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- W892015695 abstract "Proc Amer Assoc Cancer Res, Volume 47, 20061810 Changes in the actin cytoskeleton are mediated by a variety of actin-binding proteins and are essential for many cellular processes, including migration, invasion, and adhesion. Cortactin is an F-actin binding protein and Src family kinase substrate that is enriched in lamellipodia and is required for tumor cell motility and invasion. Cortactin functions to stimulate Arp2/3-mediated actin polymerization necessary for lamellipodia formation and extension, and serves to stabilize Arp2/3-F-actin networks. In this study we have investigated the role of cortactin in lamellipodia dynamics using MTLn3 breast adenocarcinoma cells, a model system for studying lamellipodia. Lamellipodia formation in MTLn3 cells stimulated with EGF was monitored using time-lapse video microscopy. MTLn3 cells expressing control siRNA displayed normal lamellipodial dynamics, with maximal extension at about 3-4 minutes, and retraction by 10 minutes. In contrast, MTLn3 cells transfected with cortactin siRNA exhibited normal lamellipodia extension, but were dramatically impaired in their ability to retract, resulting in increased lamellipod persistence. Rescue of cortactin-silenced cells by expression of GFP-tagged human cortactin partially restored the ability of these cells to retract the lamellae. Our data suggest that cortactin serves to regulate lamellipodia retraction, an essential requirement for productive cell motility. The role of cortactin tyrosine phosphorylation on lamellipodia dynamics and the impact of cortactin on the architecture of the lamellipodia actin cytoskeleton are currently under investigation." @default.
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- W892015695 date "2006-04-15" @default.
- W892015695 modified "2023-09-28" @default.
- W892015695 title "Cortactin is required for lamellipodia retraction in MTLn3 Breast Cancer Cells" @default.
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