The actin cytoskeleton, a network of protein-polymers, is responsible for the mechanical stability of cells. This biopolymer network is also crucial for processes that require spatial and temporal variations in the network structure such as cell migration, division and intracellular transport. The cytoskeleton therefore has to combine structural integrity and mechanical stability with the possibility of fast and efficient network reorganization and restructuring. Cells meet this challenge by using proteins to link filamentous actin (F-actin) and construct complex networks. The molecular properties of the cross-linking proteins determine to a large extent the (micro)structure, viscoelastic properties and dynamics of the resulting networks. This review focuses on the structural polymorphism that can be induced by cross-linking proteins in reconstituted F-actin networks and summarizes recent results on how the molecular properties of cross-linking proteins dictate the ensuing viscoelastic properties.