Journal
CELL
Volume 105, Issue 2, Pages 233-244Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(01)00314-2
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Funding
- NCI NIH HHS [CA43855] Funding Source: Medline
- NEI NIH HHS [R01 EY11310] Funding Source: Medline
- NICHD NIH HHS [HD18655, 1K08HD01384] Funding Source: Medline
- NINDS NIH HHS [R01 NS045500, R01 NS35884, NS10070-02] Funding Source: Medline
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Eph receptors transduce short-range repulsive signals for axon guidance by modulating actin dynamics within growth cones. We report the cloning and characterization of ephexin, a novel Eph receptor-interacting protein that is a member of the Dbl family of guanine nucleotide exchange factors (GEFs) for Rho GTPases. Ephrin-A stimulation of EphA receptors modulates the activity of ephexin leading to RhoA activation, Cdc42 and Rac1 inhibition, and cell morphology changes. In addition, expression of a mutant form of ephexin in primary neurons interferes with ephrin-A-induced growth cone collapse. The association of ephexin with Eph receptors constitutes a molecular link between Eph receptors and the actin cytoskeleton and provides a novel mechanism for achieving highly localized regulation of growth cone motility.
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