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XB-ART-29834
Dev Biol 1984 Feb 01;1012:436-45.
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The regulation of ribosomal protein S-6 phosphorylation in Xenopus oocytes: a potential role for intracellular pH.

Wasserman WJ , Houle JG .


Abstract
The intracellular pH of full-grown Xenopus oocytes increases from 7.2 to 7.6 in response to progesterone stimulation. Phosphorylation of the 40 S ribosomal protein S-6 increases six- to eightfold in these stimulated cells and this phosphorylation coincides with the intracellular alkalization. This is followed by a two- to threefold increase in the protein synthetic rate. Progesterone-treated cells cultured in choline chloride substituted Na-free medium fail to alkalize and S-6 is not phosphorylated. Weak bases, such as trimethylamine, methylamine, and procaine, artificially alkalize the cell cytoplasm and stimulate S-6 phosphorylation in medium containing or lacking sodium. The methylxanthine theophylline, suppresses S-6 phosphorylation and inhibits protein synthesis. This inhibition does not appear to involve cAMP. Rather, theophylline acidifies the oocyte cytoplasm. Thus, S-6 phosphorylation appears to be regulated by the intracellular pH of the cell. In addition, the level of protein synthesis in the oocyte seems to be correlated with the level of S-6 phosphorylation.

PubMed ID: 6692987
Article link: Dev Biol


Genes referenced: camp