Cargando…
c-Abl, Lamellipodin, and Ena/VASP Proteins Cooperate in Dorsal Ruffling of Fibroblasts and Axonal Morphogenesis
BACKGROUND: Tight regulation of cell motility is essential for many physiological processes, such as formation of a functional nervous system and wound healing. Drosophila Abl negatively regulates the actin cytoskeleton effector protein Ena during neuronal development in flies, and it has been postu...
Autores principales: | Michael, Magdalene, Vehlow, Anne, Navarro, Christel, Krause, Matthias |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Cell Press
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2946563/ https://www.ncbi.nlm.nih.gov/pubmed/20417104 http://dx.doi.org/10.1016/j.cub.2010.03.048 |
Ejemplares similares
-
Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments
por: Hansen, Scott D, et al.
Publicado: (2015) -
Lamellipodin and the Scar/WAVE complex cooperate to promote cell migration in vivo
por: Law, Ah-Lai, et al.
Publicado: (2013) -
Lamellipodin promotes invasive 3D cancer cell migration via regulated interactions with Ena/VASP and SCAR/WAVE
por: Carmona, G, et al.
Publicado: (2016) -
Ena/VASP clustering at microspike tips involves lamellipodin but not I-BAR proteins, and absolutely requires unconventional myosin-X
por: Pokrant, Thomas, et al.
Publicado: (2023) -
Initiation and disassembly of filopodia tip complexes containing VASP and lamellipodin
por: Cheng, Karen W., et al.
Publicado: (2020)