2006/02/09 by B. A. DiDonna, Alex J. Levine · 1 citation
Biochemistry, Genetics and Molecular Biology · Medicine · Physics and Astronomy · #Actin #Actin cytoskeleton #Aggregate (composite) #Anatomy #Biological system #Biology #Biophysics #Blood properties and coagulation #Cell #Cell biology #Cellular Mechanics and Interactions #Cytoskeleton #Filamin #Force Microscopy Techniques and Applications #Fragility #Genetics #Materials science #Nanotechnology #Observable #Physics #Strain (injury) #cond-mat.soft #cond-mat.stat-mech
paper · pdf · doi:10.1103/physrevlett.97.068104
4 Pages, 3 figures, Revtex4, submitted to PRL
arxiv created 2006/02/09 · openalex publication_date 2006/08/09 · arxiv updated 2009/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05
The semiflexible F-actin network of the cytoskeleton is cross-linked by a variety of proteins including filamin, which contains Ig domains that unfold under applied tension. We examine a simple filament network model cross-linked by such unfolding linkers that captures the main mechanical features of F-actin networks cross-linked by filamin proteins and show that, under sufficient strain, the network spontaneously self-organizes so that an appreciable fraction of the filamin cross-linkers are at the threshold of domain unfolding. We propose and test a mean-field model to account for this effect. We also suggest a qualitative experimental signature of this type of network reorganization under applied strain that may be observable in intracellular microrheology experiments of Crocker et al.