PKM2 coordinates glycolysis with mitochondrial fusion and oxidative phosphorylation.
10.1007/s13238-019-0618-z
- Author:
Tong LI
1
;
Jinbo HAN
1
;
Liangjie JIA
1
;
Xiao HU
1
;
Liqun CHEN
1
;
Yiguo WANG
2
Author Information
1. MOE Key Laboratory of Bioinformatics, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
2. MOE Key Laboratory of Bioinformatics, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China. yiguo@mail.tsinghua.edu.cn.
- Publication Type:Journal Article
- Keywords:
MFN2;
PKM2;
glycolysis;
mTOR;
oxidative phosphorylation
- From:
Protein & Cell
2019;10(8):583-594
- CountryChina
- Language:English
-
Abstract:
A change in the metabolic flux of glucose from mitochondrial oxidative phosphorylation (OXPHOS) to aerobic glycolysis is regarded as one hallmark of cancer. However, the mechanisms underlying the metabolic switch between aerobic glycolysis and OXPHOS are unclear. Here we show that the M2 isoform of pyruvate kinase (PKM2), one of the rate-limiting enzymes in glycolysis, interacts with mitofusin 2 (MFN2), a key regulator of mitochondrial fusion, to promote mitochondrial fusion and OXPHOS, and attenuate glycolysis. mTOR increases the PKM2:MFN2 interaction by phosphorylating MFN2 and thereby modulates the effect of PKM2:MFN2 on glycolysis, mitochondrial fusion and OXPHOS. Thus, an mTOR-MFN2-PKM2 signaling axis couples glycolysis and OXPHOS to modulate cancer cell growth.
