Identification of ERK2-binding domain of EBITEIN1, a novel ERK2-binding protein

Biochim Biophys Acta. 2008 Sep;1784(9):1319-25. doi: 10.1016/j.bbapap.2008.05.015. Epub 2008 Jun 11.


We recently cloned a cDNA encoding a novel extracellular signal-regulated kinase 2 (ERK2) binding protein, EBITEIN1, by yeast two-hybrid screening. In this study, we further characterized EBITEIN1. Binding experiments using various deletion mutants identified a 40-amino acid minimal sequence for binding ERK2. Binding experiments using substitution mutants indicated the crucial role of arginine residues in this sequence. Based on empirical and bioinformatic analyses, we propose two domains in EBITEIN1. One is the minimal sequence for binding ERK2 (EB domain) and the other is the EBITEIN1 C-terminal domain (ECT domain). These results might pave the way for further empirical and bioinformatic analyses of EBITEIN1- and ERK2-mediated events.

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Computational Biology
  • In Vitro Techniques
  • Male
  • Mice
  • Mitogen-Activated Protein Kinase 1 / chemistry
  • Mitogen-Activated Protein Kinase 1 / genetics
  • Mitogen-Activated Protein Kinase 1 / metabolism*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Sequence Deletion
  • Sequence Homology, Amino Acid
  • Testis / metabolism
  • Two-Hybrid System Techniques


  • Carrier Proteins
  • Recombinant Fusion Proteins
  • ebitein1 protein, mouse
  • Mitogen-Activated Protein Kinase 1