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Rac Homologues and Compartmentalized Phosphatidylinositol 4, 5-Bisphosphate Act in a Common Pathway to Regulate Polar Pollen Tube Growth
Results indicate that Rac and PtdIns 4, 5-P2 act in a common pathway to control polar pollen tube growth and provide direct evidence for a function of Ptdins 4,5-P1 compartmentalization in the regulation of this process.
Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine
It is shown that CNF1 catalyses the deamidation of a glutamine residue at position 63 of Rho, turning it into glutamic acid, which inhibits both intrinsic GTP hydrolysis and that stimulated by its GTPase-activating protein (GAP).
Inactivation of AtRac1 by abscisic acid is essential for stomatal closure.
- E. Lemichez, Y. Wu, J. P. Sánchez, A. Mettouchi, J. Mathur, N. Chua
- Environmental ScienceGenes & development
- 15 July 2001
Observations indicate that AtRac1 inactivation is a limiting step in the ABA-signaling cascade leading to stomatal closure, and defines AtRAC1 as a central element for plant adaptation to drought.
CNF1 Exploits the Ubiquitin-Proteasome Machinery to Restrict Rho GTPase Activation for Bacterial Host Cell Invasion
Rho protein regulates tight junctions and perijunctional actin organization in polarized epithelia.
It is reported that rho regulates filamentous actin organization preferentially in the apical pole of polarized intestinal epithelial cells and, in so doing, influences the organization and permeability of the associated apical tight junctions.
The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation of active Rac1.
System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes.
Rho GTPase-activating bacterial toxins: from bacterial virulence regulation to eukaryotic cell biology.
A family of bacterial toxins that modulate their activity in eukaryotic cells by activating Rho GTPases and exploiting the ubiquitin/proteasome machineries is reviewed, found in human and animal pathogenic Gram-negative bacteria.
Activated Rac1, but not the tumorigenic variant Rac1b, is ubiquitinated on Lys 147 through a JNK‐regulated process
- Orane Visvikis, P. Lorès, L. Boyer, P. Chardin, E. Lemichez, G. Gacon
- BiologyThe FEBS journal
- 1 January 2008
Rac1b appears to be more stable than Rac1L61 with regard to the ubiquitin–proteasome system, and this may be of importance for the expression and tumorigenic capacity of Rac1b; and ubiquitination of activated Rac1 occurs through a JNK‐activated process, which may explain the defective ubiquitinations of Rac 1b.
Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation (*)
LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo, and is thus a powerful tool to inhibit Ras function in vivo.