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- W2104833500 abstract "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." @default.
- W2104833500 created "2016-06-24" @default.
- W2104833500 creator A5005657340 @default.
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- W2104833500 creator A5067882665 @default.
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- W2104833500 date "2009-01-15" @default.
- W2104833500 modified "2023-10-18" @default.
- W2104833500 title "EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility" @default.
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- W2104833500 doi "https://doi.org/10.1242/jcs.036467" @default.
- W2104833500 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19118217" @default.
- W2104833500 hasPublicationYear "2009" @default.
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