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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:

Cell Polarization by Rho Proteins

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,...

Activation and Inactivation of G Proteins

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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...

GTPases and their Regulation

GTPases and their Regulation

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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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.

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Related Experiment Video

Updated: Jan 17, 2026

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

A Modular Platform for the Optogenetic Control of Small GTPase Activity in Living Cells Reveals Long-Range RhoA

Benjamin Faulkner¹, Yuchen He¹, Daniel Sitrin¹

¹Department of Chemistry, University of Virginia, Charlottesville, VA 22904, USA.

Biorxiv : the Preprint Server for Biology

|September 15, 2025

Summary

Researchers developed spLIT-small GTPases, a novel optogenetic tool for precise spatial control of small GTPase activity. This platform enables new insights into cell signaling, cytoskeletal dynamics, and cell migration.

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Last Updated: Jan 17, 2026

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

Author Spotlight: Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Author Spotlight: Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Small GTPases regulate crucial cellular functions like migration.
Precise spatial control of GTPase activity is vital for cellular signaling.
Existing methods lack generalizability for subcellular control of GTPase activity.

Purpose of the Study:

To introduce a novel optogenetic platform for spatial control of small GTPase activity.
To enable precise, subcellular regulation of GTPase signaling in living cells.
To investigate spatially defined aspects of small GTPase signaling.

Main Methods:

Development of a modular optogenetic platform, spLIT-small GTPases.
Application of the platform to control specific GTPases (Cdc42, Rac1, RhoA).
Observation of cellular responses using microscopy and live-cell imaging.

Main Results:

Spatially precise control of cytoskeletal dynamics was achieved (e.g., filopodia formation with spLIT-Cdc42).
Directed cell migration was controlled using spLIT-Rac1.
A spLIT-RhoA system revealed long-range signaling and membrane retraction in HeLa cells.

Conclusions:

spLIT-small GTPases is a versatile tool for direct, spatial control of small GTPase signaling.
The platform facilitates the discovery of spatially defined signaling mechanisms.
Optogenetic control offers new avenues for studying cellular signaling pathways.