ERK2-binding domain is required for phosphorylation of EBITEIN1, a potential downstream interactor of ERK2.
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.
Miura
Kenji
K
Department of Developmental Anatomy and Regenerative Biology, National Defense Medical College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, Japan.
D000818:Animals; D019556:COS Cells; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D002522:Chlorocebus aethiops; D008297:Male; D051379:Mice; D019950:Mitogen-Activated Protein Kinase 1 / Q000378:metabolism*; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D017434:Protein Structure, Tertiary / Q000235:genetics; D013087:Spermatids / Q000378:metabolism*; D013091:Spermatogenesis
D002352:Carrier Proteins; D010750:Phosphoproteins; C527469:ebitein1 protein, mouse; D019950:Mitogen-Activated Protein Kinase 1