RN-tre identifies a family of tre-related proteins displaying a novel potential protein binding domain

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

Research output: Contribution to journalArticlepeer-review


Eps8 is a recently identified SH3-containing substrate for tyrosine kinase receptors. To understand the role of eps8 in receptor-mediated signaling, we cloned cDNAs encoding proteins that bind to its SH3 domain. One of these cDNAs predicts the synthesis of an 828 amino acid protein with homology to the N-terminal region of the tre oncogene. We designated this protein RN-tre for Related to the N-terminus of tre. RN-tre is ubiquitously expressed and maps to 10p13, a region known to be involved in translocations in various leukemias. In addition, a 10p13 monosomy syndrome, characterized by developmental alterations, has been reported. The regional homology between RN-tre and tre, which is limited to their N-terminal portion, prompted us to investigate the origin of the tre oncogene transcriptional unit. We were able to show that tre is the fusion product of a 5' genetic element, homologous to RN-tre and a 3' element, encoding a de-ubiquinating enzyme. Moreover, we identified, within the N-terminus of RN-tre and tre, a domain (named TrH, for Tre Homology), which is conserved within several proteins from yeast to mammals and has protein-binding properties in vitro.

Original languageEnglish
Pages (from-to)2563-2571
Number of pages9
Issue number12
Publication statusPublished - 1996


  • eps8
  • SH3
  • Signal transduction
  • tre

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research
  • Genetics


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