Cytoskeletal polymer networks: the molecular structure of cross-linkers determines macroscopic properties.
In living cells the mechanical properties of the actin cytoskeleton are defined by the local activation of different actin cross-linking proteins. These proteins consist of actin-binding domains that are separated and geometrically organized by different numbers of rod domains. The detailed molecular structure of the cross-linking molecules determines the structural and mechanical properties of actin networks in vivo. In this study, we systematically investigate the impact of the length of the spacing unit between two actin-binding domains on in vitro actin networks. Such synthetic cross-linkers reveal that the shorter the constructs are, the greater the elastic modulus changes in the linear response regime. Because the same binding domains are used in all constructs, only the differences in the number of rod domains determine their mechanical effectiveness. Structural rearrangements of the networks show that bundling propensity is highest for the shortest construct. The nonlinear mechanical response is affected by the molecular structure of the cross-linker molecules, and the observed critical strains and fracture stress increase proportional to the length of the spacing unit.
Wagner
B
B
Lehrstühle für Biophysik E22 and Organische Chemie und Biochemie, Technische Universität München, 80333 Munich, Germany.
Tharmann
R
R
Haase
I
I
Fischer
M
M
Bausch
A R
AR
D000199:Actins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D000818:Animals; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D003599:Cytoskeleton / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D004548:Elasticity; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011108:Polymers / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011817:Rabbits
D000199:Actins; D003598:Cytoskeletal Proteins; D011108:Polymers