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. 2007 Nov-Dec;27(6B):3963-71.

Regulation of pyruvate kinase type M2 by A-Raf: a possible glycolytic stop or go mechanism

Sybille Mazurek  1 , Hannes C A Drexler, Jakob Troppmair, Erich Eigenbrodt, Ulf R Rapp
Affiliations
  • PMID: 18225557
Free article

Regulation of pyruvate kinase type M2 by A-Raf: a possible glycolytic stop or go mechanism

Sybille Mazurek et al. Anticancer Res. 2007 Nov-Dec.
Free article

Abstract

Recently a link between A-Raf cellular energy homeostasis and synthetic pathways has been suggested through the identification of pyruvate kinase type M2 (M2-PK), a key glycolytic enzyme, as interaction partner of A-Raf In this study, we demonstrated that A-Raf is an important regulator of M2-PK function. In primary mouse fibroblasts, which are characterized by glutamine production and serine degradation, A-Raf induced dimerization and inactivation of M2-PK, thereby reducing conversion rates from glucose to lactate. In immortalized NIH3T3 fibroblasts, showing glutamine degradation and serine production, oncogenic A-Raf increased the highly active tetrameric form of M2-PK and favored glycolytic energy production. High serine levels thus may be responsible for the activation of M2-PK in A-Raf transformed NIH3T3 cells.

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