Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

4.0K
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:
4.0K
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
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

7.2K
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...
7.2K
Rab Proteins01:14

Rab Proteins

3.9K
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
3.9K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.8K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
5.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.9K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The structural basis of RanGAP1 regulation and catalysis in nuclear transport.

bioRxiv : the preprint server for biology·2026
Same author

ERK autoinhibition mechanism informs a drug combination strategy.

Protein science : a publication of the Protein Society·2026
Same author

How Functional Variants Reconfigure the Rac2 Conformational Landscape.

bioRxiv : the preprint server for biology·2026
Same author

Energy landscapes in molecular biology: History, principles, and perspectives.

Quarterly reviews of biophysics·2026
Same author

Cyclin-E/A/CDK1/2 Kinetic Landscapes Drive Cell Cycle Phase-Specific Progression and Guide Cyclin-E Degradation Strategy.

Journal of chemical information and modeling·2026
Same author

Oncogenic PI3Kα variants reveal graded conformational spectrum with mutation-specific cryptic pockets.

Communications chemistry·2026

Related Experiment Video

Updated: Jul 5, 2025

RhoC GTPase Activation Assay
09:58

RhoC GTPase Activation Assay

Published on: August 22, 2010

12.5K

Allosteric Activation of RhoA Complexed with p115-RhoGEF Deciphered by Conformational Dynamics.

Nurit Haspel1, Hyunbum Jang2, Ruth Nussinov2,3

  • 1Department of Computer Science, University of Massachusetts Boston, Boston, Massachusetts 02125, United States.

Journal of Chemical Information and Modeling
|January 12, 2024
PubMed
Summary

Ras homologue family member A (RhoA) activation by p115-RhoGEF involves structural changes. Active RhoA-GTP interacts with the PH domain, facilitating its release from the DH domain for downstream signaling.

More Related Videos

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

16.6K
Author Spotlight: Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos
12:35

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

Published on: April 14, 2023

1.4K

Related Experiment Videos

Last Updated: Jul 5, 2025

RhoC GTPase Activation Assay
09:58

RhoC GTPase Activation Assay

Published on: August 22, 2010

12.5K
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

16.6K
Author Spotlight: Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos
12:35

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

Published on: April 14, 2023

1.4K

Area of Science:

  • Molecular biology
  • Biochemistry
  • Structural biology

Background:

  • Ras homologue family member A (RhoA) is a key regulator in the Rho family, a Ras superfamily subgroup.
  • RhoA activation is mediated by guanine nucleotide exchange factors (GEFs), such as p115-RhoGEF.

Purpose of the Study:

  • To elucidate the structural mechanism of RhoA activation by p115-RhoGEF.
  • To investigate the roles of RhoA-GDP and RhoA-GTP interactions with p115-RhoGEF domains.

Main Methods:

  • Molecular dynamics (MD) simulations
  • Essential dynamics analysis
  • Structural analysis of RhoA-GDP/GTP bound to p115-RhoGEF

Main Results:

  • Inactive RhoA-GDP binds the DH domain via its Switch I region.
  • Active RhoA-GTP exhibits increased interactions with the PH domain of p115-RhoGEF.
  • Allosteric communication pathways involved in RhoA activation were identified.

Conclusions:

  • RhoA-GTP interaction with the PH domain promotes its release from the DH domain post-activation.
  • This release mechanism makes activated RhoA available to downstream effectors.
  • Structural insights into RhoA activation and allosteric regulation within the Rho superfamily were provided.