Abstract
NF-β °B is a major gene regulator in immune responses, and ribosomal protein S3 (RPS3) is an NF-β °B subunit that directs specific gene transcription. However, it is unknown how nuclear translocation of RPS3 is regulated. Here we report that phosphorylation of RPS3 Ser209 by the kinase IKKβ 2 was crucial for nuclear localization of RPS3 in response to activating stimuli. Moreover, virulence protein NleH1 of the foodborne pathogen Escherichia coli strain O157:H7 specifically inhibited phosphorylation of RPS3 Ser209 and blocked RPS3 function, thereby promoting bacterial colonization and diarrhea but resulting in less mortality in a gnotobiotic piglet-infection model. Thus, the IKKβ 2-dependent modification of a specific amino acid in RPS3 promoted specific NF-κB functions that underlie the molecular pathogenetic mechanisms of E. coli O157:H7.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 335-344 |
| Number of pages | 10 |
| Journal | Nature Immunology |
| Volume | 12 |
| Issue number | 4 |
| DOIs | |
| State | Published - Apr 2011 |
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ASJC Scopus subject areas
- Immunology
Cite this
IKKβ 2 phosphorylation regulates RPS3 nuclear translocation and NF-κ B function during infection with Escherichia coli strain O157 : H7. / Wan, Fengyi; Weaver, Amanda; Gao, Xiaofei; Bern, Michael; Hardwidge, Philip R.; Lenardo, Michael J.
In: Nature Immunology, Vol. 12, No. 4, 04.2011, p. 335-344.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - IKKβ 2 phosphorylation regulates RPS3 nuclear translocation and NF-κ B function during infection with Escherichia coli strain O157
T2 - H7
AU - Wan, Fengyi
AU - Weaver, Amanda
AU - Gao, Xiaofei
AU - Bern, Michael
AU - Hardwidge, Philip R.
AU - Lenardo, Michael J.
PY - 2011/4
Y1 - 2011/4
N2 - NF-β °B is a major gene regulator in immune responses, and ribosomal protein S3 (RPS3) is an NF-β °B subunit that directs specific gene transcription. However, it is unknown how nuclear translocation of RPS3 is regulated. Here we report that phosphorylation of RPS3 Ser209 by the kinase IKKβ 2 was crucial for nuclear localization of RPS3 in response to activating stimuli. Moreover, virulence protein NleH1 of the foodborne pathogen Escherichia coli strain O157:H7 specifically inhibited phosphorylation of RPS3 Ser209 and blocked RPS3 function, thereby promoting bacterial colonization and diarrhea but resulting in less mortality in a gnotobiotic piglet-infection model. Thus, the IKKβ 2-dependent modification of a specific amino acid in RPS3 promoted specific NF-κB functions that underlie the molecular pathogenetic mechanisms of E. coli O157:H7.
AB - NF-β °B is a major gene regulator in immune responses, and ribosomal protein S3 (RPS3) is an NF-β °B subunit that directs specific gene transcription. However, it is unknown how nuclear translocation of RPS3 is regulated. Here we report that phosphorylation of RPS3 Ser209 by the kinase IKKβ 2 was crucial for nuclear localization of RPS3 in response to activating stimuli. Moreover, virulence protein NleH1 of the foodborne pathogen Escherichia coli strain O157:H7 specifically inhibited phosphorylation of RPS3 Ser209 and blocked RPS3 function, thereby promoting bacterial colonization and diarrhea but resulting in less mortality in a gnotobiotic piglet-infection model. Thus, the IKKβ 2-dependent modification of a specific amino acid in RPS3 promoted specific NF-κB functions that underlie the molecular pathogenetic mechanisms of E. coli O157:H7.
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U2 - 10.1038/ni.2007
DO - 10.1038/ni.2007
M3 - Article
C2 - 21399639
AN - SCOPUS:79952994560
VL - 12
SP - 335
EP - 344
JO - Nature Immunology
JF - Nature Immunology
SN - 1529-2908
IS - 4
ER -