Isolation of LERK-5: A ligand of the eph-related receptor tyrosine kinases

Douglas Pat Cerretti, Tim Vanden Bos, Nicole Nelson, Carl J. Kozlosky, Pranhitha Reddy, Eugene Maraskovsky, Linda S. Park, Stewart D. Lyman, Neal G. Copeland, Debra J. Gilbert, Nancy A. Jenkins, Frederich A. Fletcher

Research output: Contribution to journalArticlepeer-review

50 Scopus citations


Hek and elk are members of the eph-related family of receptor tyrosine kinases. Recently we isolated four cDNAs encoding membrane-bound ligands to hek and elk [Beckmann et al. (1994) EMBO J. 13, 3757-3762; Kozlosky et al. (1995) Oncogene 10, 299-306]. Because of the promiscuous nature of their binding, we have termed these proteins ligands of the eph-related kinases or LERKs. A search of GenBank revealed an expressed sequence tag (EST) with homololgy to the LERKs. Using this EST as a probe, we have isolated human and murine cDNAs that encode a protein which we call LERK-5. The human and murine cDNAs encode proteins of 333 and 336 amino acids, respectively, with a 97% amino acid identity; LERK-5 has an amino acid identity of 27-59% with the other reported LERKs. LERK-5 is a ligand for both elk and hek and induces receptor phosphorylation. It is expressed in adult lung and kidney and the fetal tissues heart, lung, kidney, and brain. In addition, Southern blot analysis of DNA from interspecific backcross mice indicated that LERK-5 (Eplg5) maps to the proximal region of mouse chromosome 8.

Original languageEnglish (US)
Pages (from-to)1197-1205
Number of pages9
JournalMolecular Immunology
Issue number16
StatePublished - Nov 1995


  • eph-family
  • ligand
  • receptor tyrosine kinase

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology


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