title: Formin' cables under stress.
abstract: How application of force affects actin remodelling during mechanotransduction has remained unclear. Mechanical manipulation of the cell cortex is now shown to trigger actin monomer release from filaments, which in turn activates formin-dependent actin filament elongation. This force-sensitive actin polymerization does not require GTPases or membrane receptors, but it involves actin itself.
authors.affiliation: Department of Chemical and Biomolecular Engineering, Department of Chemistry, University of Illinois, 600 South Mathews Avenue, Urbana, Illinois 61801, USA. Leckband@illinois.edu
authors.forename: Deborah
authors.initials: D
authors.lastname: Leckband
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism*; D000199:Actins / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D005326:Fetal Proteins / Q000378:metabolism*; D000080865:Formins; D006801:Humans; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D008840:Microfilament Proteins / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D020741:rho GTP-Binding Proteins / Q000378:metabolism*
chemical_list: D000199:Actins; D002352:Carrier Proteins; C491464:Diap1 protein, mouse; D005326:Fetal Proteins; D000080865:Formins; D008840:Microfilament Proteins; D009687:Nuclear Proteins; D020741:rho GTP-Binding Proteins
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