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• W4324142741 endingPage "890" @default.
• W4324142741 startingPage "890" @default.
• W4324142741 abstract "Filopodia are dynamic, finger-like actin-filament bundles that overcome membrane tension by forces generated through actin polymerization at their tips to allow extension of these structures a few microns beyond the cell periphery. Actin assembly of these protrusions is regulated by accessory proteins including heterodimeric capping protein (CP) or Ena/VASP actin polymerases to either terminate or promote filament growth. Accordingly, the depletion of CP in B16-F1 melanoma cells was previously shown to cause an explosive formation of filopodia. In Ena/VASP-deficient cells, CP depletion appeared to result in ruffling instead of inducing filopodia, implying that Ena/VASP proteins are absolutely essential for filopodia formation. However, this hypothesis was not yet experimentally confirmed.Here, we used B16-F1 cells and CRISPR/Cas9 technology to eliminate CP either alone or in combination with Ena/VASP or other factors residing at filopodia tips, followed by quantifications of filopodia length and number.Unexpectedly, we find massive formations of filopodia even in the absence of CP and Ena/VASP proteins. Notably, combined inactivation of Ena/VASP, unconventional myosin-X and the formin FMNL3 was required to markedly impair filopodia formation in CP-deficient cells.Taken together, our results reveal that, besides Ena/VASP proteins, numerous other factors contribute to filopodia formation." @default.
• W4324142741 created "2023-03-15" @default.
• W4324142741 creator A5000711650 @default.
• W4324142741 creator A5031255430 @default.
• W4324142741 creator A5046291484 @default.
• W4324142741 creator A5054553946 @default.
• W4324142741 creator A5066042761 @default.
• W4324142741 date "2023-03-14" @default.
• W4324142741 modified "2023-10-14" @default.
• W4324142741 title "Unleashed Actin Assembly in Capping Protein-Deficient B16-F1 Cells Enables Identification of Multiple Factors Contributing to Filopodium Formation" @default.
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