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• W2790038689 abstract "De novo formation of epithelial cell-cell contacts relies on actin-based protrusions as well as tightly controlled turnover of junctional actin once cells encounter each other and adhesion complexes assemble. The specific contributions of individual actin regulators on either protrusion formation or junctional actin turnover remain largely unexplored. Based on our previous findings of Formin-like 2 (FMNL2)-mediated control of junctional actin dynamics, we investigated its potential role in membrane protrusions and impact on newly forming epithelial contacts. CRISPR/Cas9-mediated loss of FMNL2 in human MCF10A cells combined with optogenetic control of Rac1 activity confirmed its critical function in the establishment of intercellular contacts. While lamellipodial protrusion rates remained unaffected, FMNL2 knockout cells were characterized by impaired filopodia formation similar to depletion of the Rho GTPase Cdc42. Silencing of Cdc42, however, failed to affect FMNL2-mediated contact formation. Hence, we propose a cell-cell contact-specific and Rac1-mediated function of FMNL2 entirely independent of Cdc42. Consistent with this, direct visualizations of native epithelial junction formation revealed a striking and specifically Rac1- and not Cdc42-dependent recruitment of FMNL2 to newly forming junctions as well as established cell-cell contacts within epithelial sheets." @default.
• W2790038689 created "2018-03-29" @default.
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• W2790038689 date "2018-03-26" @default.
• W2790038689 modified "2023-09-26" @default.
• W2790038689 title "A Rac1-FMNL2 signaling module affects cell-cell contact formation independent of Cdc42 and membrane protrusions" @default.
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• W2790038689 doi "https://doi.org/10.1371/journal.pone.0194716" @default.
• W2790038689 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5868805" @default.
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• W2790038689 hasPublicationYear "2018" @default.
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