Understanding the biological functions of POPX2 phosphatase through its interactome

POPX2 (Partner of PIX 2) is a serine/threonine phosphatase known to dephosphorylate PAK1, CaMKII and TAK1. POPX2 has been reported to be positively associated with cell motility and invasiveness of breast cancer cells. In order to further investigate the roles and functions of POPX2 in the cells,...

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Main Author: Kim, Purum
Other Authors: Koh Cheng Gee
Format: Thesis-Doctor of Philosophy
Language:English
Published: Nanyang Technological University 2020
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Online Access:https://hdl.handle.net/10356/136952
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-1369522023-02-28T18:32:51Z Understanding the biological functions of POPX2 phosphatase through its interactome Kim, Purum Koh Cheng Gee School of Biological Sciences cgkoh@ntu.edu.sg Science::Biological sciences::Molecular biology POPX2 (Partner of PIX 2) is a serine/threonine phosphatase known to dephosphorylate PAK1, CaMKII and TAK1. POPX2 has been reported to be positively associated with cell motility and invasiveness of breast cancer cells. In order to further investigate the roles and functions of POPX2 in the cells, we have adopted two approaches to identify POPX2-interacting proteins. In the first approach, we pulled down Flag-tagged POPX2 and determined the co-precipitated proteins using mass spectrometry (MS). We discovered Coronin 1C (Coro 1C) as a potential POPX2-interacting protein. In the second approach, we used a combination of SILAC-MS proteomics and bioinformatic analysis and identified Check point kinase 1 (Chk1) as a binding partner and possible substrate of POPX2. Doctor of Philosophy 2020-02-06T07:10:43Z 2020-02-06T07:10:43Z 2019 Thesis-Doctor of Philosophy Kim, P. (2019). Understanding the biological functions of POPX2 phosphatase through its interactome. Doctoral thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/136952 10.32657/10356/136952 en This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0). application/pdf Nanyang Technological University
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Science::Biological sciences::Molecular biology
spellingShingle Science::Biological sciences::Molecular biology
Kim, Purum
Understanding the biological functions of POPX2 phosphatase through its interactome
description POPX2 (Partner of PIX 2) is a serine/threonine phosphatase known to dephosphorylate PAK1, CaMKII and TAK1. POPX2 has been reported to be positively associated with cell motility and invasiveness of breast cancer cells. In order to further investigate the roles and functions of POPX2 in the cells, we have adopted two approaches to identify POPX2-interacting proteins. In the first approach, we pulled down Flag-tagged POPX2 and determined the co-precipitated proteins using mass spectrometry (MS). We discovered Coronin 1C (Coro 1C) as a potential POPX2-interacting protein. In the second approach, we used a combination of SILAC-MS proteomics and bioinformatic analysis and identified Check point kinase 1 (Chk1) as a binding partner and possible substrate of POPX2.
author2 Koh Cheng Gee
author_facet Koh Cheng Gee
Kim, Purum
format Thesis-Doctor of Philosophy
author Kim, Purum
author_sort Kim, Purum
title Understanding the biological functions of POPX2 phosphatase through its interactome
title_short Understanding the biological functions of POPX2 phosphatase through its interactome
title_full Understanding the biological functions of POPX2 phosphatase through its interactome
title_fullStr Understanding the biological functions of POPX2 phosphatase through its interactome
title_full_unstemmed Understanding the biological functions of POPX2 phosphatase through its interactome
title_sort understanding the biological functions of popx2 phosphatase through its interactome
publisher Nanyang Technological University
publishDate 2020
url https://hdl.handle.net/10356/136952
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