Actomyosin sliding is attenuated in contractile biomimetic cortices.
Myosin II motors embedded within the actin cortex generate contractile forces to modulate cell shape in essential behaviors, including polarization, migration, and division. In sarcomeres, myosin II-mediated sliding of antiparallel F-actin is tightly coupled to myofibril contraction. By contrast, cortical F-actin is highly disordered in polarity, orientation, and length. How the disordered nature of the actin cortex affects actin and myosin movements and resultant contraction is unknown. Here we reconstitute a model cortex in vitro to monitor the relative movements of actin and myosin under conditions that promote or abrogate network contraction. In weakly contractile networks, myosin can translocate large distances across stationary F-actin. By contrast, the extent of relative actomyosin sliding is attenuated during contraction. Thus actomyosin sliding efficiently drives contraction in actomyosin networks despite the high degree of disorder. These results are consistent with the nominal degree of relative actomyosin movement observed in actomyosin assemblies in nonmuscle cells.
Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637.
Michael
M
Murrell
Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637Department of Physics and James Franck Institute, University of Chicago, Chicago, IL 60637 gardel@uchicago.edu.
Margaret L
ML
Gardel
D000199:Actins / Q000737:chemistry / Q000502:physiology / Q000648:ultrastructure; D000205:Actomyosin / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure; D000818:Animals; D030161:Avian Proteins / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure; D002645:Chickens; D008856:Microscopy, Fluorescence; D009119:Muscle Contraction; D018482:Muscle, Skeletal / Q000502:physiology; D020836:Protein Structure, Quaternary; D059008:Time-Lapse Imaging
D000199:Actins; D030161:Avian Proteins; D000205:Actomyosin