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

Tohru Yamazaki, Junko Masuda, Tsutomu Omori, Ryosuke Usui, Hitomi Akiyama, Yoshiro Maru

研究成果査読

88 被引用数 (Scopus)

抄録

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 α 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.

本文言語English
ページ(範囲)243-255
ページ数13
ジャーナルJournal of cell science
122
2
DOI
出版ステータスPublished - 1月 15 2009
外部発表はい

ASJC Scopus subject areas

  • 細胞生物学

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