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Proceedings Paper

Visualization of EGFR and Grb2 interaction using bimolecular fluorescence complementation
Author(s): Xiangyong Li; Jun Chu; Qingming Luo; Zhihong Zhang
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Paper Abstract

The dimerization of epidermal growth factor receptor (EGFR) and its endocytic transport are important in regulating signal transduction. In the present study, we applied the strategy of Bimolecular Fluorescence Complementation (BiFC), EGFR homodimer and hetrodimer of EGFR and its partner Grb2 in cells were visualized. This strategy takes advantage of the ability of two nonfluorescent fragments of Venus fluorescent protein to form a fluorescent signal when fused to the amino termini of EGFR and Grb2. Since EGFR is a large protein contains more than 1800 amido acids, proper fold of the fusion protein is essential for the BiFC assay of EGFR and its partners. Our results indicate that BiFC is a suitable application for research of EGFR interaction with other proteins.

Paper Details

Date Published: 13 February 2008
PDF: 5 pages
Proc. SPIE 6868, Small Animal Whole-Body Optical Imaging Based on Genetically Engineered Probes, 68680T (13 February 2008); doi: 10.1117/12.763411
Show Author Affiliations
Xiangyong Li, Huazhong Univ. of Science and Technology (China)
Jun Chu, Huazhong Univ. of Science and Technology (China)
Qingming Luo, Huazhong Univ. of Science and Technology (China)
Zhihong Zhang, Huazhong Univ. of Science and Technology (China)


Published in SPIE Proceedings Vol. 6868:
Small Animal Whole-Body Optical Imaging Based on Genetically Engineered Probes
Alexander P. Savitsky; Robert E. Campbell; Robert M. Hoffman, Editor(s)

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