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VOLUME 10 ISSUE 1 (Feb, 2018)

Editorial
Articles
Qian-Ru Li , Xiu-Min Yan, Lin Guo, Jia Li, and Yi Zang
Xiaoling Bao 1,† , Heng Liu 1,† , Xing Liu 2 , Ke Ruan 1 , Yonghui Zhang 1 , Zhiyong Zhang , Qi Hu, Ying Liu, Saima Akram, Jiahai Zhang, Qingguo Gong, Wenwen Wang, Xiao Yuan, Jian Li,Lingli Zhao, Zhen Dou, Ruijun Tian, Xuebiao Yao, Jihui Wu, and Yunyu Shi
Christian Schrenk , Verena Fetz, Cecilia Vallet, Christina Heiselmayer, Elisabeth Schro ¨der, Astrid Hensel, Angelina Hahlbrock, De´sire´e Wu ¨nsch, Dorothee Goesswein, Carolin Bier, Negusse Habtemichael, Gu ¨nter Schneider, Roland H. Stauber, and Shirley K. Knauer
Xiaohua Yan,, Jingyi Wu, Quanlong Jiang, Hao Cheng, Jing-Dong J. Han, and Ye-Guang Chen
Dan Wang, Jing Zhao, Shuang Li, Jianxin Wei, Ling Nan, Rama K. Mallampalli, Nathaniel M. Weathington, Haichun Ma, and Yutong Zhao
Zheng Gao , Xiaoxin Zhang, Xingjiang Yu, Dandan Qin, Yi Xiao, Yang Yu, Yunlong Xiang,Xiaoqing Nie, Xukun Lu, Wenbo Liu, Zhaohong Yi, and Lei Li
Research Highlight
  Collection: New Insights into the Regulation of Cell Cycle


Cover legend
AMPK activity controls central spindle length. In normal condition (middle), KIF4A ATPase activity is modulated by balancing Aurora B (blue)- and AMPK (red)-dependent phosphorylation to construct a central spindle with appropriate size. Inhibiting AMPK activity or AMPK depletion induces an excess of Aurora B-dependent phosphorylation of KIF4A, which prematurely blocks central spindle elongation and shortens the central spindle length (left). In contrast, augmenting AMPK activity increases the competitiveness of AMPK-dependent phosphorylation and induces an undisturbed but elongated central spindle (right). See pages 2–17 by Li et al. for details.
 
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