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

J Biol Chem. 2005 May 13;280(19):19021-6. doi: 10.1074/jbc.M413776200. Epub 2005 Mar 7.

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-kappaB 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Apoptosis Regulatory Proteins
  • COS Cells
  • Caco-2 Cells
  • Cell Line
  • Cell Line, Tumor
  • Cytosol / metabolism
  • Epithelial Cells / metabolism
  • Epithelial Cells / microbiology
  • Escherichia coli / metabolism
  • Genes, Reporter
  • Humans
  • Immunoblotting
  • Immunoprecipitation
  • Intestinal Mucosa / metabolism
  • Intestinal Mucosa / microbiology
  • Intestinal Mucosa / pathology
  • Intestines / microbiology
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Intracellular Signaling Peptides and Proteins / physiology*
  • Luciferases / metabolism
  • Microscopy, Confocal
  • NADH, NADPH Oxidoreductases / chemistry
  • NADH, NADPH Oxidoreductases / physiology*
  • NF-kappa B / metabolism
  • Nod2 Signaling Adaptor Protein
  • Plasmids / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA, Small Interfering / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction
  • Salmonella / metabolism
  • Signal Transduction
  • Two-Hybrid System Techniques

Substances

  • Apoptosis Regulatory Proteins
  • Intracellular Signaling Peptides and Proteins
  • NF-kappa B
  • NOD2 protein, human
  • Nod2 Signaling Adaptor Protein
  • RNA, Small Interfering
  • Luciferases
  • NADH, NADPH Oxidoreductases
  • NDUFA13 protein, human