Animal cells and systems

  • 제11권2호
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  • Pages.205-213
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  • 2007
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  • 1976-8354(pISSN)
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  • 2151-2485(eISSN)
한국통합생물학회 (The Korean Society for Integrative Biology)
권호 표지

Regulation of Nek6 Functions by Its SUMOylation on the $K^{252}$ Residue

  • Lee, Eun-Jeoung (School of Science Education, Chungbuk National University) ;
  • Hyun, Sung-Hee (Department of Pre-medicine, Eulji University School of Medicine) ;
  • Chun, Jae-Sun (Department of Biology Education, Korea National University of Education) ;
  • Shin, Sung-Hwa (School of Science Education, Chungbuk National University) ;
  • Lee, Kyung-Eun (School of Science Education, Chungbuk National University) ;
  • Park, In-Suk (School of Science Education, Chungbuk National University) ;
  • Kang, Sang-Sun (School of Science Education, Chungbuk National University)
  • 발행 : 2007.12.31
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초록

Nek6 belongs to NIMA1 (never in mitosis, gene A) related kinase, which was originally identified in Aspergillus nidulans as a serine/threonine kinase critical for cell cycle progression. We noticed that the putative SUMOylation site is localized on the $K^{252}$ residue in $^{251}FKsD^{254}$ of Nek6, based on the consensus sequence ${\Phi}KxE$; where ${\Phi}$ represents L, I, V or F and x is any amino acid. We observed that the Nek6 SUMO mutant (K252R) has decreased protein kinase activity, nuclear speckle localization and protein stability, compared with that of the Nek6 wild type. However, the Nek6 SUMO mutant increased the cell survival rate of COS-1 cells as determined by FACS analysis. Therefore, our data suggest that SUMOylation on the $K^{252}$ residue of Nek6 is required for its normal functions, such as proper nuclear localization, kinase activity and protein stability, to control cell cycle.

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참고문헌

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