cDNA cloning and characterization of a Cek7 receptor protein-tyrosine kinase ligand that is identical to the ligand (ELF-1) for the Mek-4 and Sek receptor protein-tyrosine kinases

H. Shao, L. Lou, A. Pandey, Michael Verderame, D. A. Siever, V. M. Dixit

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

We have isolated a murine cDNA encoding a ligand for the Cek7 receptor protein-tyrosine kinase (RPTK), a member of the Eph/Eck RPTK subfamily. Sequence analysis predicts an open reading frame of 209 amino acids with a predicted molecular mass of 24 kDa. The Cek7 ligand shows a 48% sequence identity at the protein level to B61, a ligand for the related Eck RPTK, 30% to the Cek5 ligand, 59% to the recently cloned Ehk1-L, and identity to ELF- 1, a recently described ligand for the Mek4 and Sek RPTKs. The expressed Cek7 ligand is functionally active as it induces autophosphorylation of the Cek7 RPTK.

Original languageEnglish (US)
Pages (from-to)3467-3470
Number of pages4
JournalJournal of Biological Chemistry
Volume270
Issue number8
DOIs
StatePublished - Jan 1 1995

Fingerprint

Ephrin-A2
Cloning
Receptor Protein-Tyrosine Kinases
Organism Cloning
Complementary DNA
Ligands
Ephrin-A1
Ephrin-B1
EphA1 Receptor
Protein-Tyrosine Kinases
Open Reading Frames
Sequence Analysis
Molecular mass
Amino Acids
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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title = "cDNA cloning and characterization of a Cek7 receptor protein-tyrosine kinase ligand that is identical to the ligand (ELF-1) for the Mek-4 and Sek receptor protein-tyrosine kinases",
abstract = "We have isolated a murine cDNA encoding a ligand for the Cek7 receptor protein-tyrosine kinase (RPTK), a member of the Eph/Eck RPTK subfamily. Sequence analysis predicts an open reading frame of 209 amino acids with a predicted molecular mass of 24 kDa. The Cek7 ligand shows a 48{\%} sequence identity at the protein level to B61, a ligand for the related Eck RPTK, 30{\%} to the Cek5 ligand, 59{\%} to the recently cloned Ehk1-L, and identity to ELF- 1, a recently described ligand for the Mek4 and Sek RPTKs. The expressed Cek7 ligand is functionally active as it induces autophosphorylation of the Cek7 RPTK.",
author = "H. Shao and L. Lou and A. Pandey and Michael Verderame and Siever, {D. A.} and Dixit, {V. M.}",
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cDNA cloning and characterization of a Cek7 receptor protein-tyrosine kinase ligand that is identical to the ligand (ELF-1) for the Mek-4 and Sek receptor protein-tyrosine kinases. / Shao, H.; Lou, L.; Pandey, A.; Verderame, Michael; Siever, D. A.; Dixit, V. M.

In: Journal of Biological Chemistry, Vol. 270, No. 8, 01.01.1995, p. 3467-3470.

Research output: Contribution to journalArticle

TY - JOUR

T1 - cDNA cloning and characterization of a Cek7 receptor protein-tyrosine kinase ligand that is identical to the ligand (ELF-1) for the Mek-4 and Sek receptor protein-tyrosine kinases

AU - Shao, H.

AU - Lou, L.

AU - Pandey, A.

AU - Verderame, Michael

AU - Siever, D. A.

AU - Dixit, V. M.

PY - 1995/1/1

Y1 - 1995/1/1

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AB - We have isolated a murine cDNA encoding a ligand for the Cek7 receptor protein-tyrosine kinase (RPTK), a member of the Eph/Eck RPTK subfamily. Sequence analysis predicts an open reading frame of 209 amino acids with a predicted molecular mass of 24 kDa. The Cek7 ligand shows a 48% sequence identity at the protein level to B61, a ligand for the related Eck RPTK, 30% to the Cek5 ligand, 59% to the recently cloned Ehk1-L, and identity to ELF- 1, a recently described ligand for the Mek4 and Sek RPTKs. The expressed Cek7 ligand is functionally active as it induces autophosphorylation of the Cek7 RPTK.

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