title: How focal adhesion size depends on integrin affinity.
abstract: Understanding how the thermodynamics and kinetics of integrin receptor binding and clustering impact the formation of focal adhesions is important for understanding the mechanisms cells use to sense and respond to physical cues in their environment. Cells on chemically well-defined surfaces were observed to have distributions of focal adhesions shifted toward smaller sizes when presented with higher affinity ligands (Kato, M.; Mrksich, M. Biochemistry 2004, 43, 2699). In this paper, we account for this trend with a simple model in which integrins are treated as particles on a lattice, and their stochastic dynamics are simulated with a kinetic Monte Carlo algorithm. How the trend depends on force-coupled growth, membrane fluctuations, and heterogeneity of receptor-ligand interactions is analyzed. Predictions are made for substrates in which the ligands presented can vary in either space or time, so that the model can be validated experimentally.
authors.affiliation: Department of Chemistry, Department of Physics, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637.
authors.forename: Tong
authors.initials: T
authors.lastname: Zhao
authors.forename: Ying
authors.initials: Y
authors.lastname: Li
authors.forename: Aaron R
authors.initials: AR
authors.lastname: Dinner
mesh_terms: D022001:Focal Adhesions / Q000737:chemistry*; D016023:Integrins / Q000737:chemistry*; D008954:Models, Biological
chemical_list: D016023:Integrins