Article ID Journal Published Year Pages File Type
1936254 Biochemical and Biophysical Research Communications 2007 5 Pages PDF
Abstract

N-WASP (Neural Wiskott Aldrich Syndrome Protein) regulates actin polymerization by activating the Arp2/3 complex and promotes the formation of actin-rich structures such as filopodia. Such actin-rich structures play critical roles in cell adhesion and cell motility. Analysis of the adhesion properties of N-WASP+/+ and N-WASP−/− mouse embryonic fibroblasts to extracellular matrix proteins revealed that N-WASP is critical for cell adhesion to fibronectin. There was no significant difference in the localization of paxillin in the two cell lines, however the vinculin patches in WASP+/+ cells were thicker and more prominent than those in N-WASP−/− cells. The β1 integrins in N-WASP+/+ cells were found in large clusters, while β1 integrins were more dispersed in N-WASP−/− cells. The N-WASP−/− cells migrated more rapidly than N-WASP+/+ cells in a scratch migration assay. Thus, our data suggest that N-WASP deficiency leads to reduced adhesion to fibronectin and increased cell motility.

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