Related Experiment Video

Updated: Aug 7, 2026

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
06:56

Development and Application of Rapamycin-regulated Tyrosine Phosphatases

Published on: September 6, 2024

Regulation of Rho proteins by phosphorylation in the cardiovascular system

Gervaise Loirand1, Christophe Guilluy, Pierre Pacaud

  • 1INSERM U533 Institut du Thorax, Université de Nantes, F-44000 Nantes, France. gervaise.loirand@univ-nantes.fr

Trends in Cardiovascular Medicine
|July 15, 2006
PubMed

Insights

Small G protein Rho signaling regulates cardiovascular functions. Phosphorylation of Rho proteins offers a new mechanism for controlling their actions, especially in the arterial wall.

Area of Science:

  • Cardiovascular Biology
  • Molecular Signaling
  • Cellular Regulation

Background:

  • Rho signaling pathways are crucial for cardiovascular functions.
  • Aberrant Rho protein activation contributes to hypertension and vascular diseases.
  • Rho protein regulation is complex, involving multiple signaling cascades.

Purpose of the Study:

  • To explore the role of Rho protein phosphorylation in cardiovascular regulation.
  • To elucidate the mechanisms controlling RhoA activity in vascular smooth muscle cells.
  • To understand the interplay between endothelial nitric oxide signaling and RhoA phosphorylation.

Main Methods:

  • Investigated Rho protein signaling pathways.
  • Analyzed the effects of phosphorylation on Rho protein function.
  • Examined the role of the nitric oxide/cGMP-dependent kinase pathway in regulating RhoA.

Main Results:

  • Rho protein phosphorylation represents a key regulatory mechanism for Rho signaling.
  • This phosphorylation is particularly significant in the arterial wall.
  • Endothelial nitric oxide/cGMP-dependent kinase signaling modulates RhoA activity in vascular smooth muscle cells.

Conclusions:

  • Phosphorylation provides an additional layer of control for Rho protein functions.
  • Targeting Rho phosphorylation may offer therapeutic strategies for cardiovascular disorders.
  • Endothelial-derived signals play a vital role in vascular smooth muscle RhoA regulation.

More Related Videos

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos12:35

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

Published on: April 14, 2023

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay13:51

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

Published on: November 11, 2018

Related Concept Videos

Small GTPases - Ras and Rho01:24

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:
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
Cell Polarization by Rho Proteins01:21

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,...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...