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Journal of Cell Science 115, e2401-e2401 (2002)
Copyright © 2002 The Company of Biologists Limited


In this issue

Actin' roles for Ena/VASP proteins


Research into cytoskeletal dynamics has uncovered various actin-binding proteins, including the Arp2/3 complex, the monomer-binding protein profilin, capping proteins and Ena/VASP proteins. Over the past few years, the roles of many of these have become clearer. Ena/VASP proteins, however, have been implicated in both promotion and inhibition of actin-dependent processes. On p. 4721, Frank Gertler and co-workers discuss work that could resolve this apparent paradox, arguing that differences between whole cell behaviour and that of cell parts can account for previous contradictory findings. Studies of fibroblast motility, for example, indicate that Ena/VASP proteins bind to the free barbed ends of actin filaments in the distal tips of lamellipodia/filopodia, where they antagonize capping proteins that inhibit filament elongation. Ena/VASP proteins may thus promote lamellipodial extension but reduce overall motility, since the lamellipodia generated are unbranched and less stable. Interestingly, `anticapping' is not the only function of Ena/VASP proteins: studies of Listeria motility show it requires their profilin-binding activity instead. An additional function of these proteins might therefore be to recruit profilin and thereby provide a supply of polymerization-competent actin monomers for filament nucleation.


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Related articles in JCS:

The Ena/VASP enigma
Matthias Krause, James E. Bear, Joseph J. Loureiro, and Frank B. Gertler
JCS 2002 115: 4721-4726. [Abstract] [Full Text]  




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