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|Title:||Investigation of the function and behavior of p97/VCP||Authors:||Khong, Zi Jia||Keywords:||DRNTU::Science::Biological sciences||Issue Date:||2017||Source:||Khong, Z. J. (2017). Investigation of the function and behavior of p97/VCP. Doctoral thesis, Nanyang Technological University, Singapore.||Abstract:||p97/VCP is a multifunctional ATP-fueled ATPase quintessential for cell survival. As one of the most abundant cytosolic proteins, it is not surprising that p97/VCP regulates numerous pathways to ensure proper cell homeostasis. Here I show that p97/VCP regulates actin dynamics and cell migration via the ROCK pathway. The loss of p97/VCP triggers hyperphosphorylation of ROCK, resulting in extensive polymerization of actin. Persistent F-actin filaments and the absence of essential cell motility-related actin structures in p97/VCP knockdown cells led to compromised cell migration. I found that the loss of p97/VCP increases the level of ROCK-activating kinase, Plk1, through the ubiquitin-proteasome pathway. The increase in Plk1 thereafter affects the phosphorylation status of ROCK. Taken together, my study defines a hitherto unknown role of p97/VCP in actin regulation and describes a mechanism for the phosphorylation-dependent regulation of ROCK activity that implicates cancer metastasis and wound healing.||URI:||http://hdl.handle.net/10356/72339||Fulltext Permission:||restricted||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Theses|
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