Lee Eun-Woo, Oh Wonkyung, Song Jaewhan
Department of Food Science and Biotechnology, Faculty of Life Science and Technology, Sungkyunkwan University, Suwon 440-746, Korea.
Mol Cells. 2006 Oct 31;22(2):133-40.
Jun activation domain-binding protein 1 (Jab1) is involved in various cellular mechanisms including development in Drosophila and mouse, cell cycle control and signal transduction pathways. Recent studies also determined that Jab1 functions as a nuclear exporter and inducer of cytoplasmic degradation for several proteins including p53, p27, capsid of West Nile virus, and Smad4/7 proteins. In particular, p53 is shown to bind to and to be exported into the cytoplasm by Jab1, which helps to maintain low levels of p53 under normal conditions. This review was undertaken in an effort to understand the biological significance of the homeostasis of p53 as maintained in the presence of Jab1. Based on our observations, we have provided potential mechanistic hypotheses for the nuclear export of p53 in coordination with Jab1 and the role of other factors in these processes.
Jun激活域结合蛋白1(Jab1)参与多种细胞机制,包括果蝇和小鼠的发育、细胞周期控制以及信号转导途径。最近的研究还确定,Jab1作为几种蛋白质(包括p53、p27、西尼罗河病毒衣壳蛋白和Smad4/7蛋白)的核输出蛋白和细胞质降解诱导剂发挥作用。特别是,p53被证明与Jab1结合并被转运到细胞质中,这有助于在正常条件下维持低水平的p53。进行这项综述是为了了解在Jab1存在的情况下维持p53稳态的生物学意义。基于我们的观察结果,我们提出了p53与Jab1协同进行核输出的潜在机制假说以及其他因素在这些过程中的作用。