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• W2056196988 startingPage "31274" @default.
• W2056196988 abstract "Vasodilator-stimulated phosphoprotein (VASP) is active in many filopodium-based and cytoskeleton reorganization processes. It is not fully understood how VASP directly functions in actin-based motility and how regulatory proteins affect its function. Here, we combine bead motility assay and single filament experiments. In the presence of a bundling component, actin bundles that grow from the surface of WT-VASP-coated beads induced movement of the beads. VASP promotes actin-based movement alone, in the absence of other actin nucleators. We propose that at physiological salt conditions VASP nucleation activity is too weak to promote motility and bundle formation. Rather, VASP recruits F-actin seeds from the solution and promotes their elongation. Cofilin has a crucial role in the nucleation of these F-actin seeds, notably under conditions of unfavorable spontaneous actin nucleation. We explored the role of multiple VASP variants. We found that the VASP-F-actin binding domain is required for the recruitment of F-actin seeds from the solution. We also found that the interaction of profilin-actin complexes with the VASP-proline-rich domain and the binding of the VASP-F-actin binding domain to the side of growing filaments is critical for transforming actin polymerization into motion. At the single filament level, profilin mediates both filament elongation rate and VASP anti-capping activity. Binding of profilin-actin complexes increases the polymerization efficiency by VASP but decreases its efficiency as an anti-capper; binding of free profilin creates the opposite effect. Finally, we found that an additional component such as methylcellulose or fascin is required for actin bundle formation and motility mediated by VASP. Vasodilator-stimulated phosphoprotein (VASP) is active in many filopodium-based and cytoskeleton reorganization processes. It is not fully understood how VASP directly functions in actin-based motility and how regulatory proteins affect its function. Here, we combine bead motility assay and single filament experiments. In the presence of a bundling component, actin bundles that grow from the surface of WT-VASP-coated beads induced movement of the beads. VASP promotes actin-based movement alone, in the absence of other actin nucleators. We propose that at physiological salt conditions VASP nucleation activity is too weak to promote motility and bundle formation. Rather, VASP recruits F-actin seeds from the solution and promotes their elongation. Cofilin has a crucial role in the nucleation of these F-actin seeds, notably under conditions of unfavorable spontaneous actin nucleation. We explored the role of multiple VASP variants. We found that the VASP-F-actin binding domain is required for the recruitment of F-actin seeds from the solution. We also found that the interaction of profilin-actin complexes with the VASP-proline-rich domain and the binding of the VASP-F-actin binding domain to the side of growing filaments is critical for transforming actin polymerization into motion. At the single filament level, profilin mediates both filament elongation rate and VASP anti-capping activity. Binding of profilin-actin complexes increases the polymerization efficiency by VASP but decreases its efficiency as an anti-capper; binding of free profilin creates the opposite effect. Finally, we found that an additional component such as methylcellulose or fascin is required for actin bundle formation and motility mediated by VASP." @default.
• W2056196988 created "2016-06-24" @default.
• W2056196988 creator A5002824354 @default.
• W2056196988 creator A5056367497 @default.
• W2056196988 date "2014-11-01" @default.
• W2056196988 modified "2023-10-14" @default.
• W2056196988 title "Reconstitution of Actin-based Motility by Vasodilator-stimulated Phosphoprotein (VASP) Depends on the Recruitment of F-actin Seeds from the Solution Produced by Cofilin" @default.
• W2056196988 cites W1538692246 @default.
• W2056196988 cites W1593929303 @default.
• W2056196988 cites W1967972793 @default.
• W2056196988 cites W1969289508 @default.
• W2056196988 cites W1971766102 @default.
• W2056196988 cites W1974817627 @default.
• W2056196988 cites W1975499333 @default.
• W2056196988 cites W1976745001 @default.
• W2056196988 cites W1984559046 @default.
• W2056196988 cites W1986561157 @default.
• W2056196988 cites W1987338177 @default.
• W2056196988 cites W1988256357 @default.
• W2056196988 cites W1990426574 @default.
• W2056196988 cites W1998402489 @default.
• W2056196988 cites W2001197129 @default.
• W2056196988 cites W2002577396 @default.
• W2056196988 cites W2014056363 @default.
• W2056196988 cites W2018824068 @default.
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• W2056196988 cites W2022382803 @default.
• W2056196988 cites W2025036173 @default.
• W2056196988 cites W2025462408 @default.
• W2056196988 cites W2025957398 @default.
• W2056196988 cites W2028939491 @default.
• W2056196988 cites W2029209802 @default.
• W2056196988 cites W2033150145 @default.
• W2056196988 cites W2035771357 @default.
• W2056196988 cites W2038088851 @default.
• W2056196988 cites W2043058673 @default.
• W2056196988 cites W2049584879 @default.
• W2056196988 cites W2053431375 @default.
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• W2056196988 cites W2075805773 @default.
• W2056196988 cites W2084047996 @default.
• W2056196988 cites W2088390218 @default.
• W2056196988 cites W2091295304 @default.
• W2056196988 cites W2108167818 @default.
• W2056196988 cites W2108262896 @default.
• W2056196988 cites W2119836020 @default.
• W2056196988 cites W2120446093 @default.
• W2056196988 cites W2121588102 @default.
• W2056196988 cites W2123944878 @default.
• W2056196988 cites W2126496496 @default.
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• W2056196988 doi "https://doi.org/10.1074/jbc.m114.586958" @default.
• W2056196988 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4223328" @default.
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• W2056196988 hasPublicationYear "2014" @default.
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