Relating microstructure to rheology of a bundled and cross-linked F-actin network in vitro.
The organization of individual actin filaments into higher-order structures is controlled by actin-binding proteins (ABPs). Although the biological significance of the ABPs is well documented, little is known about how bundling and cross-linking quantitatively affect the microstructure and mechanical properties of actin networks. Here we quantify the effect of the ABP scruin on actin networks by using imaging techniques, cosedimentation assays, multiparticle tracking, and bulk rheology. We show how the structure of the actin network is modified as the scruin concentration is varied, and we correlate these structural changes to variations in the resultant network elasticity.
Shin
J H
JH
Department of Mechanical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Gardel
M L
ML
Mahadevan
L
L
Matsudaira
P
P
Weitz
D A
DA
D008841:Actin Cytoskeleton / Q000737:chemistry* / Q000378:metabolism*; D000199:Actins / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D004548:Elasticity; D006737:Horseshoe Crabs; D008297:Male; D018613:Microscopy, Confocal; D020836:Protein Structure, Quaternary; D012212:Rheology; D013094:Spermatozoa
D000199:Actins; C083765:scruin protein, Horseshoe Crab