GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells

Nicolas Barnich, Tadakazu Hisamatsu, Jose E. Aguirre, Ramnik Xavier, Hans Christian Reinecker, Daniel K. Podolsky

Research output: Contribution to journalArticle

114 Citations (Scopus)

Abstract

Nucleotide oligomerization domain 2 (NOD2) functions as a mammalian cytosolic pathogen recognition molecule, and variants have been associated with risk for Crohn disease. We recently demonstrated that NOD2 functions as an anti-bacterial factor limiting survival of intracellular invasive bacteria. To gain further insight into the mechanism of NOD2 activation and signal transduction, we performed yeast two-hybrid screening. We demonstrate that GRIM-19, a protein with homology to the NADPH dehydrogenase complex, interacts with endogenous NOD2 in HT29 cells. GRIM-19 is required for NF-κB activation following NOD2-mediated recognition of bacterial muramyl dipeptide. GRIM-19 also controls pathogen invasion of intestinal epithelial cells. GRIM-19 expression is decreased in inflamed mucosa of patients with inflammatory bowel diseases. GRIM-19 may be a key component in NOD2-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes.

Original languageEnglish
Pages (from-to)19021-19026
Number of pages6
JournalJournal of Biological Chemistry
Volume280
Issue number19
DOIs
Publication statusPublished - 2005 May 13

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Oligomerization
Nucleotides
Epithelial Cells
Pathogens
Chemical activation
Acetylmuramyl-Alanyl-Isoglutamine
NADPH Dehydrogenase
HT29 Cells
Signal transduction
Inflammatory Bowel Diseases
Crohn Disease
Yeast
Signal Transduction
Bacteria
Screening
Mucous Membrane
Yeasts
Molecules
Survival
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells. / Barnich, Nicolas; Hisamatsu, Tadakazu; Aguirre, Jose E.; Xavier, Ramnik; Reinecker, Hans Christian; Podolsky, Daniel K.

In: Journal of Biological Chemistry, Vol. 280, No. 19, 13.05.2005, p. 19021-19026.

Research output: Contribution to journalArticle

Barnich, Nicolas ; Hisamatsu, Tadakazu ; Aguirre, Jose E. ; Xavier, Ramnik ; Reinecker, Hans Christian ; Podolsky, Daniel K. / GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells. In: Journal of Biological Chemistry. 2005 ; Vol. 280, No. 19. pp. 19021-19026.
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