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Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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Split-Small GTPase Reassembly as a Method to Control Cellular Signaling with User-Defined Inputs.

Yuchen He¹, Benjamin M Faulkner¹, Rachel S Weatherford¹

¹Department of Chemistry, University of Virginia, Charlottesville, Virginia 22904, United States.

ACS Chemical Biology

|August 26, 2025

Summary

This summary is machine-generated.

Researchers developed a plug-and-play method to control small guanine triphosphate (GTP)ase activity using chemical inducers of dimerization (CID). This system allows precise temporal control over cellular signaling pathways.

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Area of Science:

Molecular Biology
Cell Signaling
Biochemistry

Background:

Small GTPases are crucial signaling enzymes regulating cell functions like migration and proliferation.
Current methods lack direct, temporal control over small GTPase activity, hindering research.
Understanding small GTPase roles requires precise tools for manipulating their signaling.

Purpose of the Study:

To develop a plug-and-play methodology for direct, temporal control of small GTPase activity.
To enable user-defined inputs for precise regulation of cellular signaling pathways.
To create a customizable platform for studying small GTPase functions.

Main Methods:

Pairing split-small GTPases with chemical inducers of dimerization (CID) systems.
Utilizing the modularity of split-small GTPase systems for CID selection.
Implementing the system in living cells to control specific signaling pathways.

Main Results:

Demonstrated a plug-and-play method for direct temporal control of small GTPase signaling.
Showcased consistent pathway activation using various CID systems.
Successfully controlled MAPK signaling, filopodia formation, and cell retraction.

Conclusions:

Split-small GTPase systems offer a customizable platform for temporal control of cellular signaling.
This method allows precise manipulation of small GTPase activity with user-defined inputs.
Provides a valuable tool for dissecting the roles of small GTPases in diverse cellular processes.