Sugar Fix Keeps RIPK3 at Bay

Cristina Giogha; Kate E Lawlor

doi:10.1016/j.immuni.2019.02.018

Sugar Fix Keeps RIPK3 at Bay

Immunity. 2019 Mar 19;50(3):539-541. doi: 10.1016/j.immuni.2019.02.018.

Authors

Cristina Giogha¹, Kate E Lawlor²

Affiliations

¹ Centre for Innate Immunity and Infectious Diseases, Hudson Institute of Medical Research, Clayton, VIC 3168, Australia. Electronic address: cristina.giogha@hudson.org.au.
² Centre for Innate Immunity and Infectious Diseases, Hudson Institute of Medical Research, Clayton, VIC 3168, Australia; Department of Molecular and Translational Science, Monash University, Clayton, VIC 3168, Australia. Electronic address: kate.lawlor@hudson.org.au.

PMID: 30893581
DOI: 10.1016/j.immuni.2019.02.018

Abstract

Immunometabolism is emerging as an important modulator of immune responses. In this issue of Immunity, Li et al. (2019) examine the link between lipopolysaccharide (LPS)-induced glucose metabolism and innate immune signaling and identify how β-N-acetylglucosamine (O-GlcNAc) modification of the RIPK3 RHIM domain limits inflammation and necroptosis.

Publication types

Comment

MeSH terms

Humans
Inflammation*
N-Acetylglucosaminyltransferases
Receptor-Interacting Protein Serine-Threonine Kinases
Serine
Sugars*
Threonine

Substances

Sugars
Threonine
Serine
N-Acetylglucosaminyltransferases
O-GlcNAc transferase
RIPK3 protein, human
Receptor-Interacting Protein Serine-Threonine Kinases