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First published online January 27, 2006

Journal of Cell Science 119, 303e (2006)
© The Company of Biologists Limited
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In this issue

SWAP meet for actin


Figure 1

The actin cytoskeleton is remodelled during many cellular processes. Yasuhisa Fukui and colleagues have been studying membrane ruffling, a form of actin remodelling induced by growth factors. They now report that the binding of SWAP-70 - a guanine-nucleotide exchange factor that regulates the activity of the small GTPase Rac - to non-muscle actin is required for membrane ruffling (see p. 500). In co-sedimentation experiments, the authors show that the C-terminal region of SWAP-70 binds directly to non-muscle actin but not to muscle actin. In vivo, a truncated mutant of SWAP-70 containing only the C-terminal region colocalizes with actin but full-length SWAP-70 only colocalizes with actin after growth-factor stimulation; this suggests that it must be activated before it can bind to actin. Finally, the authors show that the actin-binding activity of SWAP-70 is required for growth-factor-induced membrane ruffling and for ruffling induced by constitutively active Rac. Thus, they suggest, SWAP-70 and activated Rac cooperate to induce the actin rearrangements that cause membrane ruffling.


Related articles in JCS:

Direct binding of SWAP-70 to non-muscle actin is required for membrane ruffling
Sayoko Ihara, Tsutomu Oka, and Yasuhisa Fukui
JCS 2006 119: 500-507. [Abstract] [Full Text]  




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