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- W2655146467 endingPage "2479" @default.
- W2655146467 startingPage "2463" @default.
- W2655146467 abstract "Cells can control actin polymerization by nucleating new filaments or elongating existing ones. We recently identified CRMP-1 as a factor that stimulates the formation of Listeria monocytogenes actin comet tails, thereby implicating it in actin assembly. We now show that CRMP-1 is a major contributor to actin assembly in epithelial cells, where it works with the Ena/VASP family member EVL to assemble the actin cytoskeleton in the apical cortex and in protruding lamellipodia. CRMP-1 and EVL bind to one another and together accelerate actin filament barbed-end elongation. CRMP-1 also stimulates actin assembly in the presence of VASP and Mena in vitro, but CRMP-1-dependent actin assembly in MDCK cells is EVL specific. Our results identify CRMP-1 as a novel regulator of actin filament elongation and reveal a surprisingly important role for CRMP-1, EVL, and actin polymerization in maintaining the structural integrity of epithelial sheets." @default.
- W2655146467 created "2017-06-30" @default.
- W2655146467 creator A5026216808 @default.
- W2655146467 creator A5079974679 @default.
- W2655146467 creator A5085397028 @default.
- W2655146467 date "2017-06-19" @default.
- W2655146467 modified "2023-09-24" @default.
- W2655146467 title "CRMP-1 enhances EVL-mediated actin elongation to build lamellipodia and the actin cortex" @default.
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