General Information:

Id: 2,398 (click here to show other Interactions for entry)
Diseases: Pseudomonas aeruginosa diseases
pathogen-host system
Pseudomonas aeruginosa/mammalia
BTO:0000182 HT-29 cell, infected with P. aeruginosa strain 388
article
Reference: Fraylick JE et al.(2002) Eukaryotic cell determination of ExoS ADP-ribosyltransferase substrate specificity. Biochem. Biophys. Res. Commun. 291: 91-100 [PMID: 11829467]

Interaction Information:

Comment Two-dimensional electrophoresis comparisons of substrate modifications by ExoS in vitro to that following bacterial translocation into HT-29 epithelial cells identified Ras, Ral, and Rab proteins and Rac1 as in vivo substrates of ExoS ADPRT activity.
Formal Description
Interaction-ID: 21328

gene/protein

exoS

affects_activity of

gene/protein

HRAS

by ADP-ribosylation in vitro and in vivo
Drugbank entries Show/Hide entries for HRAS
Comment Two-dimensional electrophoresis comparisons of substrate modifications by ExoS in vitro to that following bacterial translocation into HT-29 epithelial cells identified Ras, Ral, and Rab proteins and Rac1 as in vivo substrates of ExoS ADPRT activity. The two modified forms of Rab5 detected by SDS-PAGE were consistent with two sites of ADP-ribosylation by ExoS.
Formal Description
Interaction-ID: 21351

gene/protein

exoS

affects_activity of

gene/protein

RAB5

by ADP-ribosylation in vitro and in vivo
Comment Two-dimensional electrophoresis comparisons of substrate modifications by ExoS in vitro to that following bacterial translocation into HT-29 epithelial cells identified Ras, Ral, and Rab proteins and Rac1 as in vivo substrates of ExoS ADPRT activity.
Formal Description
Interaction-ID: 21352

gene/protein

exoS

affects_activity of

gene/protein

RAB8

by ADP-ribosylation in vitro and in vivo
Comment Two-dimensional electrophoresis comparisons of substrate modifications by ExoS in vitro to that following bacterial translocation into HT-29 epithelial cells identified Ras, Ral, and Rab proteins and Rac1 as in vivo substrates of ExoS ADPRT activity.
Formal Description
Interaction-ID: 21353

gene/protein

exoS

affects_activity of

gene/protein

RAB7

by ADP-ribosylation in vitro and in vivo
Comment Two-dimensional electrophoresis comparisons of substrate modifications by ExoS in vitro to that following bacterial translocation into HT-29 epithelial cells identified Ras, Ral, and Rab proteins and Rac1 as in vivo substrates of ExoS ADPRT activity.
Formal Description
Interaction-ID: 21354

gene/protein

exoS

affects_activity of

gene/protein

RAB11

by ADP-ribosylation in vitro and in vivo
Comment Analyses of the Rho family of LMMG-proteins (low-molecular-mass G-proteins) for possible ADP-ribosylation identified a single shift in the mass of Rac1 following bacterial translocation of ExoS, but no alteration in the mobility of Cdc42 or RhoA, B, C was detected.
Formal Description
Interaction-ID: 21356

gene/protein

exoS

affects_activity of

gene/protein

RAC1

by ADP-ribosylation in vitro and in vivo
Drugbank entries Show/Hide entries for RAC1
Comment Analyses of the Rho family of LMMG-proteins (low-molecular-mass G-proteins) for possible ADP-ribosylation identified a single shift in the mass of Rac1 following bacterial translocation of ExoS, but no alteration in the mobility of Cdc42 or RhoA, B, C was detected.
Formal Description
Interaction-ID: 21357

gene/protein

exoS

NOT affects_activity of

gene/protein

CDC42

by ADP-ribosylation in vivo
Drugbank entries Show/Hide entries for CDC42
Comment Analyses of the Rho family of LMMG-proteins (low-molecular-mass G-proteins) for possible ADP-ribosylation identified a single shift in the mass of Rac1 following bacterial translocation of ExoS, but no alteration in the mobility of Cdc42 or RhoA, B, C was detected.
Formal Description
Interaction-ID: 21358

gene/protein

exoS

NOT affects_activity of

gene/protein

RHOA

by ADP-ribosylation in vivo
Drugbank entries Show/Hide entries for RHOA
Comment Analyses of the Rho family of LMMG-proteins (low-molecular-mass G-proteins) for possible ADP-ribosylation identified a single shift in the mass of Rac1 following bacterial translocation of ExoS, but no alteration in the mobility of Cdc42 or RhoA, B, C was detected.
Formal Description
Interaction-ID: 21359

gene/protein

exoS

NOT affects_activity of

gene/protein

RHOB

by ADP-ribosylation in vivo
Drugbank entries Show/Hide entries for RHOB
Comment Analyses of the Rho family of LMMG-proteins (low-molecular-mass G-proteins) for possible ADP-ribosylation identified a single shift in the mass of Rac1 following bacterial translocation of ExoS, but no alteration in the mobility of Cdc42 or RhoA, B, C was detected.
Formal Description
Interaction-ID: 21360

gene/protein

exoS

NOT affects_activity of

gene/protein

RHOC

by ADP-ribosylation in vivo
Comment In the Ras family, RalA, previously identified as an in vivo substrate of ExoS ADPRT activity (ADP-ribosyltransferase activity), preferentially localized to the membrane fraction, where it was efficiently modified.
Formal Description
Interaction-ID: 21361

gene/protein

exoS

affects_activity of

gene/protein

RALA

by ADP-ribosylation in vivo
Drugbank entries Show/Hide entries for RALA
Comment Exoenzyme S (ExoS) ADP-ribosylates multiple lowmolecular- mass G- (LMMG-) proteins.
Formal Description
Interaction-ID: 21362

gene/protein

exoS

increases_activity of

the most efficient substrate modification was consistently detected in the membrane fraction