Malonylation of GAPDH is an inflammatory signal in macrophages

Silvia Galván-Peña, Richard G. Carroll, Carla Newman, Elizabeth C. Hinchy, Eva Palsson-McDermott, Elektra K. Robinson, Sergio Covarrubias, Alan Nadin, Andrew M. James, Moritz Haneklaus, Susan Carpenter, Vincent P. Kelly, Michael P. Murphy, Louise K. Modis and Luke A. O’Neill ()
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Silvia Galván-Peña: Trinity College
Richard G. Carroll: Royal College of Surgeons in Ireland
Carla Newman: GlaxoSmithKline
Elizabeth C. Hinchy: University of Cambridge
Eva Palsson-McDermott: Trinity College
Elektra K. Robinson: UC Santa Cruz
Sergio Covarrubias: UC Santa Cruz
Alan Nadin: GlaxoSmithKline
Andrew M. James: University of Cambridge
Moritz Haneklaus: Trinity College
Susan Carpenter: UC Santa Cruz
Vincent P. Kelly: Trinity College
Michael P. Murphy: University of Cambridge
Louise K. Modis: GlaxoSmithKline
Luke A. O’Neill: Trinity College

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract Macrophages undergo metabolic changes during activation that are coupled to functional responses. The gram negative bacterial product lipopolysaccharide (LPS) is especially potent at driving metabolic reprogramming, enhancing glycolysis and altering the Krebs cycle. Here we describe a role for the citrate-derived metabolite malonyl-CoA in the effect of LPS in macrophages. Malonylation of a wide variety of proteins occurs in response to LPS. We focused on one of these, glyceraldehyde-3-phosphate dehydrogenase (GAPDH). In resting macrophages, GAPDH binds to and suppresses translation of several inflammatory mRNAs, including that encoding TNFα. Upon LPS stimulation, GAPDH undergoes malonylation on lysine 213, leading to its dissociation from TNFα mRNA, promoting translation. We therefore identify for the first time malonylation as a signal, regulating GAPDH mRNA binding to promote inflammation.

Date: 2019
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DOI: 10.1038/s41467-018-08187-6

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