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Small GTPases - Ras and Rho

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
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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.
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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key...

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Related Experiment Video

Updated: Feb 10, 2026

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

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Activation of Rho Family GTPases by Small Molecules.

Charuta C Palsuledesai, Zurab Surviladze, Anna Waller

¹Institute of Chemistry , Romanian Academy , Timisoara , Romania.

ACS Chemical Biology

|May 11, 2018

Summary

Researchers discovered small molecules that activate Ras and Ras-related small GTPases, crucial for cell functions. These compounds stabilize the GTP-bound state, impacting cell morphology and offering potential for drug discovery.

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Ras and Ras-related small GTPases regulate critical cellular processes including growth, survival, motility, and differentiation.
These GTPases are significant targets for understanding disease mechanisms and developing novel therapeutics.

Purpose of the Study:

To identify and characterize small molecule agonists targeting Rho, Rab, and Ras family GTPases.
To investigate the mechanism of action and cellular effects of identified GTPase activators.

Main Methods:

High-throughput screening of 200,000 compounds using flow cytometry.
Virtual screening to predict additional potential activators.
Dose-response assays, in vitro biochemical assays, and cell-based assays to confirm activity and mechanism.

Main Results:

Identified 43 small molecule agonists targeting multiple GTPase subfamilies, categorized into three chemical families.
Lead compounds demonstrated pan-activation of GTPases, while others showed partial selectivity for Ras and Rab proteins.
Compounds stabilized the GTP-bound state of GTPases, prolonging effector interactions and altering cytoskeletal rearrangements in cell-based assays.

Conclusions:

Small molecules targeting Ras and Ras-related GTPases were identified and characterized.
The compounds activate GTPases by stabilizing their active conformation, independent of canonical guanine nucleotide exchange factors or GAPs.
These activators modulate cellular functions, including cytoskeletal organization, highlighting their therapeutic potential.