The regulation of KIF3 motor complex by POPX2 phosphatase
The POPX2 serine/threonine phosphatase was first identified as a Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKPase). Later, the phosphatase was isolated as a binding partner of PIX, a guanine nucleotide exchange factor of the Rho GTPases. POPX2 has been shown to dephosphorylate and down...
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sg-ntu-dr.10356-490452023-02-28T18:43:38Z The regulation of KIF3 motor complex by POPX2 phosphatase Phang, Hui Qun Koh Cheng Gee School of Biological Sciences DRNTU::Science::Biological sciences The POPX2 serine/threonine phosphatase was first identified as a Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKPase). Later, the phosphatase was isolated as a binding partner of PIX, a guanine nucleotide exchange factor of the Rho GTPases. POPX2 has been shown to dephosphorylate and downregulate the activity of the Cdc42/Rac1-activated kinase, PAK1, through formation of POPX2-PIX-PAK1 trimeric complex. Recent studies have also demonstrated that POPX2 interacts with the mammalian Diaphanous (mDia) protein and this interaction reduced the ability of mDia to activate transcription mediated by the serum response factor (SRF). Furthermore, POPX2 has also been implicated in the regulation of breast cancer cell motility and invasiveness. DOCTOR OF PHILOSOPHY (SBS) 2012-05-14T04:32:37Z 2012-05-14T04:32:37Z 2011 2011 Thesis Phang, H. Q. (2011). The regulation of KIF3 motor complex by POPX2 phosphatase. Doctoral thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/49045 10.32657/10356/49045 en 156 p. application/pdf |
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DRNTU::Science::Biological sciences Phang, Hui Qun The regulation of KIF3 motor complex by POPX2 phosphatase |
| description |
The POPX2 serine/threonine phosphatase was first identified as a Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKPase). Later, the phosphatase was isolated as a binding partner of PIX, a guanine nucleotide exchange factor of the Rho GTPases. POPX2 has been shown to dephosphorylate and downregulate the activity of the Cdc42/Rac1-activated kinase, PAK1, through formation of POPX2-PIX-PAK1 trimeric complex. Recent studies have also demonstrated that POPX2 interacts with the mammalian Diaphanous (mDia) protein and this interaction reduced the ability of mDia to activate transcription mediated by the serum response factor (SRF). Furthermore, POPX2 has also been implicated in the regulation of breast cancer cell motility and invasiveness. |
| author2 |
Koh Cheng Gee |
| author_facet |
Koh Cheng Gee Phang, Hui Qun |
| format |
Theses and Dissertations |
| author |
Phang, Hui Qun |
| author_sort |
Phang, Hui Qun |
| title |
The regulation of KIF3 motor complex by POPX2 phosphatase |
| title_short |
The regulation of KIF3 motor complex by POPX2 phosphatase |
| title_full |
The regulation of KIF3 motor complex by POPX2 phosphatase |
| title_fullStr |
The regulation of KIF3 motor complex by POPX2 phosphatase |
| title_full_unstemmed |
The regulation of KIF3 motor complex by POPX2 phosphatase |
| title_sort |
regulation of kif3 motor complex by popx2 phosphatase |
| publishDate |
2012 |
| url |
https://hdl.handle.net/10356/49045 |
| _version_ |
1759856300897861632 |