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doi: 10.1242/10.1242/jcs.00625

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`Eph'ective signaling: forward, reverse and crosstalk

Keith K. Murai^1,* and Elena B. Pasquale^1,2,

¹ The Burnham Institute, Neurobiology Program, La Jolla, CA 92037, USA
² University of California, San Diego, Molecular Pathology Program, La Jolla, CA 92093, USA

View larger version (28K): [in a new window]   Fig. 1. Domain structure of Eph receptors and ephrins and their mode of engagement. (A) EphA and EphB receptors have a conserved domain structure (bottom). Ligands are attached to the cell membrane with a GPI (glycosylphosphatidylinositol) anchor (ephrin-A molecules) or are transmembrane proteins (ephrin-B molecules). (B) Ligand-receptor engagement induces bi-directional signaling. Both Eph receptors and ephrin-B ligands become tyrosine phosphorylated through autophosphorylation (receptors) or recruitment of a tyrosine kinase (ligand). (C) Dimerization and tetramerization interfaces of a ligand-receptor tetrameric complex.

View larger version (20K): [in a new window]   Fig. 2. Forward and reverse signals communicated downstream of the Eph-ephrin complex. Some of the known EphA—ephrin-A or EphB—ephrin-B signaling pathways are highlighted. Note that SH2 and PDZ refer to a number of identified proteins containing SH2 or PDZ domains. Grb4 is the only SH2-domain-containing protein known to bind to ephrins.