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Gene Review

Eph  -  Eph receptor tyrosine kinase

Drosophila melanogaster

Synonyms: CG1511, CT3831, DEK, Dek, Dek7, ...
 
 
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Disease relevance of Eph

  • Based on results from in situ and in vitro experiments, we hypothesize that Eph receptors and ephrins mediate axon sorting and fasciculation through repulsive axon-axon interactions [1].
 

High impact information on Eph

  • Further, several examples demonstrate that cell sorting in vivo can be driven by Eph/ephrin signalling and by the differential expression of cadherins that modulate cell adhesion and motility [2].
  • Thus, Eph/Ephrin signaling acts to guide a subset of mushroom body branches to their correct synaptic targets [3].
  • Surprisingly, and in contrast to previous results using RNA-interference techniques, embryos completely lacking Eph function show no obvious axon guidance defects [3].
  • Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase [4].
  • Eph family receptor tyrosine kinases signal axonal guidance, neuronal bundling, and angiogenesis; yet the signaling systems that couple these receptors to targeting and cell-cell assembly responses are incompletely defined [4].
 

Anatomical context of Eph

 

Associations of Eph with chemical compounds

  • En-2 regulates the expression of the ligands for Eph type tyrosine kinases in chick embryonic tectum [6].
 

Regulatory relationships of Eph

  • Recently the ligands for Eph type receptor tyrosine kinases have been shown to be expressed strongly at the caudal tectum and play a role in retinotectal map formation by repulsing the temporal retinal fibers [6].
 

Other interactions of Eph

  • Ephrin/Eph signalling is crucial for axonal pathfinding in vertebrates and invertebrates [7].
  • This suggests that the cells which express en at the early stage of tectum development acquire positional specificity as 'caudal' tectum, and these cells may later express the ligands for Eph type receptor tyrosine kinases [6].
  • Dek, for Drosophila Eph kinase, possesses all the domains characteristic of the Eph subfamily of RTKs and is equally similar in sequence to both the EphA and the EphB subclasses [8].

References

 
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