Please use this identifier to cite or link to this item:
Title: Structural basis of the PNRC2-mediated Link between mRNA surveillance and decapping
Authors: Liu, Zhou
Piao, Shunfu
Parker, Roy
Lai, Tingfeng
Cho, Hana
Kim, Yoon Ki
Song, Haiwei
Bowler, Matthew W.
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2012
Source: Lai, T., Cho, H., Liu, Z., Bowler, M. W., Piao, S., Parker, R., et al. (2012). Structural Basis of the PNRC2-Mediated Link between mRNA Surveillance and Decapping. Structure, 20(12), 2025-2037.
Series/Report no.: Structure
Abstract: Nonsense-mediated mRNA decay (NMD) is an important mRNA surveillance system, and human PNRC2 protein mediates the link between mRNA surveillance and decapping. However, the mechanism by which PNRC2 interacts with the mRNA surveillance machinery and stimulates NMD is unknown. Here, we present the crystal structure of Dcp1a in complex with PNRC2. The proline-rich region of PNRC2 is bound to the EVH1 domain of Dcp1a, while its NR-box mediates the interaction with the hyperphosphorylated Upf1. The mode of PNRC2 interaction with Dcp1a is distinct from those observed in other EVH1/proline-rich ligands interactions. Disruption of the interaction of PNRC2 with Dcp1a abolishes its P-body localization and ability to promote mRNA degradation when tethered to mRNAs. PNRC2 acts in synergy with Dcp1a to stimulate the decapping activity of Dcp2 by bridging the interaction between Dcp1a and Dcp2, suggesting that PNRC2 is a decapping coactivator in addition to its adaptor role in NMD.
ISSN: 0969-2126
DOI: 10.1016/j.str.2012.09.009
Rights: © 2012 Elsevier Ltd.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

Citations 5

Updated on Jan 18, 2023

Web of ScienceTM
Citations 5

Updated on Jan 30, 2023

Page view(s) 50

Updated on Jan 31, 2023

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.