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Regulation of Nek6 Functions by Its SUMOylation on the $K^{252}$ Residue
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  • Regulation of Nek6 Functions by Its SUMOylation on the $K^{252}$ Residue
  • Regulation of Nek6 Functions by Its SUMOylation on the $K^{252}$ Residue
저자명
Lee. Eun-Jeoung,Hyun. Sung-Hee,Chun. Jae-Sun,Shin. Sung-Hwa,Lee. Kyung-Eun,Park. In-Suk,Kang. Sang-Sun
간행물명
Integrative biosciences
권/호정보
2007년|11권 2호|pp.205-213 (9 pages)
발행정보
한국동물학회
파일정보
정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

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.