RN-tre specifically binds to the SH3 domain of eps8 with high affinity and confers growth advantage to NIH3T3 upon carboxy-terminal truncation

Broňa Matòšková, William T. Wong, Nobuo Nomura, Keith C. Robbins, Pier Paolo Di Fiore

Research output: Contribution to journalArticle

Abstract

We isolated a cDNA encoding a protein, RN-tre, which shows homology to the N-terminus of the tre oncogene product and has SH3-binding ability as well as an evolutionarily conserved domain, termed TrH, with protein-binding ability in vitro. In the present study, we identify the product of the RN-tre gene as a 97-100 kDa protein. We demonstrate stable association in vivo and in vitro between RN-tre and eps8, mediated by the SH3 domain of the latter. In vitro, RN-tre displayed remarkable preference for binding to the eps8-SH3, as compared to eight other SH3s. The Kd for the in vitro interaction between RN-tre and eps8-SH3 was between 10-8 and 10-7 M. A role for RN-tre in cell proliferation was suggested by the finding that a C-terminal truncated mutant was able to confer proliferative advantage and reduced serum-requirement to NIH3T3 fibroblasts. Finally, comparison of the structure and biological activities of RN-tre and of the tre oncogene product, provided insight into the mechanism of oncogenic activation of tre.

Original languageEnglish
Pages (from-to)2679-2688
Number of pages10
JournalOncogene
Volume12
Issue number12
Publication statusPublished - 1996

Keywords

  • eps8
  • SH3
  • Signal transduction
  • tre

ASJC Scopus subject areas

  • Cancer Research
  • Genetics
  • Molecular Biology

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