Protein Family Models

This family consists of several eukaryotic fascin or singed proteins. The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. Fascins function in the organisation of two major forms of actin-based structures: dynamic, cortical cell protrusions and cytoplasmic microfilament bundles. 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 [1]. Dictyostelium hisactophilin, another actin-binding protein, is a submembranous pH sensor that signals slight changes of the H+ concentration to actin by inducing actin polymerisation and binding to microfilaments only at pH values below seven [1]. Members of this family are histidine rich, typically contain the repeated motif of HHXH [3]. [1]. 11948621. Fascins, and their roles in cell structure and function. Kureishy N, Sapountzi V, Prag S, Anilkumar N, Adams JC;. Bioessays 2002;24:350-361. [2]. 8415664. Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product. Bryan J, Edwards R, Matsudaira P, Otto J, Wulfkuhle J;. Proc Natl Acad Sci U S A 1993;90:9115-9119. [3]. 1436061. Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor. Habazettl J, Gondol D, Wiltscheck R, Otlewski J, Schleicher M, Holak TA;. Nature 1992;359:855-858. (from Pfam)

Date:

2024-10-16

fascin domain-containing protein such as fascin-1, an actin-binding protein that contains 2 major actin binding sites and is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration.

Date:

2024-09-23