잠시만 기다려 주세요. 로딩중입니다.

Regulation of Nek6 functions by its SUMOylation on the K252 residue

Animal Cells and Systems 2007년 11권 2호 p.205 ~ 213
이은정, 현성희, 천재순, 신성화, 이경은, 박인석, 강상선,
소속 상세정보
이은정 ( Lee Eun-Jeoung ) - Chungbuk National University School of Science Education
현성희 ( Hyun Sung-Hee ) - Eulji University School of Medicine Department of Pre-medicine
천재순 ( Chun Jae-Sun ) - Korea National University of Education Department of Biology Education
신성화 ( Shin Sung-Hwa ) - Chungbuk National University School of Science Education
이경은 ( Lee Kyung-Eun ) - Chungbuk National University School of Science Education
박인석 ( Park In-Suk ) - Chungbuk National University School of Science Education
강상선 ( Kang Sang-Sun ) - Chungbuk National University School of Science Education

Abstract


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 K252 residue in 251FKsD254 of Nek6, based on the consensus sequence FKxE; where F 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 K252 residue of Nek6 is required for its normal functions, such as proper nuclear localization, kinase activity and protein stability, to control cell cycle.

키워드

Nek6; serine/threonine kinase; cell cycle; SUMOylation; Apoptosis

원문 및 링크아웃 정보

등재저널 정보