title: Actomyosin II interaction modulates cell cortex stability.
abstract: Myosin II controls the viscoelastic behavior of actin filaments, interacting with actin in an energy-dependent manner. Replacing adenosine triphosphate with adenosine diphosphate changes actomyosin sliding to cross-linking. Rheological measurements show a 3-4-fold increase of the elastic portion G' in actin filaments when myosin II is present at a molar ratio r(MA)=1:200. This observation is supported by the demonstration of inactive myosin heads along actin filaments using atomic force microscopy.
authors.affiliation: Zentralinstitut für Biomedizinische Technik, Friedrich-Alexander-Universität, Erlangen-Nürnberg, D-91052 Erlangen, Germany. wgoldmann@biomed.uni-erlangen.de
authors.forename: Wolfgang H
authors.initials: WH
authors.lastname: Goldmann
authors.forename: Horacio F
authors.initials: HF
authors.lastname: Cantiello
authors.forename: Bernard
authors.initials: B
authors.lastname: Chasan
mesh_terms: D000199:Actins / Q000378:metabolism* / Q000648:ultrastructure*; D000205:Actomyosin / Q000378:metabolism* / Q000648:ultrastructure*; D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000378:metabolism; D018625:Microscopy, Atomic Force
chemical_list: D000199:Actins; D003432:Cross-Linking Reagents; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000205:Actomyosin