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XB-ART-16783
Biochem Biophys Res Commun 1997 Mar 06;2321:218-22. doi: 10.1006/bbrc.1997.6259.
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cDNA cloning of a novel B subunit of Xenopus protein phosphatase 2A and its biological activity in oocytes.

Iwashita J , Shima H , Nagao M , Sagata N .


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We have cloned a cDNA encoding a novel B regulatory subunit of protein phosphatase 2A (PP2A) from a Xenopus oocyte cDNA library. The novel B subunit, termed B beta', shows the strongest overall sequence similarity to, but a distinct N-terminal sequence from, the beta isoform of the human/rat B subunit. When expressed ectopically in Xenopus oocytes, the B beta' isoform can augment the endogenous PP2A activity and inhibit oocyte maturation induced by progesterone. These results suggest that the B beta' isoform can form a complex with other PP2A subunits to make a trimeric PP2A holoenzyme in Xenopus oocytes and may negatively control the initiation of oocyte maturation.

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Species referenced: Xenopus
Genes referenced: ptpa