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Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

Published on: July 17, 2020

Engineering SHP2 Phosphatase for Optical Control.

Amy Ryan¹, Chasity P Janosko¹, Taylor M Courtney¹

¹Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.

|November 8, 2022

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Researchers developed novel optical methods to control protein tyrosine phosphatase SHP2. These techniques enable precise light-activated regulation of phosphatase activity and binding interactions, advancing cell signaling research.

Area of Science:

Biochemistry
Molecular Biology
Cell Signaling

Background:

Signal transduction pathways regulate vital cellular functions like proliferation and apoptosis via phosphorylation.
Protein kinases and phosphatases mediate these phosphorylation events, with post-translational modifications impacting pathway activity.
Dissecting complex signaling networks, especially the subtle regulation by phosphatases, presents a significant challenge.

Purpose of the Study:

To develop innovative methods for the optical control of SHP2 (SH2 domain-containing protein tyrosine phosphatase-2).
To enable light-activated modulation of phosphatase catalytic activity and protein binding interactions.
To provide generalizable tools for studying other PTP and SH2 domain-containing proteins.

Main Methods:

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Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

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Site-specific incorporation of caged tyrosine for light-controlled activation of SHP2 catalytic activity.
Site-specific incorporation of caged lysine within an allosteric pocket to control SHP2 binding partner interactions.
Utilizing optical methods for precise temporal and spatial control over phosphatase function.

Main Results:

Demonstrated successful optical control over SHP2's catalytic function via caged tyrosine.
Showcased light-induced regulation of SHP2 binding partner interactions using caged lysine.
Established the generalizability of these methods to other PTP and SH2 domain proteins.

Conclusions:

Developed two complementary optical methods for precise control of SHP2.
These techniques offer new avenues for dissecting complex cell signaling mechanisms.
The methods are broadly applicable to a range of phosphatases and SH2 domain proteins.