| First Author | Misra A | Year | 2007 |
| Journal | Biochem Biophys Res Commun | Volume | 364 |
| Issue | 4 | Pages | 908-12 |
| PubMed ID | 17963692 | Mgi Jnum | J:128445 |
| Mgi Id | MGI:3767123 | Doi | 10.1016/j.bbrc.2007.10.086 |
| Citation | Misra A, et al. (2007) N-WASP plays a critical role in fibroblast adhesion and spreading. Biochem Biophys Res Commun 364(4):908-12 |
| abstractText | 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 beta1 integrins in N-WASP+/+ cells were found in large clusters, while beta1 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. |
