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NDRG2 and PRA1 interact and synergistically inhibit T-cell factor/beta-catenin signaling

Authors
Kim, Jong-TaeKim, Jae WhaKang, Yun HeeKim, Kwang DongLee, Seon-JinChoi, Seung-ChulKim, Kwang SooChae, Suhn-KeeKim, Jung WooLim, Jong-SeokLee, Hee Gu
Issue Date
Nov-2012
Publisher
WILEY
Keywords
NDRG; PRA1; Protein-protein interaction; Yeast two-hybrid screen; Promoter inhibition; Cell proliferation
Citation
FEBS LETTERS, v.586, no.22, pp 3962 - 3968
Pages
7
Journal Title
FEBS LETTERS
Volume
586
Number
22
Start Page
3962
End Page
3968
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/11815
DOI
10.1016/j.febslet.2012.09.045
ISSN
0014-5793
1873-3468
Abstract
NDRG2 is a member of the N-myc downstream regulated gene (NDRG) family, implicated in cell growth and differentiation. Investigation of NDRG2 molecular interactions by yeast two-hybrid screening identified prenylated Rab acceptor-1 (PRA1), involved in vesicle trafficking and protein transport, as binding partner. Binding of NDRG2 (and NDRG1-4) with PRA1 in vitro was confirmed by GST pull-down assay and immunoprecipitation, and colocalization was verified by confocal microscopy in HCT116 cells. Intracellular coexpression showed that NDRG2 and PRA1 synergistically downregulate T-cell factor (TCF) promoter activity and GSK3 beta phosphorylation. Results suggest that NDRG2 and PRA1 might act synergistically to prevent signaling of TCF/beta-catenin. Structured summary of protein interactions: NDRG2a binds to PRA1 by pull down (View interaction) NDRG2a physically interacts with PRA1 by two hybrid (View Interaction: 1, 2) PRA1 physically interacts with NDRG2a by anti tag coimmunoprecipitation (View interaction) NDRG2a, PRA1 and Catenin beta colocalize by cosedimentation (View interaction) NDRG2a and PRA1 colocalize by fluorescence microscopy (View Interaction: 1, 2, 3) (c) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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