Open AccessFOXM1D potentiates PKM2‐mediated tumor glycolysis and angiogenesis
Author(s) -
Zhang Wei,
Zhang Xin,
Huang Sheng,
Chen Jianfeng,
Ding Peipei,
Wang Qi,
Li Luying,
Lv Xinyue,
Li Ling,
Zhang Pingzhao,
Zhou Danlei,
Wen Wenyu,
Wang Yiping,
Lei QunYing,
Wu Jiong,
Hu Weiguo
Publication year - 2021
Publication title -
molecular oncology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.332
H-Index - 88
eISSN - 1878-0261
pISSN - 1574-7891
DOI - 10.1002/1878-0261.12879
Subject(s) - glycolysis , angiogenesis , pkm2 , cancer research , chemistry , microbiology and biotechnology , medicine , biology , metabolism , biochemistry , pyruvate kinase
FOXM1D binds to tetrameric PKM2 and assembles a heterooctamer, thereby promoting aerobic glycolysis. Further, FOXM1D interacts with PKM2 and NF‐κB and induces their nuclear translocation via importin 4. The nuclear PKM2 and NF‐κB complexes subsequently augment VEGFA transcription. The increased VEGFA is secreted extracellularly via exosomes, an event potentiated by the interaction of FOXM1 with VPS11, eventually promoting tumor angiogenesis.