期刊
CURRENT BIOLOGY
卷 15, 期 10, 页码 894-904出版社
CELL PRESS
DOI: 10.1016/j.cub.2005.04.019
关键词
-
资金
- NCI NIH HHS [P30 CA016672, CA-16672] Funding Source: Medline
- NIDDK NIH HHS [K01 DK002966, K01 DK02966-01A1] Funding Source: Medline
- NIGMS NIH HHS [R01 GM056264-08S1, R01 GM62181-01, R01 GM062181-04, R01 GM056264-08, R01 GM062181-03, R01 GM062181, R01 GM056264, R01 GM062181-05, R01 GM056264-07] Funding Source: Medline
Background: The Aurora kinases control multiple aspects of mitosis, among them centrosome maturation, spindle assembly, chromosome segregation, and cytokinesis. Aurora activity is regulated in part by a subset of Aurora substrates that, once phosphorylated, can enhance Aurora kinase activity. Aurora A substrate activators include TPX2 and Ajuba, whereas the only known Aurora B substrate activator is the chromosomal passenger INCENP. Results: We report that the C. elegans Tousled kinase TLK-1 is a second substrate activator of the Aurora B kinase AIR-2. Tousled kinase (Tlk) expression and activity have been linked to ongoing DNA replication, and Tlk can phosphorylate the chromatin assembly factor Asf. Here, we show that TLK-1 is phosphorylated by AIR-2 during prophase/prometaphase and that phosphorylation increases TLK-1 kinase activity in vitro. Phosphorylated TLK-1 increases AIR-2 kinase activity in a manner that is independent of TLK-1 kinase activity but depends on the presence of ICP-1/INCENP. In vivo, TLK-1 and AIR-2 cooperate to ensure proper mitotic chromosome segregation. Conclusions: The C. elegans Tousled kinase TLK-1 is a substrate and activator of the Aurora B kinase AIR-2. These results suggest that Tousled kinases have a previously unrecognized role in mitosis and that Aurora B associates with discrete regulatory complexes that may impart distinct substrate specificities and functions to the Aurora B kinase.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据