The high diversity of cytoskeletal actin structures is accomplished by myriads of actin binding proteins (ABPs). Depending on its concentration, even a single type of ABP can induce different actin microstructures. Thus, for an overall understanding of the cytoskeleton, a detailed characterization of the cross-linker's effect on structural and mechanical properties of actin networks is required for each ABP. Using confocal microscopy and macrorheology, we investigate both cross-linked and bundled actin/filamin networks and compare their microstructures as well as their viscoelastic properties in the linear and the nonlinear regime.
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