ERK2-binding domain is required for phosphorylation of EBITEIN1, a potential downstream interactor of ERK2

Biochem Biophys Res Commun. 2008 Oct 24;375(3):367-71. doi: 10.1016/j.bbrc.2008.08.005. Epub 2008 Aug 26.


EBITEIN1 is a recently identified extracellular signal-regulated kinase 2 (ERK2)-binding protein that is abundant in round spermatids. Here, I further characterized EBITEIN1. EBITEIN1 bound to nonphosphorylated and phosphorylated forms of ERK1 and ERK2. Phosphorylation and dephosphorylation experiments indicated that EBITEIN1 is usually phosphorylated in vivo and that it is a substrate of ERK2. The ERK2-binding domain was required for phosphorylation of EBITEIN1. Based on these results, I propose that EBITEIN1 is a phosphoprotein and a downstream interactor of ERK2 that participates in the intracellular signal transduction pathway mediating the morphogenetic development of round spermatids into spermatozoa.

MeSH terms

  • Animals
  • COS Cells
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Chlorocebus aethiops
  • Male
  • Mice
  • Mitogen-Activated Protein Kinase 1 / metabolism*
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Structure, Tertiary / genetics
  • Spermatids / metabolism*
  • Spermatogenesis


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