The Eph family of receptor tyrosine kinases, and their ephrin ligands, are important for cell positioning and morphogenesis during development. EphA4 receptor can inhibit axon outgrowth and has roles in regulating axon projections during neural development. Eph signaling pathways require both receptor kinase activity and activation of Rho-GTPase guanine nucleotide-exchange factors (GEFs). Ephexin-1 is a Dbl family GEF that may be important for regulating Rho GTPase activity downstream of EphA4/FGFR complexes. EphA4 activation leads to Src kinase phosphorylation of Tyr-87 in ephexin-1, which enhances activation of RhoA, but not Rac1 or Cdc42. In addition, ephexin-1 also binds FGFRs, and is phosphorylated at Tyr-87, as well as other tyrosine sites.
Sahin, M. et al. (2005) Neuron 46:191.
Shamah, S.M. et al. (2001) Cell 105:233.
*For more information, see UniProt Accession Q8CHT1
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Fiore, L. et al. (2019) Exp Eye Res. 178:46. (WB/ICC: chick retinal neurons)
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