title: Job-splitting among integrins.
abstract: How different integrin receptors for the same extracellular ligand transduce distinct cellular responses is unclear. The characterization of the class-specific adhesomes of β1 and αV integrins now shows that whereas αV integrins promote unbranched actin polymerization, β1 integrins induce myosin-II-dependent contractility, and both integrin subtypes synergistically mediate rigidity sensing.
authors.forename: Ronen
authors.initials: R
authors.lastname: Zaidel-Bar
mesh_terms: D000818:Animals; D060833:Cellular Microenvironment; D005353:Fibronectins / Q000378:metabolism*; D039564:Integrin alphaV / Q000378:metabolism*; D019012:Integrin beta1 / Q000378:metabolism*; D008297:Male; D024462:Myosin Type II / Q000378:metabolism*
chemical_list: D005353:Fibronectins; D039564:Integrin alphaV; D019012:Integrin beta1; D024462:Myosin Type II