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© The Rockefeller University Press, 0021-9525/2002/3/879 $5.00
The Journal of Cell Biology, Volume 156, Number 5, March 4, 2002 879-892

Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension

¹ The Salk Institute, La Jolla, CA 92037
² Division of Biology and the Cancer Center, University of California at San Diego, La Jolla, CA 92093

Address correspondence to Pamela J. Woodring, The Salk Institute, 10010 North Torrey Pines Rd., La Jolla, CA 92037-1099. Tel.: (858) 453-4100. Fax: (858) 457-4765. E-mail: woodring{at}salk.edu

The nonreceptor tyrosine kinase encoded by the c-Abl gene has the unique feature of an F-actin binding domain (FABD). Purified c-Abl tyrosine kinase is inhibited by F-actin, and this inhibition can be relieved through mutation of its FABD. The c-Abl kinase is activated by physiological signals that also regulate the actin cytoskeleton. We show here that c-Abl stimulated the formation of actin microspikes in fibroblasts spreading on fibronectin. This function of c-Abl is dependent on kinase activity and is not shared by c-Src tyrosine kinase. The Abl-dependent F-actin microspikes occurred under conditions where the Rho-family GTPases were inhibited. The FABD-mutated c-Abl, which is active in detached fibroblasts, stimulated F-actin microspikes independent of cell attachment. Moreover, FABD-mutated c-Abl stimulated the formation of F-actin branches in neurites of rat embryonic cortical neurons. The reciprocal regulation between F-actin and the c-Abl tyrosine kinase may provide a self-limiting mechanism in the control of actin cytoskeleton dynamics.

Key Words: Abl-/- Arg-/- fibroblasts; latrunculin; STI571; fibronectin cell spreading; F-actin microspikes

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