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

5.6K
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:
5.6K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

12.1K
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...
12.1K
The Contractile Ring02:15

The Contractile Ring

7.4K
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...
7.4K
GTPases and their Regulation02:14

GTPases and their Regulation

10.2K
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,...
10.2K
GTPases and their Regulation02:14

GTPases and their Regulation

3.2K
3.2K
Cell Polarization by Rho Proteins01:21

Cell Polarization by Rho Proteins

4.0K
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,...
4.0K

You might also read

Related Articles

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

Sort by
Same author

Tissue mechanopathology of cancer.

Developmental cell·2026
Same author

Impact of BECLIN1 haploinsufficiency on goblet cell function and susceptibility to colitis.

Cell death & disease·2026
Same author

Sphingosine-1-phosphate cross-talks to Notch via a S1PR1-Dll4-MPDZ complex to regulate endothelial barrier function.

bioRxiv : the preprint server for biology·2026
Same author

Bridging scales for cellular communities.

The Journal of cell biology·2026
Same author

Synergistic targeting of eIF4A-mediated translation initiation and apoptosis in acute myeloid leukemia.

Blood neoplasia·2026
Same author

Multiscale mechanisms driving tissue rupture by invading cells.

Developmental cell·2026

Related Experiment Video

Updated: Mar 16, 2026

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

2.0K

Cycling Rho for tissue contraction.

Jessica L Teo1, Alpha S Yap2

  • 1Division of Cell Biology and Molecular Medicine, Institute for Molecular Bioscience, The University of Queensland, St. Lucia, Brisbane, Queensland, Australia 4072.

The Journal of Cell Biology
|August 24, 2016
PubMed
Summary
This summary is machine-generated.

Cyclic inactivation of RhoA GTPase by C-GAP is crucial for effective cell contractility. This process is essential for proper tissue morphogenesis, ensuring cells can effectively change shape.

More Related Videos

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

10.4K
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

9.7K

Related Experiment Videos

Last Updated: Mar 16, 2026

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

2.0K
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

10.4K
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

9.7K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • Cell contractility is vital for tissue morphogenesis.
  • RhoA GTPase is a key regulator of cell contractility.

Purpose of the Study:

  • To investigate the mechanism by which RhoA GTPase activity influences effective cell contractility.
  • To understand the role of C-GAP in regulating RhoA activity during tissue development.

Main Methods:

  • Utilized molecular biology techniques to study RhoA GTPase activity.
  • Investigated the interaction between RhoA and its antagonist, C-GAP.
  • Observed cellular contractility and tissue morphogenesis in relevant model systems.

Main Results:

  • Demonstrated that cyclic inactivation of RhoA GTPase is essential for effective contractility.
  • Identified C-GAP as the antagonist mediating this cyclic inactivation.
  • Linked this regulatory mechanism to successful tissue morphogenesis.

Conclusions:

  • Cyclic RhoA inactivation by C-GAP is a critical regulatory step for cell contractility.
  • This mechanism is fundamental for achieving proper tissue morphogenesis.