Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility.
By J. Bear, T. Svitkina, M. Krause, D. Schafer, J. Loureiro, Geraldine Strasser, I. Maly, O. Chaga, J. Cooper, Gary G. Borisy and 1 more. Cell, 2002
869 citations recorded by the source corpus.
Subfields: Biomedical Engineering, Biophysics, Cell Biology
View Paper: https://www.semanticscholar.org/paper/51f835af3eef459a06448fd3ec0f8fe530e32b5f
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Citations in the corpus
- The Actin Cytoskeleton and Actin-Based Motility (2018, background): “The long filaments can be bundled by fascin to produce filopodia (Svitkina et al. 2003) or buckled under the membrane and produce ruffles (Bear et al. 2002).”
- Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration. (2003, background): “Conversely, overexpression of Ena/VASP leads to longer than normal filaments at the leading edge (Bear et al. 2002).”
- Random versus directionally persistent cell migration (2009, background): “For example, inhibition of the enabled/vasodilator-stimulated phosphoprotein (ENA/VASP) family of actin-binding proteins slows the dynamics of lamellipodia and increases the rate of migratio”
- How and why does β‐actin mRNA target? (2005, background): “Shuttling of the profilin–actin complex to polymerizing barbed ends by VASP (Bear et al., 2002) and N-WASP (Suetsugu et al., 1998) is required to antagonize capping of free barbed ends, of an actin filament preferred for polymerization, in lamellipods and to elongate filopods respectively.”
- The Growth Cone Cytoskeleton in Axon Outgrowth and Guidance (2011, background): “Ena/VASP increases filament length by interacting directly with free barbed ends and 1) binding profilin:G-actin complexes and directly transferring actin monomer from profilin to the barbed end, 2) enhancing the rate of actin polymerization, and 3) delaying termination of filament elongation by F-a”
- Mechanism of filopodia initiation by reorganization of a dendritic network (2003, background): “…and Pantaloni, 1997), enabled/vasodilator-stimulated phosphoprotein (Ena/VASP)* family proteins protect elongating barbed ends from capping (Bear et al., 2002), cortactin stabilizes branches (Weaver et al., 2001), and filamin A (Flanagan et al., 2001) and -actinin stabilize and consolidate…”
- Regulation of actin assembly associated with protrusion and adhesion in cell migration. (2008, background): “The fact that VASP localizes at the tip of filopodia (218) and causes the dissociation of capping proteins from the barbed ends (12) led the authors to propose a model in which VASP promotes filopodia extension by protecting the barbed ends of actin filaments generated by Arp2/3 from capping.”
- Filopodia: molecular architecture and cellular functions (2008, background): “Initial analyses suggested that ENA/VASP proteins promote filopodia formation by preventing capping of actin filament barbed end”
- Cytoskeletal dynamics and transport in growth cone motility and axon guidance. (2003, background): “Conversely, when the microtubule-destabilizing drug because these proteins are known to enhance actin polymerization (Bear et al., 2002; Dent and Meiri, 1998;nocodazole is locally applied to one side of the growth cone, turning to the opposite side occurs (Buck and He et al., 1997; Lanier et al.,…”
- Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity. (2002, background): “Recent cell biological studies further implicate Ena/VASP in regulating cell motility by interacting with barbed ends and shielding them from capping proteins (Bear et al. 2002).”