Matrix Metalloprotease-7 Mediates Nucleolar Assembly and Intra-nucleolar Cleaving p53 in Gefitinib-Resistant Cancer Stem Cells.

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ID: 264349
2020
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Abstract
The enlarged distinct bulky-ball-like nucleolus matrix assembly is observed in most cancer stem cells (CSCs); however, the underlying mechanism is largely unknown. We show that matrix metalloproteinase-7 (MMP-7) shedding MUC-1 SEA domain releases MUC-1 C-ter, facilitating the nucleolus trafficking of p53 in gefitinib-resistant lung CSCs. The nucleolus colocalizations of p53, MUC-1 C-ter, MMP-7 and nucleolin were observed in the CD34 CXADR CD44v gefitinib-resistant EGFR CSC colonies. MUC-1 C-ter induced a unique porous bulky-ball-shaped, cagelike nucleolus that functions as a nucleus molecular "garage" for potent tumor suppressor, p53. Nucleolus could also facilitate the novel sub-nucleus compartment for proteolytic processing p53 by MMP-7 to generate a 35 kDa fragment. Moreover, we show that salinomycin, an anti-CSC agent, disrupts nucleolus by inducing nucleoplasm translocation of p53 and sensitizing CSC to chemotherapy drugs. Thus, this study highlights the MMP-7-MUC-1-p53 axis in nucleolus as a potential therapeutic target for anti-CSCs to resolve the chemotherapy-resistance dilemma.
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yu2020matrixiscience Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Yu, Wei-Hsuan;Wu, Erxi;Li, Yongqing;Hou, Hsin-Han;Yu, Shuan-Su C;Huang, Po-Tsang;Kuo, Wen-Hung;Qi, Dan;Yu, Chong-Jen;
Journal iScience
Year 2020
DOI
10.1016/j.isci.2020.101600
URL
Keywords
Cancer cell biology molecular biology

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