NDRG2 and PRA1 interact and synergistically inhibit T-cell factor/beta-catenin signaling
- Authors
- Kim, Jong-Tae; Kim, Jae Wha; Kang, Yun Hee; Kim, Kwang Dong; Lee, Seon-Jin; Choi, Seung-Chul; Kim, Kwang Soo; Chae, Suhn-Kee; Kim, Jung Woo; Lim, Jong-Seok; Lee, 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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