Involvement of protein-tyrosine phosphorylation and dephosphorylation in sperm-induced Xenopus egg activation

FEBS Letters
K SatoYasuo Fukami

Abstract

We have analyzed tyrosine-phosphorylated proteins in Xenopus laevis eggs before and after fertilization by immunoblotting with anti-phosphotyrosine antibody. A number of egg proteins with different subcellular distribution became tyrosine-phosphorylated or dephosphorylated within 30 min after insemination. Tyrosine kinase-specific inhibitors genistein and herbimycin A were found to inhibit sperm-induced egg activation judged by the egg cortical contraction. Surprisingly, sodium orthovanadate, a tyrosine phosphatase inhibitor, also inhibited the egg activation. Moreover, we found that fertilization-dependent tyrosine dephosphorylation of 42-kDa mitogen-activated protein kinase was inhibited in genistein-treated eggs. These results suggest that both protein-tyrosine phosphorylation and dephosphorylation pathways play an important role in the sperm-induced Xenopus egg activation.

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Jun 26, 2001·Molecular Reproduction and Development·R J BeltonK R Foltz
Jul 19, 2005·Biochemical and Biophysical Research Communications·Fabiana Geraci, Giovanni Giudice
Jun 30, 2000·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·K SatoY Fukami
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