國家衛生研究院 NHRI:Item 3990099045/8427
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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/8427


    Title: Unraveling the impact of lipid domains on the dimerization processes of single-molecule EGFRs of live cells
    Authors: Lin, CY;Huang, JY;Lo, LW
    Contributors: Institute of Biomedical Engineering and Nanomedicine
    Abstract: Epidermal growth factor receptor (EGFR/ErbB1) is a transmembrane protein that can drive cell growth and survival via the ligand-induced dimerization of receptors. Because dimerization is a common mechanism for signal transduction, it is important to improve our understanding of how the dimerization process and membrane structure regulate signal transduction. In this study, we examined the effect of lipid nanodomains on the dimerization process of EGFR molecules. We discovered that after ligand binding, EGFR molecules may move into lipid nanodomains. The lipid nanodomains surrounding two liganded EGFRs can merge during their correlated motion. The transition rates between different diffusion states of liganded EGFR molecules are regulated by the lipid domains. Our method successfully captures both the sensitivity of single-molecule processes and statistic accuracy of data analysis, providing insight into the connection between the mobile clustering process of receptors and the hierarchical structure of plasma membrane.
    Date: 2015-03
    Relation: Biochimica et Biophysica Acta (BBA) - Biomembranes. 2015 Mar;1848(3):886-893.
    Link to: http://dx.doi.org/10.1016/j.bbamem.2014.12.019
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0005-2736&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000349582500016
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84921047771
    Appears in Collections:[Leu-Wei Lo] Periodical Articles

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