Isolation and Characterization of Proteins Interacting with Activin Type Ⅱ Receptors

作     者：LIU Biao BAO Yong-li WEI Zhuang WU Yin MENG Xiang-ying LI Yu-xin YIN Wei-tian 

作者机构：Department of Hand Surgery China-japan Union Hospital Jilin University Changchun 130031 P. R. China Institute of Genetics and Cytology Northeast Normal University Changchun 130024 P. R. China 

出 版 物：《Chemical Research in Chinese Universities》 (高等学校化学研究（英文版）)

年 卷 期：2006年第22卷第2期

页      面：217-220页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 0703[理学-化学] 

基　　金：SupportedbytheDistinguishedYoungScholarsFundofJilinProvince(No.20050114) 

主　　题：Activin Activin receptor Ⅱ A( ActR Ⅱ A) Activin receptor interaction protein(ARIP) 

摘      要：Regulation of the number of aetivin receptors that are present in the cell membrane plays a key role in the modulation of cellular responses to activin. In order to find the regulators, a novel protein ARIPzip, interacting with activin type II receptors, was searched and identified by using yeast two-hybrid screening. ARIPzip is a splicing variant of ARIP2. This has been discussed previously. ARIPzip can specifically interact with ActR Ⅱ A, and is widely distributed in mouse tissues. Overexpression of ARIPzip can cause the activin-induced transcriptional activities to increase in a dose-dependent manner while the overexpression of ARIV2 can decrease these activities. These data suggest that the C-terminal rezions of ARIP2 and ARIPzip are involved in the regulation of activin signaling.