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Mol. Cell. Biol., Sep 1995, 4921-4929, Vol 15, No. 9
AD Bergemann, HJ Cheng, R Brambilla, R Klein and JG Flanagan
The Eph receptors are the largest known family of receptor tyrosine kinases
and are notable for distinctive expression patterns in the nervous system
and in early vertebrate development. However, all were identified as orphan
receptors, and only recently have there been descriptions of a
corresponding family of ligands. We describe here a new member of the Eph
ligand family, designated ELF-2 (Eph ligand family 2). The cDNA sequence
for mouse ELF-2 indicates that it is a transmembrane ligand. It shows
closest homology to the other known transmembrane ligand in the family,
ELK-L/LERK-2/Cek5-L, with 57% identity in the extracellular domain. There
is also striking homology in the cytoplasmic domain, including complete
identity of the last 33 amino acids, suggesting intracellular interactions.
On cell surfaces, and in a cell-free system, ELF-2 binds to three closely
related Eph family receptors, Elk, Cek10 (apparent ortholog of Sek-4 and
HEK2), and Cek5 (apparent ortholog of Nuk/Sek-3), all with dissociation
constants of approximately 1 nM. In situ hybridization of mouse embryos
shows ELF- 2 RNA expression in a segmental pattern in the hindbrain region
and the segmenting mesoderm. Comparable patterns have been described for
Eph family receptors, including Sek-4 and Nuk/Sek-3, suggesting roles for
ELF-2 in patterning these regions of the embryo.
Copyright © 1995, American Society for Microbiology
ELF-2, a new member of the Eph ligand family, is segmentally expressed in mouse embryos in the region of the hindbrain and newly forming somites
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
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