Yuhui Jiang, Yugang Wang,Ting Wang, David H. Hawke, Yanhua Zheng, Xinjian Li, Qin Zhou,Sadhan Majumder, Erfei Bi, David X. Liu, Suyun Huang&
Zhimin Lu

Summary:
Pyruvate kinase M2 (PKM2) is expressed at high levels during embryonic development and tumour progression and is important for cell growth. However, it is not known whether it directly controls cell division. Here, we found that Aurora B phosphorylates PKM2, but not PKM1, at T45; this phosphorylation is required for PKM2’s localization and interaction with myosin light chain 2 (MLC2) in the contractile ring region of mitotic cells during cytokinesis.
PKM2 phosphorylates MLC2 at Y118, which primes the binding of ROCK2 to MLC2 and subsequent ROCK2-dependent MLC2 S15 phosphorylation. PKM2-regulated MLC2 phosphorylation, which is greatly enhanced by EGF stimulation or EGFRvIII, K-Ras G12V and B-Raf V600E mutant expression, plays a pivotal role in cytokinesis, cell proliferation and brain tumour development. These findings underscore the instrumental function of PKM2 in oncogenic EGFR-, K-Ras- and B-Raf-regulated cytokinesis and tumorigenesis.

Cited Products

11589	MLC2 (Phospho-Tyr118) Antibody
11590	MLC2 (Phospho-Ser15) Antibody
21157	Myosin Light Chain 2 (Ab-19) Antibody
21540	Cyclin B1(Ab-147) Antibody
21577	PKM1 Antibody
21578	PKM2 Antibody