MUC4-ErbB2 Oncogenic Complex: Binding studies using Microscale Thermophoresis.
作者： Maxime Liberelle , Romain Magnez , Xavier Thuru , Yamina Bencheikh , Severine Ravez
DOI: 10.1038/S41598-019-53099-0
关键词:
摘要: The MUC4 membrane-bound mucin is a large O-glycoprotein involved in epithelial homeostasis. At the cancer cell surface interacts with ErbB2 receptor via EGF domains to promote proliferation and migration. highly regarded as therapeutic target pancreatic it not expressed healthy pancreas, while neoexpressed early preneoplastic stages (PanINs). However, association/dissociation constant of MUC4-ErbB2 complex unknown. Protein-protein interactions (PPIs) have become major area research past years characterization their interactions, especially by biophysical methods, intensively used drug discovery. To characterize interaction, we MicroScale Thermophoresis (MST), powerful method for quantitative protein interaction analysis under challenging conditions. We worked CHO lysates containing either transmembrane β subunit (MUC4β) or truncated mutant encompassing only (MUC4EGF3+1+2). MST studies led equilibrium dissociation constants (Kd) MUC4β-ErbB2 (7–25 nM) MUC4EGF3+1+2/ErbB2 (65–79 nM) complexes. This work provides new information regarding at level also confirms that presence three sufficient provide efficient interaction. technological approach will be very useful future validate small molecule binding affinities targeting discovery development cancer. It high interest other known membrane mucins forming oncogenic complexes ErbBs surface.
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