Pharmacological Activation of Pyruvate Kinase M2 Inhibits CD4+ T Cell Pathogenicity and Suppresses Autoimmunity
Cell Metabolism 31(2): 391-405.e8
Article 2019 English
Authors
SA
Stefano Angiari
MR
Marah C. Runtsch
CS
Caroline E. Sutton
Abstract
1 min read
Pyruvate kinase (PK) catalyzes the conversion of phosphoenolpyruvate to pyruvate during glycolysis. The PK isoform PKM2 has additional roles in regulation of gene transcription and protein phosphorylation. PKM2 has been shown to control macrophage metabolic remodeling in inflammation, but its role in T cell biology is poorly understood. Here, we report PKM2 upregulation, phosphorylation, and nuclear accumulation in murine and human CD4
Juliana E. Toller-Kawahisa, Carlos Hiroji Hiroki, Camila M. Silva, Daniele C. Nascimento, Gabriel Azevedo Públio, Timna Varela Martins, Luis Eduardo Alves Damasceno, Flávio P. Veras, Paula Ramos Viacava, Fábio Yuji Sukesada, Emily A. Day, Alessia Zotta, Tristram A. J. Ryan, Rodrigo Moreira da Silva, Thiago M. Cunha, Norberto Peporine Lopes, Fernando Q. Cunha, Luke O'neill, José C. Alves‐Filho
Eva M. Pålsson‐McDermott, Annie M. Curtis, Gautam Goel, Mario A. Lauterbach, Frederick J. Sheedy, Laura E. Gleeson, Mirjam W.M. van den Bosch, Susan R. Quinn, Raquel Domingo-Fernandéz, Daniel Johnston, Jian‐kang Jiang, William J. Israelsen, Joseph Keane, Craig J. Thomas, Clary B. Clish, Matthew G. Vander Heiden, Ramnik J. Xavier, Luke O'neill
Discussion(0)
No comments yet. Be the first to comment.