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J Biol Chem, Vol. 274, Issue 9, 5522-5531, February 26, 1999
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From the A 95-kDa protein in Xenopus oocytes,
Xp95, was shown to be phosphorylated from the first through the second
meiotic divisions during progesterone-induced oocyte maturation. Xp95
was purified and cloned. The Xp95 protein sequence exhibited homology
to mouse Rhophilin, budding yeast Bro1, and Aspergillus
PalA, all of which are implicated in signal transduction. It also
contained three conserved features including seven conserved tyrosines,
a phosphorylation consensus sequence for the Src family of tyrosine
kinases, and a proline-rich domain near the C terminus that contains
multiple SH3 domain-binding motifs. We showed the following: 1) that
both Xp95 isolated from Xenopus oocytes and a synthetic
peptide containing the Src phosphorylation consensus sequence of Xp95
were phosphorylated in vitro by Src kinase and to a lesser
extent by Fyn kinase; 2) Xp95 from Xenopus oocytes or eggs
was recognized by an anti-phosphotyrosine antibody, and the relative
abundance of tyrosine-phosphorylated Xp95 increased during oocyte
maturation; and 3) microinjection of deregulated Src mRNA into
Xenopus oocytes increased the abundance of
tyrosine-phosphorylated Xp95. These results suggest that Xp95 is an
element in a tyrosine kinase signaling pathway that may be involved in
progesterone-induced Xenopus oocyte maturation.
Departments of Clinical
Investigation, § Molecular Genetics, and ¶ Experimental
Radiation Oncology, Department of Pharmacology,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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