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GTPases and their Regulation

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒ small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...

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Related Experiment Video

Updated: Dec 21, 2025

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

Multiplexed GTPase and GEF biosensor imaging enables network connectivity analysis.

Daniel J Marston¹, Marco Vilela², Jaewon Huh²

¹Department of Pharmacology, UNC Chapel Hill, Chapel Hill, NC, USA.

Nature Chemical Biology

|May 20, 2020

Summary

This summary is machine-generated.

Researchers developed new biosensors to track guanine exchange factor (GEF) activity in real-time. This allows precise mapping of how specific GEFs, like Asef, regulate cell movement by controlling Rho GTPases.

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Area of Science:

Cell signaling
Molecular biology
Biophysics

Background:

Fluorescent biosensors enable spatial and temporal mapping of signaling molecule activation.
Quantifying the contribution of individual activation events to cell behavior remains challenging.

Purpose of the Study:

To develop novel fluorescence resonance energy transfer (FRET) biosensors for guanine exchange factors (GEFs).
To quantify the contribution of individual GEFs to Rho GTPase activation and cell movement.
To elucidate real-time signal transduction network connectivity.

Main Methods:

Engineered FRET biosensors by inserting fluorescent protein pairs into a conserved GEF structural hinge.
Simultaneously imaged GEF biosensors and Rho GTPase biosensors within the same cells.
Applied partial correlation analysis to dissect GEF-GTPase regulatory relationships.

Main Results:

Successfully generated and utilized GEF FRET biosensors.
Identified specific spatiotemporal regulation of Cdc42 and Rac1 by the GEF Asef during cell protrusion.
Demonstrated Asef's role in controlling cell edge dynamics.

Conclusions:

This approach provides a powerful method for dissecting complex signal transduction networks in real-time.
Enables quantitative analysis of GEF activity and its downstream effects on cell behavior.
Offers new insights into the molecular mechanisms governing cell movement and dynamics.