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

作者：Miura Kenji^*

来源：Biochemical and Biophysical Research Communications, 2008, 375(3): 367-371.

DOI：10.1016/j.bbrc.2008.08.005

• EBITEIN
• EB domain
• protein-protein interaction
• binding protein
• binding domain
• phosphorylation
• electrophoretic mobility
• testis
• ERK2
• spermatogenesis

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 ERIO 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.

• 出版日期2008-10-24