Faculty Research 1990 - 1999

SPIN, a substrate in the MAP kinase pathway in mouse oocytes.

Document Type

Article

Publication Date

1998

Keywords

adenine, Ca(2+)-Calmodulin-Dependent-Protein-Kinase, Cell-Cycle-Proteins Cycloheximide, Enzyme-Inhibitors, Mice, Mice-Inbred-C57BL, Mitotic-Spindle-Apparatus, Mutagenesis, Okadaic-Acid, Oocytes, Phosphoproteins, Protein-Processing-Post-Translational, Protein-Synthesis-Inhibitors, Protein-Serine-Threonine-Kinases, Proto-Oncogene-Proteins-c-mos, Substrate-Specificity

First Page

240

Last Page

249

JAX Source

Mol Reprod Dev 1998 Jun;50(2):240-9

Grant

CA62392/CA/NCI, CA37225/CA/NCI, HD35352/HD/NICHD

Abstract

The newly cloned gene Spin encodes a 30-kDa protein, a well-defined abundant molecule found in mouse oocytes and early embryos. This protein SPIN undergoes metaphase-specific phosphorylation and binds to the spindle. To understand the role of SPIN in oocyte meiosis, oocytes were treated with drugs that affect the cell cycle by activating or inactivating specific kinases. The posttranslational modification of SPIN in the treated oocytes was then investigated by one- and two-dimensional gel electrophoresis. Modification of SPIN is inhibited by treatment with 6-dimethylaminopurine (DMAP), suggesting that SPIN is phosphorylated by a serine-threonine kinase. Furthermore, SPIN from cycloheximide-treated oocytes that lack detectable MAP kinase activity is only partially phosphorylated, indicating that SPIN may be phosphorylated by the MOS/MAP kinase pathway. To confirm this observation, SPIN was analyzed in Mos-null mutant mice lacking MAP kinase activity. Normal posttranslational modification of SPIN did not occur in Mos-null mutant oocytes. In addition, there is reduced association of SPIN with the metaphase I spindle in Mos-null mutant oocytes, as determined by immunohistochemical analysis. These findings suggest that SPIN is a substrate in the MOS/ MAP kinase pathway and further that this phosphorylation of SPIN may be essential for its interaction with the spindle.

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