Galectin-3 Binding to α<sub>5</sub>β<sub>1</sub> Integrin in Pore Suspended Biomembranes
Nirod Kumar Sarangi, Massiullah Shafaq‐Zadah, Guilherme B. Berselli, J. B. D. Robinson, Estelle Dransart, Aurélie Di Cicco, Daniel Lévy, Ludger Johannes, Tia E. Keyes
Abstract
integrin assemblies. Overall, our study demonstrates the capacity of WTGal3 to oligomerize in a cargo protein-dependent manner at low nanomolar concentrations. Of note, these WTGal3 oligomers appeared to have membrane active properties that could only be revealed using our sensitive methods. At slightly higher WTGal3 concentrations, the capacity to generate lateral assemblies between cargo proteins was observed. In cells, this could lead to the construction of tubular endocytic pits according to the glycolipid-lectin (GL-Lect) hypothesis or to the formation of galectin lattices, depending on cargo glycoprotein stability at the membrane, the local Gal3 concentration, or plasma membrane intrinsic parameters. The study also demonstrates the utility of microcavity array-suspended lipid bilayers to address the biophysics of transmembrane proteins.