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Related Concept Videos

Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

3.9K
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:
3.9K
GTPases and their Regulation02:14

GTPases and their Regulation

8.3K
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,...
8.3K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

6.7K
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...
6.7K
Cell Polarization by Rho Proteins01:21

Cell Polarization by Rho Proteins

2.7K
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,...
2.7K
The Contractile Ring02:15

The Contractile Ring

6.3K
Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
6.3K
Rab Cascades01:25

Rab Cascades

2.6K
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.
2.6K

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Related Experiment Video

Updated: Jun 4, 2025

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

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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Structural Dynamics of Rho GTPases.

Yuan Lin1, Yi Zheng2

  • 1Division of Experimental Hematology and Cancer Biology, Cancer and Blood Diseases Institute, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, USA.

Journal of Molecular Biology
|December 21, 2024
PubMed
Summary

Rho GTPases are crucial signaling hubs. Understanding their structure and dynamics, especially cancer-associated mutations, is key to developing targeted therapies, similar to progress made with Ras proteins.

Keywords:
Rho GTPaseatomic structuresconformation dynamicsmolecular dynamicsoncogenic mutation

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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates
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Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates

Published on: March 31, 2012

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Related Experiment Videos

Last Updated: Jun 4, 2025

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

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

Published on: November 11, 2018

9.8K
Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

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Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates
11:28

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates

Published on: March 31, 2012

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Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Cancer Research

Background:

  • Rho family GTPases are key regulators of cellular processes, analogous to the well-studied Ras superfamily.
  • Recent discovery of cancer-related Rho GTPase mutations highlights their role in oncogenesis.
  • Understanding Rho GTPase structure and dynamics is crucial for cancer drug development.

Purpose of the Study:

  • To explore the structure-function relationship of Rho GTPases.
  • To investigate the role of Rho GTPase mutations in cancer.
  • To provide insights for developing novel cancer therapies targeting Rho GTPases.

Main Methods:

  • Structural biology techniques to analyze Rho GTPase conformation.
  • Biochemical assays to study Rho GTPase activity and signaling.
  • Bioinformatic analysis of cancer-related Rho GTPase mutations.

Main Results:

  • Elucidation of structural dynamics in Rho GTPase signaling.
  • Identification of key structural features contributing to oncogenic potential.
  • New insights into how Rho GTPase mutations drive cancer progression.

Conclusions:

  • Structural dynamics of Rho GTPases offer new therapeutic targets.
  • Targeting Rho GTPases holds promise for effective cancer treatment.
  • Further research into Rho GTPase structure-function is essential for advancing cancer therapy.