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Title: Phosphatase POPX2 interferes with cell cycle by interacting with Chk1
Authors: Kim, Pu Rum
Koon, Yen Ling
Lee, Raphael Tze Chuen
Azizan, Farouq
Koh, Dylan Hong Zheng
Chiam, Keng-Hwee
Koh, Cheng-Gee
Keywords: Science::Biological sciences
Issue Date: 2020
Source: Kim, P. R., Koon, Y. L., Lee, R. T. C., Azizan, F., Koh, D. H. Z., Chiam, K. & Koh, C. (2020). Phosphatase POPX2 interferes with cell cycle by interacting with Chk1. Cell Cycle, 19(4), 405-418.
Project: 2016- T1-002-081
Journal: Cell Cycle
Abstract: Protein-protein interaction network analysis plays critical roles in predicting the functions of target proteins. In this study, we used a combination of SILAC-MS proteomics and bioinformatic approaches to identify Checkpoint Kinase 1 (Chk1) as a possible POPX2 phosphatase interacting protein. POPX2 is a PP2C phosphatase that has been implicated in cancer cell invasion and migration. From the Domain-Domain Interaction (DDI) database, we first determined that the PP2C phosphatase domain interacts with Pkinase domain. Subsequently, 46 proteins with Pkinase domain were identified from POPX2 SILAC-MS data. We then narrowed down the leads and confirmed the biological interaction between Chk1 and POPX2. We also found that Chk1 is a substrate of POPX2. Chk1 is a key regulator of the cell cycle and is activated when the cell suffers DNA damage. Our approach has led us to identify POPX2 as a regulator of Chk1 and can interfere with the normal function of Chk1 at G1-S transition of the cell cycle in response to DNA damage.
ISSN: 1538-4101
DOI: 10.1080/15384101.2020.1711577
Schools: School of Biological Sciences 
Interdisciplinary Graduate School (IGS) 
Organisations: Bioinformatics Institute, A*STAR
Rights: © 2020 Informa UK Limited, trading as Taylor & Francis Group. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
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