosensitive proteins to carry out detailed biophysical studies of enzyme activity and subcellular regulation.

Minimally disruptive optical control of protein tyrosine phosphatases

2019 Spring National Meeting

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.