Fascin Function

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The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. They are a 54-58Kda protein that was originally isolated from sea urchin egg (Strongylocentrotus purpuratus) but is also found in drosophila and vertebrates including man. Fascins function in the organisation of two major forms of actin-based structures: dynamic, cortical cell protrusions and cytoplasmic microfilament bundles. Cell protrusions are extensions of the plasma membrane that are supported internally by actin-based structures that impart mechanical stiffness. The cortical structures, which include filopodia, spikes, lamellipodial ribs, oocyte microvilli and the dendrites of dendritic cells, have roles in cell-matrix adhesion, cell interactions and cell migration, whereas the cytoplasmic actin bundles appear to participate in cell architecture and intracellular movements [1]. The fascin–actin interaction is under complex regulation from the extracellular matrix, peptide factors and other actin-binding proteins.

Figure 1 Figure 1. Fig. 1: Schematic view of an actin bundle (left). ABPs such as fascin organize actin filaments in a parallel fashion. In vitro these actin/fascin bundles create a purely bundled network (right, scale bar is 10 µm).

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