Activity modulation of the bacterial Rho GAP YopE: an inspiration for the investigation of mammalian Rho GAPs.
The Yersinia enterocolitica Rho GTPase Activating Protein (Rho GAP) YopE belongs to a group of bacterial virulence factors that is translocated into infected target cells by a type three secretion system. Structurally and biochemically YopE resembles eukaryotic Rho GAPs which control various cellular functions by modulating the activity of Rho GTP binding proteins. Here we summarise the published information on cellular effects, Rho protein substrates, compartmentalisation and turnover of YopE. A fascinating picture evolves of how this virulence factor integrates in host cellular regulatory mechanisms to fine tune bacterial pathogenicity.
Institute of Medical Microbiology, Virology and Hygiene, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, Germany. m.aepfelbacher@uke.de
Martin
M
Aepfelbacher
Bernhard
B
Roppenser
Moritz
M
Hentschke
Klaus
K
Ruckdeschel
D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D001427:Bacterial Toxins / Q000378:metabolism; D020690:GTPase-Activating Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D054875:Ubiquitination; D015008:Yersinia enterocolitica / Q000378:metabolism*; D020741:rho GTP-Binding Proteins / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D001427:Bacterial Toxins; D020690:GTPase-Activating Proteins; C085379:rho GTPase-activating protein; C063239:yopE protein, Yersinia; D020741:rho GTP-Binding Proteins