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First published online December 31, 2008
doi: 10.1242/10.1242/jcs.036467

Journal of Cell Science 122, 243-255 (2009)
Published by The Company of Biologists 2009
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Research Article

EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility

Tohru Yamazaki*, Junko Masuda*, Tsutomu Omori, Ryosuke Usui, Hitomi Akiyama and Yoshiro Maru{ddagger}

Department of Pharmacology, Tokyo Women's Medical University, 8-1 Kawada-cho, Shinjuku-ku, Tokyo 162-8666, Japan

{ddagger} Author for correspondence (e-mail: ymaru{at}research.twmu.ac.jp)

Accepted 7 October 2008

The Eph-ephrin receptor-ligand system is implicated in cell behavior and morphology. EphA1 is the founding member of the Eph receptors, but little is known about its function. Here, we show that activation of EphA1 kinase inhibits cell spreading and migration in a RhoA-ROCK-dependent manner. We also describe a novel interaction between EphA1 and integrin-linked kinase (ILK), a mediator of interactions between integrin and the actin cytoskeleton. The C-terminal sterile {alpha} motif (SAM) domain of EphA1 is required and the ankyrin region of ILK is sufficient for the interaction between EphA1 and ILK. The interaction is independent of EphA1 kinase activity but dependent on stimulation of the EphA1 ligand ephrin-A1. Activation of EphA1 kinase resulted in a decrease of ILK activity. Finally, we demonstrated that expression of a kinase-active form of ILK (S343D) rescued the EphA1-mediated spreading defect, and attenuated RhoA activation. These results suggest that EphA1 regulates cell morphology and motility through the ILK-RhoA-ROCK pathway.

Key words: EphA1, ILK, Ephrin-A1, Migration


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