title: Structure and function of focal adhesions.
abstract: Integrin-dependent cell adhesions come in different shapes and serve in different cell types for tasks ranging from cell-adhesion, migration, and the remodeling of the extracellular matrix to the formation and stabilization of immunological and chemical synapses. A major challenge consists in the identification of adhesion-specific as well as common regulatory mechanisms, motivating the need for a deeper analysis of protein-protein interactions in the context of intact focal adhesions. Specifically, it is critical to understand how small differences in binding of integrins to extracellular ligands and/or cytoplasmic adapter proteins affect the assembly and function of an entire focal adhesion. By using the talin-integrin pair as a starting point, I would like to discuss how specific protein-protein and protein-lipid interactions can control the behavior and function of focal adhesions. By responding to chemical and mechanical cues several allosterically regulated proteins create a dynamic multifunctional protein network that provides both adhesion to the extracellular matrix as well as intracellular signaling in response to mechanical changes in the cellular environment.
authors.affiliation: University of Geneva, Department of Cell Physiology and Metabolism, Centre Médical Universitaire, 1. Rue Michel-Servet, 1211 Geneva 4, Switzerland. Bernhard.Wehrle-Haller@unige.ch
authors.forename: Bernhard
authors.initials: B
authors.lastname: Wehrle-Haller
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D002448:Cell Adhesion; D003593:Cytoplasm / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism; D022001:Focal Adhesions / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D016023:Integrins / Q000378:metabolism; D015398:Signal Transduction; D016608:Talin / Q000378:metabolism
chemical_list: D000199:Actins; D016023:Integrins; D016608:Talin