Structural model and functional significance of pH-dependent talin-actin binding for focal adhesion remodeling

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 105; no. 38; pp. 14436 - 14441
• Main Authors: Srivastava, J, Barreiro, G, Groscurth, S, Gingras, A.R, Goult, B.T, Critchley, D.R, Kelly, M.J.S, Jacobson, M.P, Barber, D.L
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 23.09.2008; National Acad Sciences
• Subjects: Actins; Actins - chemistry; Actins - metabolism; Amino acids; Animals; Binding sites; Biological Sciences; Cell adhesion & migration; Cell Line; Cell motility; Chemical equilibrium; Computer Simulation; Focal adhesions; Focal Adhesions - metabolism; Hydrogen-Ion Concentration; Mice; Microfilaments; Models, Molecular; Molecular structure; Mutation; NMR; Nuclear magnetic resonance; Nuclear Magnetic Resonance, Biomolecular; Physiological regulation; Protein Binding; Protein Structure, Tertiary; Proteins; Renovations; Sensors; Talin - chemistry; Talin - genetics; Talin - metabolism

Actin filament binding by the focal adhesion (FA)-associated protein talin stabilizes cell-substrate adhesions and is thought to be rate-limiting in cell migration. Although F-actin binding by talin is known to be pH-sensitive in vitro, with lower affinity at higher pH, the functional significance o...