The ezrin-like family of tyrosine kinase substrates: Receptor-specific pattern of tyrosine phosphorylation and relationship to malignant transformation

F. Fazioli, W. T. Wong, S. J. Ullrich, K. Sakaguchi, E. Appella, P. P. Di Fiore

Research output: Contribution to journalArticle

Abstract

A method for the isolation of tyrosine kinases substrates was developed. The method takes advantage of immuno-affinity purification of an entire set of proteins phosphorylated by tyrosine kinases, followed by generation of antisera against the purified protein pool and immunological screening of bacterial expression libraries with these antisera. By applying this methodology to the study of the phosphorylation events triggered by activation of the epidermal growth factor receptors, we have isolated several cDNAs encoding novel putative tyrosine kinase substrates. One of these cDNAs encodes radixin, a protein belonging to the band 4.1 family of proteins and highly related to ezrin and moesin. We demonstrated that, despite a high degree of relatedness, these three proteins exhibit a distinct receptor-specific pattern of phosphorylation, raising the possibility that they might mediate receptor-specific cellular changes. In addition the generation of antibodies specific for either radixin, ezrin or moesin allowed us to show that a previously described tumor transplantation antigen is indeed ezrin, thus implicating this protein in the determination of the biological phenotype of certain tumors.

Original languageEnglish
Pages (from-to)1335-1345
Number of pages11
JournalOncogene
Volume8
Issue number5
Publication statusPublished - 1993

ASJC Scopus subject areas

  • Cancer Research
  • Genetics
  • Molecular Biology

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