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Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation.

Authors: Winslow, JW  Moran, P  Valverde, J  Shih, A  Yuan, JQ  Wong, SC  Tsai, SP  Goddard, A  Henzel, WJ  Hefti, F 
Citation: Winslow JW, etal., Neuron 1995 May;14(5):973-81.
Pubmed: (View Article at PubMed) PMID:7748564

REK7 is an Eph-related tyrosine kinase receptor expressed exclusively in the nervous system, predominantly in hippocampus and cortex. A soluble REK7-IgG fusion protein, produced to analyze the biological role of REK7, prevents axon bundling in cocultures of cortical neurons with astrocytes, a model of late stage nervous system development and differentiation. Using REK7-IgG as an affinity reagent, we purified and cloned a novel REK7 ligand called AL-1, a GPI-linked protein homologous to other members of an emerging ligand family. Membrane attachment of AL-1 appears necessary for receptor activation, since REK7 on cortical neurons is efficiently activated by transfected cells expressing GPI-linked AL-1, but not by soluble AL-1. Consistent with this, soluble AL-1 blocks axon bundling. Our findings, together with the observation that both molecules are expressed in the brain, suggest a role in the formation of neuronal pathways, a crucial feature of nervous system development and regeneration.


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CRRD Object Information
CRRD ID: 728210
Created: 2003-11-12
Species: All species
Last Modified: 2004-05-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.