Pellino3 ubiquitinates RIP2 and mediates Nod2-induced signaling and protective effects in colitis

Typeset version

 

TY  - JOUR
  - Yang, S,Wang, BW,Humphries, F,Jackson, R,Healy, ME,Bergin, R,Aviello, G,Hall, B,McNamara, D,Darby, T,Quinlan, A,Shanahan, F,Melgar, S,Fallon, PG,Moynagh, PN
  - 2013
  - September
  - Nature immunology
  - Pellino3 ubiquitinates RIP2 and mediates Nod2-induced signaling and protective effects in colitis
  - Validated
  - Altmetric: 3 ()
  - NF-KAPPA-B TOLL-LIKE RECEPTOR MURAMYL DIPEPTIDE CROHNS-DISEASE INTESTINAL INFLAMMATION POLYUBIQUITIN CHAINS CYTOKINE PRODUCTION CARD15 MUTATIONS LIGASE PELLINO BLAU-SYNDROME
  - 14
  - 927
  - Mutations that result in loss of function of Nod2, an intracellular receptor for bacterial peptidoglycan, are associated with Crohn's disease. Here we found that the E3 ubiquitin ligase Pellino3 was an important mediator in the Nod2 signaling pathway. Pellino3-deficient mice had less induction of cytokines after engagement of Nod2 and had exacerbated disease in various experimental models of colitis. Furthermore, expression of Pellino3 was lower in the colons of patients with Crohn's disease. Pellino3 directly bound to the kinase RIP2 and catalyzed its ubiquitination. Loss of Pellino3 led to attenuation of Nod2-induced ubiquitination of RIP2 and less activation of the transcription factor NF-kappa B and mitogen-activated protein kinases (MAPKs). Our findings identify RIP2 as a substrate for Pellino3 and Pellino3 as an important mediator in the Nod2 pathway and regulator of intestinal inflammation.
  - 10.1038/ni.2669
DA  - 2013/09
ER  - 
@article{V243945068,
   = {Yang,  S and Wang,  BW and Humphries,  F and Jackson,  R and Healy,  ME and Bergin,  R and Aviello,  G and Hall,  B and McNamara,  D and Darby,  T and Quinlan,  A and Shanahan,  F and Melgar,  S and Fallon,  PG and Moynagh,  PN },
   = {2013},
   = {September},
   = {Nature immunology},
   = {Pellino3 ubiquitinates RIP2 and mediates Nod2-induced signaling and protective effects in colitis},
   = {Validated},
   = {Altmetric: 3 ()},
   = {NF-KAPPA-B TOLL-LIKE RECEPTOR MURAMYL DIPEPTIDE CROHNS-DISEASE INTESTINAL INFLAMMATION POLYUBIQUITIN CHAINS CYTOKINE PRODUCTION CARD15 MUTATIONS LIGASE PELLINO BLAU-SYNDROME},
   = {14},
  pages = {927},
   = {{Mutations that result in loss of function of Nod2, an intracellular receptor for bacterial peptidoglycan, are associated with Crohn's disease. Here we found that the E3 ubiquitin ligase Pellino3 was an important mediator in the Nod2 signaling pathway. Pellino3-deficient mice had less induction of cytokines after engagement of Nod2 and had exacerbated disease in various experimental models of colitis. Furthermore, expression of Pellino3 was lower in the colons of patients with Crohn's disease. Pellino3 directly bound to the kinase RIP2 and catalyzed its ubiquitination. Loss of Pellino3 led to attenuation of Nod2-induced ubiquitination of RIP2 and less activation of the transcription factor NF-kappa B and mitogen-activated protein kinases (MAPKs). Our findings identify RIP2 as a substrate for Pellino3 and Pellino3 as an important mediator in the Nod2 pathway and regulator of intestinal inflammation.}},
   = {10.1038/ni.2669},
  source = {IRIS}
}
AUTHORSYang, S,Wang, BW,Humphries, F,Jackson, R,Healy, ME,Bergin, R,Aviello, G,Hall, B,McNamara, D,Darby, T,Quinlan, A,Shanahan, F,Melgar, S,Fallon, PG,Moynagh, PN
YEAR2013
MONTHSeptember
JOURNAL_CODENature immunology
TITLEPellino3 ubiquitinates RIP2 and mediates Nod2-induced signaling and protective effects in colitis
STATUSValidated
TIMES_CITEDAltmetric: 3 ()
SEARCH_KEYWORDNF-KAPPA-B TOLL-LIKE RECEPTOR MURAMYL DIPEPTIDE CROHNS-DISEASE INTESTINAL INFLAMMATION POLYUBIQUITIN CHAINS CYTOKINE PRODUCTION CARD15 MUTATIONS LIGASE PELLINO BLAU-SYNDROME
VOLUME14
ISSUE
START_PAGE927
END_PAGE
ABSTRACTMutations that result in loss of function of Nod2, an intracellular receptor for bacterial peptidoglycan, are associated with Crohn's disease. Here we found that the E3 ubiquitin ligase Pellino3 was an important mediator in the Nod2 signaling pathway. Pellino3-deficient mice had less induction of cytokines after engagement of Nod2 and had exacerbated disease in various experimental models of colitis. Furthermore, expression of Pellino3 was lower in the colons of patients with Crohn's disease. Pellino3 directly bound to the kinase RIP2 and catalyzed its ubiquitination. Loss of Pellino3 led to attenuation of Nod2-induced ubiquitination of RIP2 and less activation of the transcription factor NF-kappa B and mitogen-activated protein kinases (MAPKs). Our findings identify RIP2 as a substrate for Pellino3 and Pellino3 as an important mediator in the Nod2 pathway and regulator of intestinal inflammation.
PUBLISHER_LOCATION
ISBN_ISSN
EDITION
URL
DOI_LINK10.1038/ni.2669
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