Abstract
The ability of cells to control the internal dynamics of actin filaments plays a crucial role in many cellular processes, including cell motility and cell division. We demonstrate that spontaneous fragmentation is the crucial process in the comparably slow steady state dynamics of in vitro actin filaments. Yet, in vivo, actin turn-over is enhanced by many different regulator proteins. Simultanously, cells need mechanisms to locally stabilize actin filaments against induced depolymerisation in order to maintain certain actin structures for longer times. Using biochemical and fluorescence microscopy techniques we demonstrate that employment of cross-linking and bundling proteins not only gives cells a powerful tool to govern the architecture of cytoskeletal systems, but also allows for a drastic stabilization against internal kinetics by suppressing disassembly of cytoskeletal filaments. Even the actin depolymerizing factors are not sufficient to disintegrate highly cross-linked actin networks unless molecular motors are used simultaneously.View Large Image | View Hi-Res Image | Download PowerPoint Slide
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