Litcius/Paper detail

Pyruvate metabolism controls chromatin remodeling during CD4+ T cell activation

Enric Mocholí, Laura Russo, Keshav Gopal, Andrew G. Ramstead, Sophia M. Hochrein, Harmjan R. Vos, Geert Geeven, Adeolu Adegoke, Anna T. Hoekstra, Robert M. van Es, José M. Ramos Pittol, Sebastiaan J. Vastert, Jared Rutter, Timothy R. D. J. Radstake, Jorg van Loosdregt, Celia R. Berkers, Michal Mokrý, Colin C. Anderson, Ryan M. O’Connell, Martin Vaeth, John R. Ussher, Boudewijn Burgering, Paul J. Coffer

2023Cell Reports39 citationsDOIOpen Access PDF

Abstract

Upon antigen-specific T cell receptor (TCR) engagement, human CD4+ T cells proliferate and differentiate, a process associated with rapid transcriptional changes and metabolic reprogramming. Here, we show that the generation of extramitochondrial pyruvate is an important step for acetyl-CoA production and subsequent H3K27ac-mediated remodeling of histone acetylation. Histone modification, transcriptomic, and carbon tracing analyses of pyruvate dehydrogenase (PDH)-deficient T cells show PDH-dependent acetyl-CoA generation as a rate-limiting step during T activation. Furthermore, T cell activation results in the nuclear translocation of PDH and its association with both the p300 acetyltransferase and histone H3K27ac. These data support the tight integration of metabolic and histone-modifying enzymes, allowing metabolic reprogramming to fuel CD4+ T cell activation. Targeting this pathway may provide a therapeutic approach to specifically regulate antigen-driven T cell activation.

Topics & Concepts

Cell biologyPyruvate dehydrogenase complexChromatin remodelingHistoneAcetyl-CoAP300-CBP Transcription FactorsPyruvate dehydrogenase kinaseChemistryBiologyHistone acetyltransferaseT cellBiochemistryMetabolismHistone AcetyltransferasesEnzymeGeneImmunologyImmune systemHistone Deacetylase Inhibitors ResearchImmune cells in cancerCancer, Hypoxia, and Metabolism