title: Bacterial FIC Proteins AMP Up Infection.
abstract: Proteins containing FIC (filamentation induced by cyclic adenosine monophosphate) domains are found in both prokaryotic and eukaryotic organisms, but their function has remained elusive. Recent studies indicate that bacterial FIC domain-containing proteins disrupt host cell processes after being delivered into eukaryotic host cells: The Vibrio parahaemolyticus VopS protein interferes with Rho guanine triphosphatase (GTPase) function, and the Legionella pneumophila AnkX protein disrupts the microtubule-dependent transport of vesicles. Analysis of the VopS protein revealed that the FIC domain covalently modifies Rac by transferring adenosine 5'-monophosphate (AMP) to a threonine residue in the switch 1 region of the protein. Thus, FIC domain-mediated AMPylation is involved in the posttranslational regulation of protein function, and this activity has been subverted by microbial pathogens to modulate cellular functions during infection.
authors.affiliation: Yale University, New Haven, CT 06536, USA. craig.roy@yale.edu
authors.forename: Craig R
authors.initials: CR
authors.lastname: Roy
authors.forename: Shaeri
authors.initials: S
authors.lastname: Mukherjee
mesh_terms: D000249:Adenosine Monophosphate / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D007239:Infections / Q000503:physiopathology*; D016952:Legionella pneumophila / Q000737:chemistry; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000235:genetics / Q000502:physiology*; D033921:Vesicular Transport Proteins / Q000378:metabolism; D014736:Vibrio parahaemolyticus / Q000737:chemistry; D020744:rac GTP-Binding Proteins / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; D033921:Vesicular Transport Proteins; C482598:fic protein, E coli; D000249:Adenosine Monophosphate; D020744:rac GTP-Binding Proteins