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

@article{Miura2008ERK2bindingDI,
  title={ERK2-binding domain is required for phosphorylation of EBITEIN1, a potential downstream interactor of ERK2.},
  author={Kenji Miura},
  journal={Biochemical and biophysical research communications},
  year={2008},
  volume={375 3},
  pages={
          367-71
        }
}
  • K. Miura
  • Published 24 October 2008
  • Biology, Medicine
  • Biochemical and biophysical research communications
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… Expand
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