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Short Report
SCFPof3 and SCFPof1 regulate Wee1 degradation and mitotic entry in fission yeast
Cui Qiu, Yuan-yuan Yi, Rafael Lucena, Meng-juan Wu, Jia-hao Sun, Xi Wang, Quan-wen Jin, Yamei Wang
J Cell Sci 2017 : jcs.202895 doi: 10.1242/jcs.202895 Published 19 December 2017
Cui Qiu
State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China
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Yuan-yuan Yi
State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China
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Rafael Lucena
Department of Molecular, Cell and Developmental Biology, University of California, Santa Cruz, CA 95064, USA
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Meng-juan Wu
State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China
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Jia-hao Sun
State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China
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Xi Wang
State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China
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Quan-wen Jin
State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China
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  • For correspondence: wangyamei@xmu.edu.cnjinquanwen@xmu.edu.cn
Yamei Wang
State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China
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  • For correspondence: wangyamei@xmu.edu.cnjinquanwen@xmu.edu.cn
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Abstract

The key kinase Cdk1 (Cdc2) promotes irreversible mitotic entry mainly by activating the phosphatase Cdc25 while suppressing the tyrosine kinase Wee1. Wee1 needs to be down-regulated at the onset of mitosis to ensure rapid activation of Cdk1. In human somatic cells, one mechanism of suppressing Wee1 activity is mediated by ubiquitylation-dependent proteolysis through the Skp1/Cul1/F-box protein (SCF) ubiquitin E3 ligase complex. This mechanism is believed to be conserved from yeasts to humans. So far, the best characterized human F-box proteins involved in recognition of Wee1 are β-TrCP and Tome-1. Although fission yeast Wee1 is the first identified member of its conserved kinase family, the F-box proteins involved in recognition and ubiquitylation of Wee1 have not been identified in this organism. In this study, our screen using Wee1-Renilla luciferase as the reporter revealed that two F-box proteins Pof1 and Pof3 are required for downregulating Wee1 and are possibly responsible for recruiting Wee1 to SCF. Our genetic analyses supported a functional relevance between Pof1 and Pof3 and the rate of mitotic entry, and Pof3 might play a major role in this process.

  • Received February 20, 2017.
  • Accepted December 12, 2017.
  • © 2017. Published by The Company of Biologists Ltd
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Keywords

  • fission yeast
  • Wee1
  • SCF
  • F-box protein
  • Pof1
  • Pof3

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SCFPof3 and SCFPof1 regulate Wee1 degradation and mitotic entry in fission yeast
Cui Qiu, Yuan-yuan Yi, Rafael Lucena, Meng-juan Wu, Jia-hao Sun, Xi Wang, Quan-wen Jin, Yamei Wang
J Cell Sci 2017 : jcs.202895 doi: 10.1242/jcs.202895 Published 19 December 2017
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SCFPof3 and SCFPof1 regulate Wee1 degradation and mitotic entry in fission yeast
Cui Qiu, Yuan-yuan Yi, Rafael Lucena, Meng-juan Wu, Jia-hao Sun, Xi Wang, Quan-wen Jin, Yamei Wang
J Cell Sci 2017 : jcs.202895 doi: 10.1242/jcs.202895 Published 19 December 2017

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