期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 99, 期 4, 页码 1984-1989出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.042689299
关键词
intramolecular binding; inhibition mitosis; mammalian cells
资金
- NIGMS NIH HHS [R01 GM059172, GM59172] Funding Source: Medline
Mammalian polo-like kinase (Pik) acts at various stages in early and late mitosis. Pik is phosphorylated and activated in mitosis, and the proper subcellular localization of Pik is essential for mitotic regulation. We have observed that overexpression of the C-terminal domain of Pik is more effective than wild-type or kinase-defective Pik in causing mitotic delay or arrest. The specific activity of Pik with C-terminal deletions or substitution of aspartate for threo-nine-210 is increased severalfold relative to wild type. We show in this communication that the C-terminal domain can bind to full-length or the catalytic domain of Pik and inhibit its kinase activity, and that this binding is disrupted when threonine-210 is substituted with an aspartic acid residue. The C-terminal domain binds unphosphorylated Pik from G(2) arrested cells, but not phosphorylated Pik from mitotic cells. Green fluorescent protein-C-terminal Pik is localized at the centrosome and the midbody of transfected cells as shown previously for full-length enzyme. These and other data indicate that although the C terminus serves to regulate Pik kinase activity, the localization of the C terminus at the centrosome and other sites in transfected cells may block the correct localization of endogenous Pik.
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