NIRF induces G1 arrest and associates with Cdk2
NIRF induces G1 arrest and associates with Cdk2
复制标题
DOI：
10.1016/j.bbrc.2004.04.190
复制
发表时间：
2004-06-25
影响因子：
3.1
通讯作者：
Kochi, H
中科院分区：
文献类型：
--
作者：
Li, YY;Mori, T;Kochi, H
NIRF是具有泛素样结构域、PHD指、YDG/SRA结构域和RING指结构域的RING指蛋白。研究表明NIRF是一种与细胞增殖相关的核蛋白。在这项研究中，我们进一步表征了NIRF在细胞周期调控中的功能。流式细胞仪分析表明，NIRF过表达诱导G1期细胞增加。免疫沉淀和免疫印迹实验表明，NIRF结合到失活的Cdk 2-细胞周期蛋白E复合物。细胞内存在磷酸化的NIRF，去磷酸化的NIRF与Cdk 2相互作用。NIRF在体外被Cdk 2磷酸化。这些结果提示NIRF可能参与了G1/S转换的调控。(C)2004爱思唯尔公司All rights reserved.
NIRF is a RING finger protein with a ubiquitin-like domain, a PHD finger, a YDG/SRA domain, and a RING finger domain. Previous study showed that NIRF is a nuclear protein expressed in association with cell proliferation. In this study, we further characterized NIRF functions in cell cycle regulation. Flow cytometric analysis showed that overexpression of NIRF induced an increase in G1 phase cells. Immunoprecipitation and immunoblotting experiments showed that NIRF bound to the inactive Cdk2-cyclin E complex. There existed phosphorylated NIRF in cells, and dephosphorylated NIRF interacted with Cdk2. NIRF was phosphorylated by Cdk2 in vitro. These results suggest that NIRF may participate in the G1/S transition regulation. (C) 2004 Elsevier Inc. All rights reserved.