Format

Send to

Choose Destination
Glycobiology. 2016 Jan;26(1):13-8. doi: 10.1093/glycob/cwv076. Epub 2015 Sep 14.

Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.

Author information

1
Department of Chemistry and Biochemistry.
2
Department of Biological Sciences, University of Delaware, Newark, DE 19716, USA.
3
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
4
Department of Chemistry and Biochemistry Department of Biological Sciences, University of Delaware, Newark, DE 19716, USA cgrimes@udel.edu.

Abstract

Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide. Upon activation, Nod2 induces the production of various inflammatory molecules such as cytokines and chemokines. Genetic linkage analysis identified and revealed three major mutations in Nod2 that are associated with the development of Crohn's disease. The objective of this study is to further characterize this protein by determining whether Nod2 is posttranslationally modified by O-N-acetylglucosamine (O-GlcNAc). O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins. We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.

KEYWORDS:

Crohn's disease; NF-κB; Nod2; O-GlcNAcylation; OGT

PMID:
26369908
PMCID:
PMC4672147
DOI:
10.1093/glycob/cwv076
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Silverchair Information Systems Icon for PubMed Central
Loading ...
Support Center