title: Talin: an emerging focal point of adhesion dynamics.
abstract: The adhesion protein talin and the phosphoinositide PIP2 are emerging as key modulators of adhesion dynamics. Recent genetic studies on talin demonstrate its physiological role in organizing adhesions, stabilizing integrin-actin linkages and mediating integrin signaling in vivo. Biophysical force measurements provide further evidence that it is required for the reinforcement of the extracellular matrix-integrin-actin connection. Knockdown data along with structural analyses establish a major role for talin in 'inside-out' integrin activation through its direct interaction with integrin cytoplasmic domains. A recently uncovered role for talin is the recruitment of a PIPKI gamma isoform to adhesions. This introduces a novel connection between talin and PIP2 generation. Finally, PIP2 also stimulates the transient, direct binding interaction of the Arp2/3 complex with vinculin and thus may couple adhesion to actin assembly.
authors.affiliation: Department of Cell Biology, UVa School of Medicine, 1300 Jefferson Park Ave, PO Box 800732, Charlottesville, VA 22908-0732, USA.
authors.forename: Anjana
authors.initials: A
authors.lastname: Nayal
authors.forename: Donna J
authors.initials: DJ
authors.lastname: Webb
authors.forename: Alan F
authors.initials: AF
authors.lastname: Horwitz
mesh_terms: D000818:Animals; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D002465:Cell Movement; D016023:Integrins / Q000378:metabolism; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000096:biosynthesis; D016608:Talin / Q000502:physiology*
chemical_list: D015815:Cell Adhesion Molecules; D016023:Integrins; D019269:Phosphatidylinositol 4,5-Diphosphate; D016608:Talin