期刊
CELL CYCLE
卷 11, 期 7, 页码 1354-1363出版社
TAYLOR & FRANCIS INC
DOI: 10.4161/cc.19755
关键词
C. elegans; cdc-25.1; wee-1.3; cdk-1; cyb-3; germline mitotic proliferation; cell cycle rate
类别
资金
- National Research Foundation of Korea (NRF)
- Ministry of Education, Science and Technology [2010-0011182, 2010-0009509]
- Konkuk University, Korea
- Seoul Scholarship Foundation
- National Institutes of Health National Center for Research Resources
- National Research Foundation of Korea [2010-0009509, 2010-0011182] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
In Caenorhabditis elegans, cdc-25.1 loss-of-function mutants display a lack of germline proliferation. We found that the proliferation defect of cdc-25.1 mutants was suppressed by wee-1.3 RNAi. Further, among the seven cdk and seven cyclin homologs examined, cdk-1 and cyb-3 RNAi treatment caused the most severe germline proliferation defects in an rrf-1 mutant background, which were similar to those of the cdc-25.1 mutants. In addition, while RNAi of cyd-1 and cye-1 caused significant germline proliferation defects, RNAi of cdk-2 and cdk-4 did not. Compared with the number of germ nuclei in wee-1.3(RNAi) worms, the number in wee-1.3(RNAi); cdk-1(RNAi) and wee-1.3(RNAi); cyb-3(RNAi) worms further decreased to the level of cdk-1(RNAi) and cyb-3(RNAi) worms, respectively, indicating that cdk-1 and cyb-3 are epistatic and function downstream of cdc-25.1 and wee-1.3 in the control of the cell cycle. BrdU labeling of adult worms showed that, while 100% of the wild-type germ nuclei in the mitotic region incorporated BrdU when labeled for more than 12 h at 20 C, a small fraction of the cdc-25.1 mutant germ nuclei failed to incorporate BrdU even when labeled for 68 h. These results indicate that CDC-25.1 is required for maintaining proper rate of germline mitotic cell cycle. We propose that CDC-25.1 regulates the rate of germline mitotic cell cycle by counteracting WEE-1.3 and by positively controlling Cdk1, which forms a complex primarily with CYB-3, but also possibly with CYD-1 and CYE-1.
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