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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.
Three regulatory proteins control their activity:

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, also known...

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, also known...

Activation and Inactivation of G Proteins

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...

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Cell Polarization by Rho Proteins

Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...

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Related Experiment Video

Updated: May 24, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Exploiting effectors of Rac GTPase.

Hakryul Jo¹, Hongbo R Luo

¹Environmental Health Sciences, Yale University School of Public Health, 7th Floor, 1 Church Street, New Haven, CT 06510, USA. hakryul.jo@yale.edu

Chemistry & Biology

|February 28, 2012

Summary

Researchers developed a method to inhibit reactive oxygen species production by targeting the Rac GTPase and p67(phox) interaction. This specific inhibition avoids disrupting other crucial cellular processes mediated by Rac.

Area of Science:

Molecular Biology
Cell Signaling
Biochemistry

Background:

Signaling pathways offer potential therapeutic targets.
Rac GTPase is involved in various cellular processes, including reactive oxygen species (ROS) production.
Specificity in targeting signaling pathways is crucial to avoid off-target effects.

Purpose of the Study:

To develop a method for specifically inhibiting ROS production.
To exploit the interaction between Rac GTPase and its effector p67(phox) for targeted inhibition.
To ensure that other Rac-mediated cellular functions remain unperturbed.

Main Methods:

Investigating the interactive interface between Rac GTPase and p67(phox).
Developing molecular tools to modulate this specific interaction.

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Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

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

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Last Updated: May 24, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

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

Assessing the impact on ROS production and other Rac-dependent cellular activities.

Main Results:

Successfully identified and exploited the Rac GTPase-p67(phox) interface.
Demonstrated specific inhibition of ROS production.
Confirmed that other Rac-mediated cellular processes were not significantly affected.

Conclusions:

Targeting the Rac GTPase-p67(phox) interaction provides a specific strategy for inhibiting ROS production.
This approach allows for selective modulation of cellular signaling without broad disruption.
Offers a potential therapeutic avenue for conditions involving excessive ROS production.