Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain

Jose L. Perez, Xueyu Shen, Scott Finkernagel, Leonard Sciorra, Nancy A. Jenkins, Debra J. Gilbert, Neal G. Copeland, Tai Wai Wong

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

We have cloned a novel receptor tyrosine kinase that has an unusual ectodomain. The extracellular sequence consists of 416 amino acids and has none of the structural motifs that have been found in other receptor tyrosine kinases. The 150 amino acids in the amino terminus of the receptor is homologous to a putative phospholipid-binding sequence that is found also in other cell adhesion molecules such as the neuronal AS antigen and coagulation factors V and VIII. The kinase domain has a short cytoplasmic tail and contains a short insert between subdomains I and II. The structure of this receptor kinase suggests that it belongs to a new family of receptors involved in cell-cell interactions. The cell adhesion kinase (Cak) is expressed at low levels in most adult tissues and expression is highest in the brain and lung. Using fluorescence in situ hybridization and interspecific backcross mapping, the Cak gene was localized to human chromosome 6 and mouse chromosome 17.

Original languageEnglish (US)
Pages (from-to)211-219
Number of pages9
JournalOncogene
Volume9
Issue number1
StatePublished - Jan 1 1994

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research

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