General Information:

Id: 2,398
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
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: 21363

gene/protein

RALA

is localized in

cellular component

host cell plasma membrane

Drugbank entries Show/Hide entries for RALA
Comment In previous studies it was found that Ras, which is plasma membrane associated, was more efficiently modified by ExoS in vivo than Rap1a, which is localized to the endocytic and lysosomal vesicles.
Formal Description
Interaction-ID: 21364

gene/protein

HRAS

is localized in

cellular component

host cell plasma membrane

Drugbank entries Show/Hide entries for HRAS
Comment Rac and Cdc42, which normally localize to the cytosol, were found to re-localize to the membrane fraction when exposed to ExoS producing bacteria, where modification was detected. In direct comparisons of Cdc42 and Rac1 in the P100 fraction, a much smaller portion of Cdc42 was found to be localized to the membrane and modified.
Formal Description
Interaction-ID: 21365

gene/protein

RAC1

is localized in

cellular component

host cell plasma membrane

in response to ExoS
Drugbank entries Show/Hide entries for RAC1
Comment Rac and Cdc42, which normally localize to the cytosol, were found to re-localize to the membrane fraction when exposed to ExoS producing bacteria, where modification was detected. In direct comparisons of Cdc42 and Rac1 in the P100 fraction, a much smaller portion of Cdc42 was found to be localized to the membrane and modified.
Formal Description
Interaction-ID: 21366

gene/protein

CDC42

is localized in

cellular component

host cell plasma membrane

in response to ExoS
Drugbank entries Show/Hide entries for CDC42