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MBC in Press, published online ahead of print November 12, 2008
Mol. Biol. Cell 10.1091/mbc.E08-06-0662

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Submitted on July 1, 2008
Revised on October 3, 2008
Accepted on October 31, 2008

FGF Receptor-Induced Phosphorylation of EphrinB1 Modulates its Interaction with Dishevelled

Hyun-Shik Lee, Kathleen Mood, Gopala Battu, Yon Ju Ji, Arvinder Singh, and Ira O. Daar

Laboratory of Cell and Developmental Signaling, National Cancer Institute-Frederick, Frederick, MD 21702

Monitoring Editor: Marcos Gonzalez-Gaitan

The Eph family of receptor tyrosine kinases and their membrane-bound ligands, the ephrins, have been implicated in regulating cell adhesion and migration during development by mediating cell-to-cell signaling events. The transmembrane ephrinB1 protein is a bidirectional signaling molecule that signals through its cytoplasmic domain to promote cellular movements into the eye field, whereas activation of the fibroblast growth factor receptor (FGFR) represses these movements and retinal fate. In Xenopus embryos, ephrinB1 plays a role in retinal progenitor cell movement into the eye field through an interaction with the scaffold protein Dishevelled (Dsh). However, the mechanism by which the FGFR may regulate this cell movement is unknown. Here we present evidence that FGFR-induced repression of retinal fate is dependent upon phosphorylation within the intracellular domain of ephrinB1. We demonstrate that phosphorylation of tyrosines 324 and 325 disrupts the ephrinB1/Dsh interaction, thus modulating retinal progenitor movement that is dependent on the planar cell polarity (PCP) pathway. These results provide mechanistic insight into how FGF signaling modulates ephrinB1 control of retinal progenitor movement within the eye field.

Address correspondence to: Ira O. Daar (daar{at}ncifcrf.gov)






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