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Updated: Jun 14, 2026

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
Published on: November 11, 2018
Direct modifications of Rho proteins: deconstructing GTPase regulation
Orane Visvikis1, Madhavi P Maddugoda, Emmanuel Lemichez
1INSERM, U895, Centre Méditerranéen de Médecine Moléculaire, C3M, Toxines Microbiennes dans la relation hôte pathogènes, Nice, F-06204 Cedex 3, France.
Abstract:
Small GTPases of the Rho protein family are master regulators of the actin cytoskeleton and are targeted by potent virulence factors of several pathogenic bacteria. Their dysfunctional regulation can lead to severe human pathologies. Both host and bacterial factors can activate or inactivate Rho proteins by direct post-translational modifications: such as deamidation and transglutamination for activation, or ADP-ribosylation, glucosylation, adenylylation and phosphorylation for inactivation. We review and compare these unconventional ways in which both host cells and bacterial pathogens regulate Rho proteins.
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