Actomyosin II interaction modulates cell cortex stability.
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.
Goldmann
Wolfgang H
WH
Zentralinstitut für Biomedizinische Technik, Friedrich-Alexander-Universität, Erlangen-Nürnberg, D-91052 Erlangen, Germany. wgoldmann@biomed.uni-erlangen.de
Cantiello
Horacio F
HF
Chasan
Bernard
B
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
D000199:Actins; D003432:Cross-Linking Reagents; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000205:Actomyosin