Effect of sialylation on EGFR phosphorylation and resistance to tyrosine kinase inhibition

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 112; no. 22; pp. 6955 - 6960
• Main Authors: Yen, Hsin-Yung, Liu, Ying-Chih, Chen, Nai-Yu, Tsai, Chia-Feng, Wang, Yi-Ting, Chen, Yu-Ju, Hsu, Tsui-Ling, Yang, Pan-Chyr, Wong, Chi-Huey
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 02.06.2015; National Acad Sciences
• Subjects: Biological Sciences; carcinogenesis; Cell Line, Tumor; Cells; Dimerization; Enzyme Inhibitors; Epidermal growth factor; epidermal growth factor receptors; gene expression regulation; Humans; Kinases; Lung cancer; lung neoplasms; Models, Molecular; Mutation; Mutation, Missense - genetics; Neuraminidase - pharmacology; Phosphorylation; Phosphorylation - drug effects; Protein Binding - drug effects; Protein-Tyrosine Kinases - antagonists & inhibitors; Quinazolines; Receptor, Epidermal Growth Factor - genetics; Receptor, Epidermal Growth Factor - metabolism; tyrosine; lung cancer; dimerization; glycosylation; gefitinib; tyrosin kinase inhibitor

Epidermal growth factor receptor (EGFR) is a heavily glycosylated transmembrane receptor tyrosine kinase. Upon EGF-binding, EGFR undergoes conformational changes to dimerize, resulting in kinase activation and autophosphorylation and downstream signaling. Tyrosine kinase inhibitors (TKIs) have been...