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AMPK regulates anaphase central spindle length by phosphorylation of KIF4A Free
Qian-Ru Li 1,2 , Xiu-Min Yan 3 , Lin Guo 2, * , Jia Li 1, * , and Yi Zang 1, *
1 National Center for Drug Screening, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China
2 State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China
3 State Key Laboratory of Cell Biology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China
* *Correspondence to:Yi Zang, E-mail:; Jia Li, E-mail:; Lin Guo, E-mail:
J Mol Cell Biol, Volume 10, Issue 1, February 2018, Pages 2-17
Keyword:  AMPK, phosphoregulation, KIF4A, mitosis, central spindle length

AMP-activated protein kinase (AMPK) is an energy sensor that couples the cellular energy state with basic biological processes. AMPK is thought to be linked with cell division although the underlying mechanisms remain largely unknown. Here, we show that AMPK functionally participates throughout cell division and that AMPK catalytic subunits, especially α2, are sequentially associated with separate mitotic apparatus. Using quantitative phosphoproteomics analysis, we found that the strong direct substrate KIF4A is phosphorylated by AMPK at Ser801. Further analysis revealed that AMPK and Aurora B competitively phosphoregulates KIF4A during mitotic phase due to overlapping recognition motifs, resulting in the elaborate phosphoregulation for KIF4A-dependent central spindle length control. Given the intrinsic energy-sensing function of AMPK, our study links the KIF4A-dependent control of central spindle length with cellular glucose stress.