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Direct modifications of Rho proteins: deconstructing GTPase regulation
Author(s) -
Visvikis Orane,
Maddugoda Madhavi P.,
Lemichez Emmanuel
Publication year - 2010
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1042/bc20090151
Subject(s) - biology , gtpase , microbiology and biotechnology , deamidation , actin , actin cytoskeleton , phosphorylation , gtpase activating protein , cytoskeleton , adenylylation , biochemistry , signal transduction , cell , g protein , gene , enzyme , biosynthesis
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.