General Information:

Id: 3,862 (click here to show other Interactions for entry)
Diseases: Pseudomonas aeruginosa diseases
pathogen-host system
Pseudomonas aeruginosa/mammalia
HeLa cells, infected with P. aeruginisa strain (GESPA 1999 collection)
article
Reference: Gendrin C et al.(2012) Structural basis of cytotoxicity mediated by the type III secretion toxin ExoU from Pseudomonas aeruginosa PLoS Pathog. 8 [PMID: 22496657]

Interaction Information:

Comment To analyse the multi-faceted behavior of ExoU, the authors solved its crystal structure, which was achieved in the presence of its chaperone, SpcU. ExoU forms a 1:1 complex with SpcU, and folds into three distinct domains, which fulfill catalytic, bridging, and membrane-binding functions.
Formal Description
Interaction-ID: 38807

gene/protein

spcU

increases_folding of

gene/protein

exoU

as shown in a crystal structure
Comment To analyse the multi-faceted behavior of ExoU, the authors solved its crystal structure, which was achieved in the presence of its chaperone, SpcU. ExoU forms a 1:1 complex with SpcU, and folds into three distinct domains, which fulfill catalytic, bridging, and membrane-binding functions.
Formal Description
Interaction-ID: 38811

gene/protein

spcU

interacts (colocalizes) with

gene/protein

exoU

as shown in a crystal structure
Comment In protein-lipid overlay assays it has been demonstrated that ExoU strongly interacts with PI(4,5)P2 (phosphatidylinositol (4,5) di-phosphate), a negatively-charged polyvalent phospholipid that is abundant in the cytosolic leaflet of the PM (plasma membrane).
Formal Description
Interaction-ID: 38813

gene/protein

exoU

interacts (colocalizes) with

Comment The non-catalytic mutant ExoU-S142A also displays a strong affinity for PI(4,5)P2, but this interaction is completely abolished in the case of a mutant lacking residues 679-683, which suggests a direct role of PI(4,5)P2 interaction for ExoU PM (plasma membrane) localization. These results thus provide a molecular explanation for ExoU's PM targeting, which constitutes the toxin's premier localization upon T3SS translocation.
Formal Description
Interaction-ID: 38816

gene/protein

exoU

is localized in

cellular component

host cell plasma membrane

Comment Ubiquitinated ExoU is targeted to endosomes. Ub-ExoU-S142A (catalytically-inactive mutant) did not co-localize with endoplasmic reticulum nor with Golgi markers, but was targeted to acidic organelles, as evidenced by its co-localization with the early endosome marker EEA1 and with lysotracker-stained compartments.
Formal Description
Interaction-ID: 38818

gene/protein

exoU

is localized in

cellular component

early endosome

the ubiquitinated form of ExoU
Comment ExoU's co-localization with endosomes is directly dependent on its ubiquitination of Lys178.
Formal Description
Interaction-ID: 38820

gene/protein

UBB

interacts (colocalizes) with

gene/protein

exoU

targeting ExoU to endosomal compartments
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