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Eph Receptors and Ephrin Ligands in Axon Guidance

This chapter appears in the following book:

Axon Growth and Guidance

Edited by: Dominique Bagnard
ISBN: 978-0-387-76714-7
» Get more information about this book at landesbioscience.com «

Chapter authors:
Michael Reber, Robert Hindges and Greg Lemke


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The Eph tyrosine kinase receptors (a receptor family named for the expression of Eph in an erythropoietin-producing human hepatocellular carcinoma cell line) make up the largest family of receptor tyrosine kinases. In vertebrates, 14 Eph receptor members have been identified, divided in two sub-groups, the EphAs (EphA1 to A8) and EphBs (EphB1 to B6). Their 9 membrane-bound ligands, the ephrins, are also subdivided into the ephrin-As (ephrin-A1 to A6) and ephrin-Bs (ephrin-B1 to B3). The first Eph receptor (EphA1) was identified in 1987, whereas the ephrin ligands were cloned in the mid-90s. Eph receptors and ephrins have been found in all animal species analyzed so far, from C. elegans to humans, and are highly conserved through evolution. Ephs and ephrins are involved in numerous developmental processes, such as boundary formation, angiogenesis and cell migration. Within the nervous system, Eph signaling regulates the migration pattern of neural crest cells, the boundary formation between hindbrain segments (rhombomeres), the proper formation of the corticospinal tract, the establishment of neural topographic maps and the formation and functional properties of neuronal synapses. It is therefore not surprising that nature built a complicated and detailed network of proteins interacting with each other to fine tune each of these important processes. The identity of the receptor or ligand molecule is as important as the structure of the receptor-ligand complex to activate a specific signaling pathway and ultimately elicit the right cell decision.

Michael Reber
INSERM U.575, Centre de Neurochimie

Robert Hindges

Greg Lemke

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