The actin cytoskeleton, consisting of the dynamic biopolymer actin and numerous additional regulatory proteins, is essential for many cellular processes. While basic functions of many actin binding proteins have been, it is still elusive how cells regulate the actin cytoskeleton in space and time. Using reconstituted systems, it is shown here that cross-linking proteins slow down the actin kinetics, which allows to couple the structure of an actin assembly with its internal dynamics. Moreover, cross-linked actin structures can passively adapt to mechanical forces, and triggering effects such as changes in pH will affect actin structures according to the present cross-linking proteins. This suggests that cross-linkers not only provide mechanical stability but also fulfill important tasks as regulators of the cytoskeleton.
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The actin cytoskeleton, consisting of the dynamic biopolymer actin and numerous additional regulatory proteins, is essential for many cellular processes. While basic functions of many actin binding proteins have been, it is still elusive how cells regulate the actin cytoskeleton in space and time. Using reconstituted systems, it is shown here that cross-linking proteins slow down the actin kinetics, which allows to couple the structure of an actin assembly with its internal dynamics. Moreover, c...
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