Fascin is an actin filament bundling protein localized to lamellipodia and filopodia where it has important roles in cell motility. Regulation of fascin occurs through PKC-mediated phosphorylation of Ser-39 in the F-actin binding site. Cell permeant peptides that block PKC phosphorylation of Ser-39 increase cell migration, while peptides that block fascin binding to F-actin alter lamellipodial morphology and cause aberrant cell motility. Studies using RNA interference of fascin show that fibroblasts have reduced number and abnormal morphology of filopodia, while Ser-39 phosphorylation status may determine filopodial frequency. In Drosophila neurons, fascin deficiency causes alterations in actin filaments and leads to abnormal morphology of developing neurons. Thus, fascin is a critical element of actin-based motility in various cell types.
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*For more information, see UniProt Accession Q16658
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Bulek, K et al. (2019) J Immunol. 202(5):1540. (WB: mouse smooth muscle)
Rodriques, PC et al. (2017) Oncotarget. 8(43):74736. (WB: oral squamous cell carcinoma)
Kliewe, F. et al. (2017) Sci Rep. 7(1):9916. (WB: mouse podocytes)
Saad, A. et al. (2016) Sci Rep. 6:36699. (WB,IP,ICC,IHC: Breast Cancer cells/tissue)
Van Audenhove, I. (2014) FASEB Journal 28(4): 1805. (WB: human prostate PC-3)
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