Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/25362
Title: TYROSINE PHOSPHORYLATED WBP2 REGULATES CELL PROLIFERATION THROUGH THE E2F PATHWAY
Authors: TAN KAH YAP
Keywords: E2F, WBP2, breast cancer, proliferation, cell cycle, tyrosine phosphorylation
Issue Date: 10-Jan-2011
Source: TAN KAH YAP (2011-01-10). TYROSINE PHOSPHORYLATED WBP2 REGULATES CELL PROLIFERATION THROUGH THE E2F PATHWAY. ScholarBank@NUS Repository.
Abstract: WBP2 is a WW domain binding protein. It was identified as a nuclear cofactor that associates with estrogen receptor and progesterone receptor and mediates the transcriptional activation function of these receptors. We have previously shown that WBP2 was tyrosine phosphorylated following EGF stimulation. In this study, we characterized the phosphorylation kinetics of WBP2 in an endogenous system and identified the phosphorylation sites. By creating MCF7 cells stably expressing WBP2, its phospho-mimic and phospho-defective mutants, we found that phosphorylation of WBP2 leads to increased cancer cell proliferation, even in the absence of hormones. To understand the mechanism behind WBP2¿s effect in conferring hormone independence to cancer cells, we conducted luciferase pathway reporters screening. We identified the E2F pathway as one of the pathways activated by WBP2. Protein levels of G1/S cell cycle regulator E2Fs were elevated in cells expressing phospho-mimic WBP2 along with increased DNA synthesis. By RNA interference of E2F1 and E2F3, we found that cell proliferation of phospho-mimic WBP2 stable cell line was more dependent on E2F compared to cells expressing vector control. Our results implicate the WBP2-E2F pathway as a mechanism in WBP2 mediated cancer cell proliferation.
URI: http://scholarbank.nus.edu.sg/handle/10635/25362
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